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4. Multivariate Analysis of RNA Chemistry Marks Uncovers Epitranscriptomics-Based Biomarker Signature for Adult Diffuse Glioma Diagnostics

Author

Relier, S., primary, Amalric, A., additional, Attina, A., additional, Koumare, I.B., additional, Rigau, V., additional, Burel Vandenbos, F., additional, Fontaine, D., additional, Baroncini, M., additional, Hugnot, J.P., additional, Duffau, H., additional, Bauchet, L., additional, Hirtz, C., additional, Rivals, E., additional, and David, A., additional

Published
2022
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11. Tau protein in cerebrospinal fluid: a novel biomarker of the time of death?

Author

Peyron, PA, Hirtz, C, Baccino, E, Ginestet, N, Tiers, L, Martinez, AY, Lehmann, S, and Delaby, C

Subjects
Cerebrospinal fluid, Phosphorylated tau, Post-mortem interval, Tau protein, Biochemistry, Forensic pathology
Abstract

Background Tau proteins are recognized biomarkers of neurodegeneration and neuronal damage in the cerebrospinal fluid (CSF). It has also been suggested that these CSF proteins could increase post-mortem due to neuronal death. The aim of this study was to investigate the changes in CSF total and phosphorylated tau (p-tau) levels in the early post-mortem interval (PMI), to determine whether these proteins could be relevant biomarkers of time since death. Methods Tau and p-tau levels were measured by ELISA in lumbar and cisternal CSF samples from 82 corpses (46 men, 36 women, mean age: 72.4 +/- 15.2 years) with a PMI < 12 h. Forty-eight of them were considered neurologically healthy at the time of death. Rectal and tympanic temperatures were also measured in 37 individuals, and two validated temperature-based methods of PMI estimation were applied (Henssge's nomogram and Baccino's method). Results CSF tau and p-tau levels were significantly increased, with respective median values of 3315 pg/mL and 68.5 pg/mL in the whole cohort, while lower but still increased levels were observed in neurologically healthy patients. Sub-occipital punctures systematically provided higher tau and p-tau values (p < 0.0001). Despite a great inter-individual variability, the concentrations of both biomarkers were positively correlated with the early PMI, with the highest correlation for cisternal p-tau (r = 0.50, p < 0.0001 in the whole cohort; r = 0.58, p = 0.0003 in the neurologically healthy patients). Higher levels of CSF biomarkers were observed for PMI > 6 h versus PMI 6 h), with a Se of 83% and a Sp of 100% (AUC = 0.95). Conclusion Our findings suggest that CSF tau and p-tau proteins could serve as potential biomarkers of time since death, in association with tympanic temperature. The practical applicability of such an integrated approach has to be assessed by further studies.

Published
2021

12. Analytical comparison of ELISA and mass spectrometry for quantification of serum hepcidin in critically ill patients

Author

Delaby, C, Vialaret, J, Hirtz, C, Lefebvre, T, Herkert, M, Puy, H, Lasocki, S, and Lehmann, S

Subjects
ELISA, hepcidin, anemia, mass spectrometry
Abstract

Aim: To compare methods of quantifying serum hepcidin (based on MS and ELISA) and their ability to diagnose true iron deficiency anemia in critically ill patients. Materials & methods: Serum hepcidin was measured in 119 critically ill patients included in the HEPCIDANE clinical trial, using either an ultra-sensitive ELISA kit (from DRG) or two different MS methods. Results: The results show a good correlation between the different methods studied. The Bland-Altman analysis and the Kappa test for clinical groups show a good or very good agreement between the different tests. Conclusion: ELISA or MS show a satisfactory commutability to quantify serum hepcidin. This is of great importance for the determination of therapeutic strategies in iron deficiency.

Published
2021

13. Cytokines as new biomarkers of skin wound vitality

Author

Peyron, PA, Colomb, S, Becas, D, Adriansen, A, Gauchotte, G, Tiers, L, Marin, G, Lehmann, S, Baccino, E, Delaby, C, and Hirtz, C

Subjects
Immunoassay, integumentary system, Wound, Cytokines, Vitality, Immunohistochemistry, Forensic pathology
Abstract

Background The diagnosis of skin wound vitality is currently based on standard histology, but histological findings lack sensitivity in case of a short survival time. New reliable biomarkers of vitality are therefore strongly needed. We assessed the ability of 10 candidate cytokines (IFN-gamma, IL-1 beta, IL-2, IL-4, IL-6, IL-8, IL-10, IL-12p70, IL-13, TNF-alpha) to discriminate between vital and early post-mortem wounds. Methods Twenty-four cadavers with a recent open skin wound (< 3 h) were included (20 men, 4 women, mean age = 51.0 +/- 24.3 years). An early post-mortem wound was performed in an uninjured skin area, and both wounds were sampled at the autopsy (post-mortem interval (PMI) = 66.3 +/- 28.3 h). Needle-puncture sites related to resuscitation cares were included as very early post-mortem wounds (n = 6). In addition to standard histology, cytokines levels were simultaneously measured in each sample using a multiplex sandwich immunoassay, then normalized on healthy skin levels. A quantitative evaluation of IL-8-positive cells in ante- and post-mortem wound samples was also performed. Results In the training set of samples (n = 72), cytokine levels were significantly higher in vital wounds (mean age = 47 +/- 53 min) than in post-mortem wounds (mean PMI = 6.9 +/- 9.0 h) (p < 0.2), except for two cytokines (IFN-gamma and IL-2). IL-8 was the best discriminatory cytokine (Se = 54%, Sp = 100%, AUC = 0.79), while a multivariate model combining IL-4 and IL12p70 was a bit more discriminant (Se = 55%, Sp = 100%, AUC = 0.84). In the validation set (n = 72), the discriminatory power of the cytokines and the predictive model was slightly lower, with IL-8 remaining the best cytokine (Se = 46%, Sp = 96%, AUC = 0.75). The predictive model remained highly specific (Sp = 100%). Both the cytokines and the predictive model allowed the iatrogenic injuries to be correctly classified as post-mortem wounds. Standard histology and immunohistochemistry showed 21% sensitivity and a specificity of 79% and 100%, respectively. Only two iatrogenic wounds could be properly categorized histologically. Conclusion This study suggests that cytokines could be useful biomarkers of skin wound vitality and that the immunoassay method could be more sensitive than immunohistochemistry to identify wounds with a short survival time. Further research is underway to confirm these preliminary data.

Published
2021

14. Detection of amyloid beta peptides in body fluids for the diagnosis of alzheimer's disease: Where do we stand?

Author

Veerabhadrappa, B, Delaby, C, Hirtz, C, Vialaret, J, Alcolea, D, Lleo, A, Fortea, J, Santosh, MS, Choubey, S, and Lehmann, S

Subjects
saliva, Amyloid peptides, diagnosis, blood, Alzheimer disease, cerebrospinal fluid
Abstract

Alzheimer's disease (AD) is an incurable neurodegenerative disease characterized by progressive decline of cognitive abilities. Amyloid beta peptides (A beta), Tau proteins and the phosphorylated form of the Tau protein, p-Tau, are the core pathological biomarkers of the disease, and their detection for the diagnosis of patients is progressively being implemented. However, to date, their quantification is mostly performed on cerebrospinal fluid (CSF), the collection of which requires an invasive lumbar puncture. Early diagnosis has been shown to be important for disease-modifying treatment, which is currently in development, to limit the progression of the disease. Nevertheless, the diagnosis is often delayed to the point where the disease has already progressed, and the tools currently available do not allow for a systematic follow-up of patients. Thus, the search for a molecular signature of AD in a body fluid such as blood or saliva that can be collected in a minimally invasive way offers hope. A number of methods have been developed for the quantification of core biomarkers, especially in easily accessible fluids such as the blood, that improve their accuracy, specificity and sensitivity. This review summarizes and compares these approaches, focusing in particular on their use for A beta detection, the earliest biomarker to be modified in the course of AD. The review also discusses biomarker quantification in CSF, blood and saliva and their clinical applications.

Published
2020

18. Plasma and CSF biomarkers for the diagnosis of Alzheimer's disease in adults with Down syndrome: a cross-sectional study

Author

Fortea J., Carmona-Iragui M., Benejam B., Fernández S., Videla L., Barroeta I., Alcolea D., Pegueroles J., Muñoz L., Belbin O., de Leon M.J., Maceski A.M., Hirtz C., Clarimón J., Videla S., Delaby C., Lehmann S., Blesa R., and Lleó A.

Subjects
Adult, Male, Down syndrome, Prodromal Symptoms, tau Proteins, prodromal symptom, Comorbidity, tau protein, Article, cerebrospinal fluid, blood, Alzheimer Disease, Neurofilament Proteins, middle aged, cross-sectional study, lumbar puncture, Humans, neurofilament protein, controlled study, human, neurofilament protein L, cerebrospinal fluid analysis, Amyloid beta-Peptides, biological marker, major clinical study, enzyme linked immunosorbent assay, protein phosphorylation, female, Cross-Sectional Studies, priority journal, amyloid beta protein, dementia
Abstract

Background: Diagnosis of Alzheimer's disease in Down syndrome is challenging because of the absence of validated diagnostic biomarkers. We investigated the diagnostic performance of plasma and CSF biomarkers in this population. Methods: We did a cross-sectional study of adults aged 18 years and older with Down syndrome enrolled in a population-based health plan in Catalonia, Spain. Every person with Down syndrome assessed in the health plan was eligible to enter the Down Alzheimer Barcelona Neuroimaging Initiative, and those with a plasma or CSF sample available were included in this study. Participants underwent neurological and neuropsychological examination and blood sampling, and a subset underwent a lumbar puncture. Adults with Down syndrome were classified into asymptomatic, prodromal Alzheimer's disease, or Alzheimer's disease dementia groups by investigators masked to biomarker data. Non-trisomic controls were a convenience sample of young (23–58 years) healthy people from the Sant Pau Initiative on Neurodegeneration. Amyloid-ß (Aß) 1–40 , Aß 1–42 , total tau (t-tau), 181-phosphorylated tau (p-tau; only in CSF), and neurofilament light protein (NfL) concentrations were measured in plasma with a single molecule array assay and in CSF with ELISA. Plasma and CSF biomarker concentrations were compared between controls and the Down syndrome clinical groups. Diagnostic performance was assessed with receiver operating characteristic curve analyses between asymptomatic participants and those with prodromal Alzheimer's disease and between asymptomatic participants and those with Alzheimer's disease dementia. Findings: Between Feb 1, 2013, and Nov 30, 2017, we collected plasma from 282 participants with Down syndrome (194 asymptomatic, 39 prodromal Alzheimer's disease, 49 Alzheimer's disease dementia) and 67 controls; CSF data were available from 94 participants (54, 18, and 22, respectively) and all 67 controls. The diagnostic performance of plasma biomarkers was poor (area under the curve [AUC] between 0·53 [95% CI 0·44–0·62] and 0·74 [0·66–0·82]) except for plasma NfL concentrations, which had an AUC of 0·88 (0·82–0·93) for the differentiation of the asymptomatic group versus the prodromal Alzheimer's disease group and 0·95 (0·92–0·98) for the asymptomatic group versus the Alzheimer's disease dementia group. In CSF, except for Aß 1–40 concentrations (AUC 0·60, 95% CI 0·45–0·75), all biomarkers had a good performance in the asymptomatic versus prodromal Alzheimer's disease comparison: AUC 0·92 (95% CI 0·85–0·99) for Aß 1–42 , 0·81 (0·69–0·94) for t-tau, 0·80 (0·67–0·93) for p-tau, and 0·88 (0·79–0·96) for NfL. Performance of the CSF biomarkers was optimal in the asymptomatic versus Alzheimer's disease dementia comparison (AUC =0·90 for all except Aß 1–40 [0·59, 0·45–0·72]). Only NfL concentrations showed a strong correlation between plasma and CSF biomarker concentrations in participants with Down syndrome (rho=0·80; p

Published
2018

21. Towards a routine application of Top-Down approaches for label-free discovery workflows

Author

Schmit, P.O., Vialaret, J., Wessels, H.J., Gool, A.J. van, Lehmann, S., Gabelle, A., Wood, J., Bern, M., Paape, R., Suckau, D., Kruppa, G., Hirtz, C., Schmit, P.O., Vialaret, J., Wessels, H.J., Gool, A.J. van, Lehmann, S., Gabelle, A., Wood, J., Bern, M., Paape, R., Suckau, D., Kruppa, G., and Hirtz, C.

Abstract

Item does not contain fulltext

Published
2018

22. Serum neurofilament light chain at time of diagnosis is an independent prognostic factor of survival in amyotrophic lateral sclerosis.

Author

Thouvenot, E., Demattei, C., Lehmann, S., Maceski‐Maleska, A., Hirtz, C., Juntas‐Morales, R., Pageot, N., Esselin, F., Alphandéry, S., Vincent, T., and Camu, W.

Subjects
AMYOTROPHIC lateral sclerosis, CYTOPLASMIC filaments, MONOCLONAL gammopathies, WEIGHT loss, SINGLE molecules, SERUM
Abstract

Background and purpose: The prognostic value of serum neurofilament light chain (sNfL), a biomarker of neurodegeneration, compared to other prognostic factors of amyotrophic lateral sclerosis (ALS) at the time of diagnosis, remains unclear. Methods: Sera from ALS patients were prospectively collected at the first diagnostic visit in our centre. sNfL levels were determined by single molecule array in 207 ALS patients and in 21 healthy controls. The prognostic value of sNfL was compared with that of other known clinical prognostic factors using a Cox regression model and multivariate analysis. Results: Serum neurofilament light chain levels were higher in ALS patients than in controls (P < 0.0001). Seven parameters were predictive of death in ALS: older age, bulbar onset, higher ALS Functional Rating Scale revised (ALSFRS‐R) score, greater weight loss, lower maximal inspiratory pressure, forced vital capacity and higher sNfL levels. A Cox regression model showed that sNfL (P < 0.0001), weight loss (P = 0.040) and site at onset (P = 0.048) were independent predictive factors of death. In a sub‐cohort restricted to 139 patients with complete spirometry data, sNfL level (P < 0.005) and forced vital capacity (P = 0.022) were independent factors predictive of death. In a subgroup of 142 patients in whom ALSFRS‐R score was available at several time points, sNfL levels positively correlated with ALSFRS‐R rate of decline (r = 0.571, P < 10−12). Conclusions: Higher sNfL concentration is a strong and independent prognostic factor of death in ALS as early as the time of diagnosis. [ABSTRACT FROM AUTHOR]

Published
2020
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26. Strain effect on extracellular laccase activities from <italic>Botrytis cinerea</italic>.

Author

Quijada‐Morin, N., Garcia, F., Lambert, K., Walker, A.‐S., Tiers, L., Viaud, M., Sauvage, F.‐X., Hirtz, C., and Saucier, C.

Subjects
LACCASE, BOTRYTIS cinerea, EXTRACELLULAR enzymes, FUNGAL enzymes, OXIDATION of phenols, GLYCOSYLATION
Abstract

Abstract: Background and Aims: Laccase enzymes produced by Botrytis cinerea are involved in the oxidation of phenolic substances during the development of grey mould, which causes significant economic losses. The aim of this work was to study the structural and activity characteristics of the laccase enzymes secreted by three B. cinerea strains that are involved in the development of grey mould. Methods and Results: Laccase enzymes obtained from three B. cinerea strains [one reference strain (B05.10) and two strains obtained from two French vineyards (VA612 and RM344)] were characterised. Analysis by LC‐QTOF‐MS revealed that the three strains contained a mixture of Laccase‐2‐BcLCC2 and Laccase‐3‐BcLCC7. The structural characteristics of the laccases from the three strains, such as molecular weight and glycosylation degree, were identical. Nevertheless, their catalytic activities were significantly different. Conclusions: Differences in catalytic activities could be due either to possible differences in the relative amount of Laccase‐2‐BcLCC2 and Laccase‐3‐BcLCC7 produced by each strain or to differences in the glycosidic fraction of the enzymes. Significance of the Study: The severity of the infection caused by B. cinerea may be not only related to the infection level but also to the strain involved. [ABSTRACT FROM AUTHOR]

Published
2018
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27. Complejidad del proteoma de la saliva humana

Author

Hirtz, C., Chevalier, François, Centeno, D., Egea, J., Rossignol, M., Sommerer, N., de Périère, Deville, Laboratoire de physiologie, UFR d'Odontologie, Université Montpellier 1, Université Montpellier 1 (UM1), Unité de Recherche Protéomique (PROTEOMIQUE), Institut National de la Recherche Agronomique (INRA), and Université de Montpellier (UM)

Subjects
[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2005

28. Epidermal growth factor: a probable oral and digestive health protector

Author

Égéa, J.C, Hirtz, C., Valcarcel, J, Deville De Périère, D., Unité d’Endocrinologie et de Physiologie Orofaciale, Faculté d'odontologie [Montpellier], and Université de Montpellier (UM)-Université de Montpellier (UM)

Subjects
Inflammation, Digestive mucosa, Salive, Mouth Mucosa, Epidermal growth factor, Inflammatory disease, Digestive System Physiological Phenomena, Gastric Mucosa, Neoplasms, Muqueuse digestive, Humans, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Intestinal Mucosa, Saliva, Biomarkers, Maladie inflammatoire, Facteur de croissance épidermique
Abstract

The integrity of oral and digestive mucosa depend on many salivary components like the Epidermal Growth Factor (EGF). Sometimes indicative, sometimes stimulated or modulated factor of oral and digestive health, EGF appears as a clinical marker in neoplastic and inflammatory diseases. As cellular growth factor, it protects the digestive mucosa with stimulation of mucus production and with inhibition of gastric secretion. Equally implicated in healing process, it enhances this one, and determines, in patients, more or less sensibility to inflammatory damages. Its strategic place in various pathologies, as stomach ulcer and tumoral process, open research prospects with a real potential of repair and pronostic.; L'intégrité des muqueuses orales et digestives est sous la dépendance d'une multitude de facteurs et constituants salivaires, parmi lesquels, le facteur de croissance épidermique (EGF) tient une place particulière et controversée suivant le niveau de ses implications dans les processus physiopathologiques. Tantôt indicateur, tantôt stimulateur ou modulateur sur la santé orodigestive, l'EGF apparaît aussi comme marqueur clinique dans les affections inflammatoires et néoplasiques. En tant que facteur de croissance cellulaire, il serait un agent protecteur des muqueuses digestives par la stimulation de la synthèse de mucus et l'inhibition de la sécrétion gastrique. Impliqué également dans les processus de cicatrisation, dont il potentialise les capacités, l'EGF conditionnerait les sujets à une plus ou moins grande sensibilité aux agressions inflammatoires. Sa place stratégique, au carrefour des pathologies aussi diverses que l'ulcère gastrique et les processus tumoraux, ouvre des perspectives de recherche sur ses réelles capacités de réparateur ou de pronostic.

Published
2002

29. The effect of environmental salinity on the proteome of the sea bass (Dicentrarchus labrax L.)

Author

Ky, Chin Long, De Lorgeril, Julien, Hirtz, C, Sommerer, N, Rossignol, M, Bonhomme, F, Ky, Chin Long, De Lorgeril, Julien, Hirtz, C, Sommerer, N, Rossignol, M, and Bonhomme, F

Abstract

The European sea bass, Dicentrarchus labrax L., tolerates a range of salinities from freshwater to hyper-saline. To study differences in protein expression, fish were reared in both freshwater and seawater. After 3-month acclimation, gill and intestine epithelia were collected and the soluble protein extracted. In all, 362 spots were differentially expressed in the gills and intestines of fishes reared in seawater compared to those from freshwater. Fifty differential protein spots were excised from a colloidal Coomassie-stained gel. Nine separate protein spots were identified unambiguously by mass spectrometry and database searching. Among the six proteins over-expressed in gill cells in seawater, five were cytoskeleton proteins and one was the aromatase cytochrome P450. In gill cells under freshwater conditions, the two over-expressed proteins identified were the prolactin receptor and the major histocompatibility complex class II beta-antigen. In intestinal cells under freshwater conditions, the Iroquois homeobox protein Ziro5 was upregulated over ninefold. The expression of these proteins, their possible direct or indirect roles in the adaptation of D. labrax to salinity, and their correspondences with a previous study are discussed.

Published
2007
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31. ENDOMETRIOSIS, ENDOMETRIUM, IMPLANTATION AND FALLOPIAN TUBE

Author

Nesbitt-Hawes, E., primary, Campbell, N., additional, Won, H., additional, Maley, P., additional, Henry, A., additional, Abbott, J., additional, Potdar, N., additional, Mason-Birks, S., additional, Elson, C. J., additional, Gelbaya, T. A., additional, Nardo, L. G., additional, Stavroulis, A., additional, Nnoaham, K., additional, Hummelshoj, L., additional, Zondervan, K., additional, Saridogan, E., additional, GSWH Consortium, W. E. R. F., additional, Chamie, L. P., additional, Soares, A. C. P., additional, Kimati, C. T., additional, Gomes, C., additional, Fettback, P., additional, Riboldi, M., additional, Serafini, P., additional, Lalitkumar, S., additional, Menezes, J., additional, Evdokia, D., additional, Gemzell-Danielsson, K., additional, Lalitkumar, P. G. L., additional, Bailey, J., additional, Newman, T. A., additional, Johnston, A., additional, Zisimopoulou, K., additional, White, M., additional, Sadek, K., additional, Shreeve, N., additional, Macklon, N., additional, Cheong, Y., additional, Al-Akoum, M., additional, Akoum, A., additional, Giles, J., additional, Garrido, N., additional, Vidal, C., additional, Mondion, M., additional, Gallo, C., additional, Ramirez, J., additional, Pellicer, A., additional, Remohi, J., additional, Ghosh, S., additional, Chattopadhyay, R., additional, Jana, S., additional, Goswami, S. K., additional, Bose, G., additional, Chakravarty, M., additional, Chowdhuri, K., additional, Chakravarty, B. N., additional, Kendirci Ceviren, A., additional, Ozcelik Tanriverdi, N., additional, Urfan, A., additional, Donmez, L., additional, Isikoglu, M., additional, Romano, A., additional, Schreinemacher, M. H., additional, Backes, W. H., additional, Slenter, J. M., additional, Xanthoulea, S. A., additional, Delvoux, B., additional, van Winden, L., additional, Beets-Tan, R. G., additional, Evers, J. L. H., additional, Dunselman, G. A. J., additional, Jana, S. K., additional, Chaudhury, K., additional, Maruyama, T., additional, Yamasaki, A., additional, Miyazaki, K., additional, Arase, T., additional, Uchida, H., additional, Yoshimura, Y., additional, Kaser, D., additional, Ginsburg, E., additional, Missmer, S., additional, Correia, K., additional, Racowsky, C., additional, Streuli, I., additional, Chouzenoux, S., additional, de Ziegler, D., additional, Chereau, C., additional, Weill, B., additional, Chapron, C., additional, Batteux, F., additional, Arianmanesh, M., additional, Fowler, P. A., additional, Al-Gubory, K. H., additional, Urata, Y., additional, Osuga, Y., additional, Izumi, G., additional, Nagai, M., additional, Takamura, M., additional, Yamamoto, N., additional, Saito, A., additional, Hasegawa, A., additional, Takemura, Y., additional, Harada, M., additional, Hirata, T., additional, Hirota, Y., additional, Yoshino, O., additional, Koga, K., additional, Taketani, Y., additional, Mohebbi, A., additional, Janan, A., additional, Nasri, S., additional, Lakpour, M. R., additional, Ramazanali, F., additional, Moini, A., additional, Aflatoonian, R., additional, Germeyer, A., additional, Novak, O., additional, Renke, T., additional, Jung, M., additional, Jackus, J., additional, Toth, B., additional, Strowitzki, T., additional, Bhattacharya, J., additional, Mitra, A., additional, Kundu, S., additional, Pal, M., additional, Kundu, A., additional, Gumusel, A., additional, Basar, M., additional, Yaprak, E., additional, Aslan, E., additional, Arda, O., additional, Ilvan, S., additional, Kayisli, U., additional, Guzel, E., additional, Haouzi, D., additional, Monzo, C., additional, Lehmann, S., additional, Hirtz, C., additional, Tiers, L., additional, Hamamah, S., additional, Choi, D., additional, Choi, J., additional, Jo, M., additional, Lee, E., additional, Shen, X., additional, Wang, B. I. N., additional, Li, X., additional, Tamura, I., additional, Maekawa, R., additional, Asada, H., additional, Tamura, H., additional, Sugino, N., additional, Liu, H., additional, Jiang, Y., additional, Chen, J., additional, Zhu, L., additional, Wang, B., additional, Yan, G., additional, Sun, H., additional, Coughlan, C., additional, Sinagra, M., additional, Ledger, W., additional, Li, T. C., additional, Laird, S. M., additional, Dafopoulos, K., additional, Vrekoussis, T., additional, Chalvatzas, N., additional, Messini, C. I., additional, Kalantaridou, S., additional, Georgoulias, P., additional, Messinis, I. E., additional, Makrigiannakis, A., additional, Xue, Q., additional, Xu, Y., additional, Zuo, W. L., additional, Zhang, L., additional, Shang, J., additional, Zhu, S. N., additional, Bulun, S. E., additional, Tomassetti, C., additional, Geysenbergh, B., additional, Meuleman, C., additional, Fieuws, S., additional, D'Hooghe, T., additional, Suginami, K., additional, Sato, Y., additional, Horie, A., additional, Matsumoto, H., additional, Fujiwara, H., additional, Konishi, I., additional, Jung, Y., additional, Cho, S., additional, Choi, Y., additional, Lee, B., additional, Seo, S., additional, Urman, B., additional, Yakin, K., additional, Oktem, O., additional, Alper, E., additional, Taskiran, C., additional, Aksoy, S., additional, Takeuchi, K., additional, Kurematsu, T., additional, Yu-ki, Y., additional, Fukumoto, Y., additional, Homan, Y., additional, Sata, Y., additional, Kuroki, Y., additional, Takeuchi, M., additional, Awata, S., additional, Muneyyirci-Delale, O., additional, Charles, C., additional, Anopa, J., additional, Osei-Tutu, N., additional, Dalloul, M., additional, Weedon, J., additional, Muney, A., additional, Stratton, P., additional, Yilmaz, B., additional, Kilic, S., additional, Aksakal, O., additional, Kelekci, S., additional, Aksoy, Y., additional, Lordlar, N., additional, Sut, N., additional, Gungor, T., additional, Chan, J., additional, Tan, C. W., additional, Lee, Y. H., additional, Tan, H. H., additional, Choolani, M., additional, Griffith, L., additional, Oldeweme, J., additional, Barcena de Arellano, M. L., additional, Reichelt, U., additional, Schneider, A., additional, Mechsner, S., additional, Munch, S., additional, Vercellino, G. F., additional, Chiantera, V., additional, Santoro, L., additional, D'Onofrio, F., additional, Campo, S., additional, Ferraro, P. M., additional, Tondi, P., additional, Gasbarrini, A., additional, Santoliquido, A., additional, Jung, M. H., additional, Kim, H. Y., additional, Arnold, J., additional, Buttner, A., additional, Karaer, A., additional, Celik, O., additional, Bay Karabulut, A., additional, Celik, E., additional, Kiran, T. R., additional, Simsek, O. Y., additional, Yilmaz, E., additional, Turkcuoglu, I., additional, Tanrikut, E., additional, Alieva, K., additional, Kulakova, E., additional, Ipatova, M., additional, Smolnikova, V., additional, and Kalinina, E., additional

Published
2012
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34. 35th Annual Meeting of the European Association for the Study of Diabetes

Author

Melander, A., Olsson, J., Lindberg, G., Salzman, A., Howard, T., Stang, P., Lydick, E., Emslie-Smith, A., Boyle, D. I. R., Evans, J. M. M., Macdonald, T. M., Bain, J., Sullivan, F., Juhl, C., Pørksen, N., Sturis, J., Hollingdal, M., Pincus, S., Veldhuis, J., Dejgaard, A., Schmitz, O., Kristensen, J. S., Frandsen, K. B., Bayer, Th., Müller, P., Dunning, B. E., Paladini, S., Gutierrez, C., Deacon, R., Valentin, M., Grunberger, G., Weston, W. M., Patwardhan, R., Rappaport, E. B., Sargeant, L. A., Wareham, N. J., Khaw, K. T., Zethelius, Björn, Lithell, Hans, Hales, C. Nicholas, Berne, Christian, Lakka, H.-M., Oksanen, L., Tuomainen, T.-P., Kontula, K., Salonen, J. T., Dekker, J. M., de Boks, P., de Vegt, F., Stehouwer, C. D. A., Nijpels, G., Bouter, L. M., Heine, R. J., Bruno, G., Cavallo-Perin, P., Bargero, G., D’Errico, N., Borra, M., Macchia, G., Pagano, G., Newton, R. W., Ruta, D. A., New, J. P., Wallace, C., Roxburgh, M. A., Young, R. J., Vaughan, N. J. A., Elliott, P., Brennan, G., Devers, M., MacAlpine, R., Steinke, D., Lawson, D. H., Decallonne, B., Casteels, K., Gysemans, C., Bouillon, R., Mathieu, C., Linn, Thomas, Strate, Christine, Schneider, Kerstin, Funda, D. P., Jirsa, M., Kozáková, H., Kaas, A., Kofronová, O., Tlaskalová-Hogenová, H., Buschard, K., Wanka, H., Hartmann, A., Kuttler, B., Rasmussen, S. B., Sørensen, T. S., Markholst, H., Petersen, J. S., Karounos, D., Dyrberg, T., Mabley, J. G., Haskó, G., Szabó, C., Seissler, J., Nguyen, T. B. T., Steinbrenner, H., Scherbaum, W. A., Cipriani, R., Gabriele, A., Sensi, M., Guidobaldi, L., Pantellini, F., Cerrito, M. G., Scarpa, S., Di Mario, U., Morano, S., Ceolotto, G., Iori, E., Baritono, E., Del Prato, S., Semplicini, A., Trevisan, R., Zerbini, G., Meregalli, G., Asnaghi, V., Tentori, F., Maestroni, A., Mangili, R., Marescotti, C., Vedovato, M., Tiengo, A., Tadjieva, J., Mankovsky, B. N., Van Aken, S., Raes, A., Vande Walle, J., Matthys, D., Craen, M., Hansen, H. P., Lund, S. S., Rossing, P., Jensen, T., Parving, H.-H., Andersen, S., Tarnow, L., Hansen, B. V., Trautner, C., Haastert, B., Ennenbach, N., Willich, S., Tabák, Á. Gy., Orchard, T. J., Spranger, J., Preissner, K. T., Schatz, H., Pfeiffer, A., Cantón, A., Burgos, R., Hernández, C., Lecube, A., Mesa, J., Segura, R. M., Mateo, C., Simó, R., Fathallah, L., Greene, D. A., Obrosova, I., Gilbert, R. E., Kelly, D. J., Cox, A. J., Berka-Wilkinson, J. L., Taylor, H. R., Panagiotopoulos, S., Lee, V., Jerums, G., Cooper, M. E., Hitman, G. A., Aganna, E., Ogunkolade, W. B., Rema, M., Deepa, R., Shanthi-Rani, C. S., Barakat, K., Kumarajeewa, T. R., Cassell, P. G., McDermott, M. F., Mohan, V., Ways, K., Bursell, S., Devries, T., Woodworth, J., Alatorre, C., King, G., Aiello, L. P., Karisen, A. E., Pavlovic, D., Nielsen, K., Jensen, J., Andersen, H. U., Pociot, F., Mandrup-Poulsen, T., Eizirik, D. L., Nerup, J., Lortz, S., Tiedge, M., Lenzen, S., Lally, F. J., Bone, A. J., Darville, M. I., Ho, Y.-S., Sternesjö, J., Sandler, S., Chen, M.-C., Schuit, F., Pipeleers, D. G., Merezak, S., Hardikar, A., Hoet, J. J., Remacle, C., Reusens, B., Bréant, B., Garofano, A., Czernichow, P., Kubota, N., Terauchi, Y., Miki, H., Tamemoto, H., Yamauchi, T., Nakano, R., Komeda, K., Eto, K., Tobe, K., Kimura, S., Kadowaki, T., Ide, T., Murakami, K., Tsunoda, M., Mochizuki, T., Ozanne, S. E., Nave, B. T., Wang, C. L., Dorling, M. W., Petry, C. J., Koopmans, S. J., van der Bent, C., Que, I., Radder, J. K., Sebokova, E., Sana, A. K., Klimes, I., Ruderman, N., Morviducci, L., Pastore, L., Morelli, S., Sagratella, E., Zorretta, D., Buongiomo, A., Tamburrano, G., Giaccari, A., Martinenghi, Sabina, De Angelis, Gabriella Cusella, Ravasi, Flavio, Bifari, Francesco, Bordignon, Claudio, Falqui, Luca, Kessler, A., Dransfeld, O., Sasson, S., Tomas, E., Zorzano, A., Eckel, J., Thorsby, P., Rosenfalck, A. M., Kjems, L., Hanssen, K. F., Madsbad, S., Birkeland, K. I., Hamilton-Wessler, M., Markussen, J., Bergman, R. N., Melki, V., Hanaire-Broutin, H., Bessières-Lacombe, S., Tauber, J.-P., Home, P. D., Lindholm, A., Riis, A., Rosenstock, J., Schwartz, S., Clark, C., Edwards, M., Donley, D., Swift, P., Mortensen, H. B., Lynggaard, H., Hougaard, P., Cull, C. A., Neil, H. A. W., Frighi, V., Manley, S. E., Holman, R. R., Turner, R. C., Steiner, G., Davis, W. A., Weeraratna, T., Bruce, D. G., Davis, T. M. E., Vergès, B., Duvillard, L., Pont, F., Florentin, E., Gambert, Ph., Benko, B., Ljubić, S., Turk, Z., Granić, M., März, W., Wollschläger, H., Klein, G., Neiss, A., Wehling, M., Huxtable, S. J., Saker, P. J., Walker, M., Frayling, T. M., Levy, J. C., O’Rahilly, S., Hattersley, A. T., McCarthy, M. I., Orecchio, A., Giacchini, A., Dominici, R., Canettieri, G., Trinti, B., Zani, M., Andreoli, M., Sciacchitano, S., de Silva, A. M., Whitecross, K., Pasco, J., Kotowicz, M., Nicholson, G., Zimmet, P., Boyko, E. J., Collier, G. R., Frittitta, L., Pizzuti, A., Argiolas, A., Graci, S., Goldfine, I. D., Bozzali, M., Ercolino, T., Costanzo, B., Iacoviello, L., Tassi, V., Trischitta, V., Wauters, M., Rankinen, T., Mertens, I., Chagnon, M., Bouchard, C., Van Gaal, L., Sivenius, K., Valve, R., Hakkarainen, V., Niskanen, L., Laakso, M., Uusitupa, M., Beridze, N., Japaridze, M., Kurashvili, R., Dundua, M., Kebuladze, G., Kazakhashvili, N., Offley-Shore, B., Thomas, B., Ghebremeskel, K., Crawford, M., Lowy, C., Eriksson, Ulf J., Martin Simán, C., Wisse, Bert, Gittenberger-de Groot, Adriana C., Wentzel, P., Eriksson, U. J., Wender-Ożegowska, E., Drews, K., Biczysko, R., Bronisz, A., Rość, D., Graczykowska-Koczorowska, A., Kotschy, M., Sokup, A., Kohnert, K. D., Besch, W., Strese, J., Frick, U., Zander, E., Kemer, W., Škrha, J., Kvasnička, J., Kalvodová, B., Hilgertová, J., Schatteman, K., Goossens, F., Scharpé, S., De Leeuw, I., Hendriks, D., Legakis, I. N., Panayiotou, D., Mountokalakis, Th. D., Enderle, M. D., Beckmann, P., Balletshofer, B., Rittig, K., Maerker, E., Volk, A., Meisner, C., Jacob, S., Matthaei, S., Häring, H. U., Rett, K., Ueda, K., Nakagawa, T., Shimajiri, Y., Kokawa, M., Matsumoto, E., Sasaki, H., Sanke, T., Nanjo, K., McKinnon, Caroline M., Macfarlane, Wendy M., Docherty, Kevin, Furukawa, N., Shirotani, T., Kishikawa, H., Kaneko, K., Araki, E., Shichiri, M., Prentki, M., Roduit, R., Susini, S., Buteau, J., Ejrnæs, A. M., Andersen, N. Aa., Osterhoff, M., Möhlig, M., Ortmann, J., Bikashaghi, F., Mayer, C., Bikashagi, F., Ackermans, M. T., Pereira Arias, A. M., Bisschop, P. H. L. T., Endert, E., Sauerwein, H. P., Romijn, J. A., Gastaldelli, A., Baldi, S., Pettiti, M., Natali, A., Frascerra, S., Camastra, S., Toschi, E., Ferrannini, E., Stingl, H., Krssak, M., Bischof, M. G., Krebs, M., Fürnsinn, C., Nowotny, P., Waldhäusl, W., Roden, M., Neeft, M., Meijer, A. J., Båvenholm, P., Pigon, J., Efendic, S., Kästenbauer, T., Sauseng, S., Sokol, G., Auinger, M., Irsigler, K., Abbott, C. A., Carrington, A. L., Faragher, B., Kulkarni, J., Van Ross, E. R. E., Boulton, A. J. M., Armstrong, D. G., Hadi, S., Nguyen, H. C., Harkless, L. B., Jirkovská, A., Kasalicky, P., Hosová, J., Skibova, J., Uccioli, L., Caselli, A., Giacomozzi, C., Macellari, V., Giurato, L., Lardieri, L., Menzinger, G., Pham, H. T., Rosenblum, B. I., Lyons, T. E., Giurini, J. M., Smakowski, P., Chrzan, J. S., Habershaw, G. M., Veves, A., Foster, A. M., Bates, M., Doxford, M., Edmonds, M. E., Kecha, O., Winkler, R., Martens, H., Collette, J., Lefèbvre, P. J., Greiner, D., Geenen, V., Atlan-Gepner, C., Naspetti, M., Valéro, R., Barad, M., Lepault, F., Vialettes, B., Naquet, P., de Galan, B., Netea, M. G., Hancu, N., Smits, P., Van der Meer, J. W. M., Osterbye, T., Jørgensen, K. H., Tranum-Jensen, J., Fredman, P., Høy, M., Bokvist, K., Olsen, H. L., Horn, T., Gromada, J., Laub, R., Lohmann, T., Hahn, H. J., Adler, T., Emmrich, F., Rabuazzo, A. M., Lupi, R., Dotta, F., Patanè, G., Marselli, L., Realacci, M., Piro, S., Del Guerra, S., Santangelo, C., Navalesi, R., Purrello, F., Marchetti, P., de Vos, P., Visser, L., de Haan, B. J., Klok, P., van Schilfgaarde, R., Poppema, S., Juang, J.-H., Kuo, C.-H., Hsu, B. R.-S., Nacher, V., Pérez, M., Biarnés, M., Raurell, M., Soler, J., Montanya, E., Ritzel, R., Maubach, J., Büsing, M., Becker, T., Klempnauer, J., Hücking, K., Schmiegel, W. H., Nauck, M. A., Bouček, P., Saudek, F., Adamec, M., Kožitarová, R., Jedináková, T., Vlasáková, Z., Skibová, J., Bartoš, V., Maffi, P., Bertuzzi, F., Aldrighetti, L., Taglietti, M. V., Castelnuovo, A., Pozza, G., Di Carlo, V., Secchi, A., Renier, G., Mamputu, J.-C., Gillespie, J. S., McMaster, D., Mercer, C., Trimble, E. R., Lecomte, M., Véricel, E., Paget, C., Ruggiero, D., Lagarde, M., Wiernsperger, N., Pricci, F., Leto, G., Amadio, L., Cordone, S., Iacobini, C., Catalano, S., Violi, F., Rotella, C. M., Pugliese, G., Zicari, A., Gradini, R., Sale, P., Pala, L., Cresci, B., Giannini, S., Manuelli, C., Dahlfors, G., Arnqvist, H. J., Gonelle-Gispert, C., Halnan, P. A., Sadoul, K., Wolter, S., Lang, J., Niwa, T., Yu, W., Hidaka, H., Senda, T., Niki, I., Fukasawa, T., Renstrom, E., Barg, S., Seward, E., Rorsman, P., Rutter, G. A., Molinete, M., Lilla, V., Ravazzola, M., Halban, P. A., Efanov, A. M., Bertorello, A. M., Zaitsev, S. V., Zwiller, J., Berggren, P.-O., MŞengül, A., Salman, F., Sargrn, M., Özer, E., Karşidaǧ, K., Salman, S., Gedik, S., Satman, İ., Dinççaǧ, N., Yılmaz, M. T., Lloyd, A., Hopkinson, P. K., Testa, M. A., Blonde, L., Turner, R. R., Hayes, J., Simonson, D. C., van der Ven, N. C. W., Lubach, C. H. C., Snoek, F. J., Mollema, E. D., van der Ploeg, H. M., Danne, T., Hoey, H., McGee, H., Fitzgerald, H., Lernmark, B., Thernlund, G., Fredin, K., Hägglöf, B., Lugari, R., Dell’Anna, C., Ugolotti, D., Dei Cas, A., Barilli, A. L., Sard, L., Marani, B., Iotti, M., Zandomeneghi, R., Gnudi, A., Kjems, L. L., Volund, Aa., Toft-Nielsen, M., Damholt, M. B., Hilsted, L., Hughes, T. E., Krarup, T., Holst, J. J., Young, A., Gottlieb, A., Fineman, M., Kolterman, O., Cancelas, J., García-Martínez, J. A., Villanueva-Peñacarrillo, M. L., Valverde, I., Malaisse, W. J., Filipsson, K., Ahrén, B., Balkan, B., Kwasnik, L., Battle, B., Li, X., Egan, J. M., Clocquet, A. R., Elahi, D., Petrella, E., Pricket, K., Petersen, K. F., Sullivan, J. T., Amatruda, J. M., Livingston, J. N., Shulman, G. I., Freyse, E.-J., Knospe, S., Glund, K., Demuth, H.-U., Walker, D., Malik, R. A., Reljanovic, M., Barada, A., Milicevic, Z., Tack, Cees J., Goldstein, David S., Van Huysen, C., Stevens, M. J., Cao, X., Sundkvist, G., Dahlin, L.-B., Eriksson, K.-F., Rosén, I., Lattimer, S. A., Sima, A. A. F., Sullivan, K., Shaw, J. E., de Courten, M. P., Zimmet, P. Z., Gourdy, P., Ruidavets, J. B., Arveiler, D., Amouyel, Ph., Bingham, A., Tauber, J. P., Lam, K. S. L., Wat, N. M. S., Lam, T. H., Janus, E. D., de Pablos, P., Rodriguez, F., Martínez, J., Sánchez, V., Santana, C., García, I., Macías, A., Levin, K., Hother-Nielsen, O., Henriksen, J. E., Beck-Nielsen, H., Brechtel, K., Machann, J., Koch, M., Nielsen, M., Löblein, K., Becker, R., Denignger, M., Renn, W., Machicao, F., Claussen, C. D., Schick, F., Diraison, F., Moulin, P., Beylot, M., Thams, P., Capito, K., Eliasson, Lena, Barg, Sebastian, Göpel, Sven, Kanno, Takahiro, Renström, Erik, Meda, P., Charollais, A., Gjnovci, A., Calabrese, A., Wonkam, A., Caton, D., Wisznievski, L., Serre, V., Cogne, F., Bauquis, J., Bosco, D., Huarte, J., Herrera, P., Gotfredsen, C. F., Vessby, B., Manuel y Keenoy, B., Engelen, W., Vertommen, J., Schrans, S., Louheranta, A., Lindström, J., Tuomilehto, J., Segal, K. R., Heymsfield, S., Hauptman, J., Boldrin, M., Lucas, C., Pandolfi, A., Cetrullo, D., Polishchuck, R., Alberta, M., Pellegrini, G., Calafiore, A., Vitacolonna, E., Capani, F., Consoli, A., Halleux, C. M., Gillot, E. F., Brichard, S. M., Van der Planken, M., Corthouts, B., Peiffer, F., Scholten, D., Walke, M., Assert, R., Pirags, V., Pedula, K. L., Hillier, T. A., Brown, J. B., Santini, S. A., Marra, G., Cotroneo, P., Manto, A., Di Leo, M. A. S., Di Gregorio, S., Tordi, A., Pitocco, D., Ruotolo, V., Ghirlanda, G., Temelkova-Kurktschiev, T., Schaper, F., Koehler, C., Henkel, E., Hanefeld, M., Mancini, L., Citterio, F., Cotroneo, A., Ceroone, S., Castagneto, M., Rajbhandari, S. M., Dent, M. T., Plater, M. E., Harris, N. D., Tesfaye, S., Ward, J. D., Dupuy, O., Mayaudon, H., Lecoules, S., Bauduceau, B., Palou, M., Farret, O., Molinié, C., Antonelli-Incalzi, R., Fuso, L., Giordano, A., Calcagni, M. L., Todaro, L., Basso, S., Tramaglino, L. M., Troncone, L., Pistelli, R., Guillot, R., Bringuier, A., Porokhov, B., Guillausseau, P. J., Feldmann, G., Zivanic, S., Cizmic, M., Dragojevic, R., Vanovic, M., Borghouts, L. B., van Kranenburg, G. P. J., Schaart, G., Keizer, H. A., Niess, A. M., Dickuth, H. H., Lutz, O., Barbe, P., Calazel-Fournier, C., Hernandez, G., Saint-Martin, F., Galitzky, J., Gonçalves, A. A., da Silva, E. C., Brito, I. J. L., da Silva, C. A., Lawrence, N. J., Kousta, E., Mulnier, H., Penny, A., Millauer, B., Johnston, D. G., Robinson, S., Perriello, G., Pimenta, W., Pampanelli, S., Lucidi, P., Lepore, M., Porcellati, F., Cordoni, M. C., De Feo, P., Bolli, G. B., Sjöstrand, M., Holmäng, A., Lönnroth, P., Hauer, B., Grauer, P., Artzner, S., Lang, R., Stumvoll, M., Monti, L. D., Piatti, P. M., Gemone, F., Valsecchi, G., Magni, M., Barbieri, E., Setola, E., Sandoli, E. P., Galli-Kienle, M., Pontiroli, A. E., Nichols, Gregory A., Brown, Jonathan B., Salzsieder, E., Boltz, H., Ramirez, J. C., Rutscher, A., Fischer, U., Koenig, Ch., Friske, M., Schramm, W., Landgraf, R., Bachmann, W., Bangemann, M., Groeneveld, G., Edvell, Anders, Lindström, Per, Tsiotra, P., Koukourava, A., Raptis, S. A., Tsigos, C., Boutou, E., Triandaffilopoulou, A., Egido, E. M., Rodríguez-Gallardo, J., Gutiérrez, E., García, P., Silvestre, R. A., Marco, J., Khan, Akhtar, Ling, Zong-Chao, Ahren, Bo, Efendic, Suad, Bünting, C., Du, X., Zhi Sui, G., Rösen, P., Koschinsky, T., Kearney, T. M., Sharp, P. S., Lapolla, A., Fedele, D., Martano, L., Garbeglio, M., Seraglia, R., Favretto, D., Traldi, P., Meerwaldt, R., Smit, A. J., Links, Th. P., v. Roon, A. M., Graaf, R., Gans, R. O. B., Deynelİ, O., Ersöz, H. Ö., Gogas, D., Fak, A. S., Akalin, S., Veglio, M., Sivieri, R., Chinaglia, A., Scaglione, L., Le, T., Wong, N., Detrano, R., Charles, M. A., Colhoun, H. M., Francis, D. P., Rubens, M., Underwood, S. R., Fuller, J. H., Knudsen, E., Sato, A., Nielsen, F. S., Bonora, E., Kiechl, S., Willeit, J., Oberhollenzer, F., Egger, G., Bonadonna, R., Muggeo, M., Festa, A., D’Agostino, R., Howard, G., Mykkänen, L., Tracy, R. P., Haffner, S. M., Poulsen, P., Vach, K., Ijzerman, R. G., Bakker, S. J. L., Truster, J., Crowther, N. J., Cameron, N., Gray, I. P., Chaillous, L., Carel, J. C., Thivolet, C., Boitard, C., Charbonnel, B., Saï, P., Decochez, K., Keymeulen, B., Somers, G., Dorchy, H., Rottiers, R., Winnock, F., ver Elst, K., Weets, I., Pipeleers, D., Gorus, F., Seebaum, S., Schumm-Draeger, P.-M., Petzoldt, R., Federlin, K., Bonnevie-Nielsen, V., Martensen, P. M., Justesen, J., Worsaa, A., Karlsson, Maria, Sederholm, Sofia, Ludvigsson, Johnny, Bélicar, P., Dale, C., Vague, Ph., Alessis, C., Lassmann-Vague, V., Bode, B. W., Gross, T. M., Ghegan, M., Steed, R. D., Davidson, P. C., Ordoñez, A., Rubio, J. L., Sulleiro, J. M., Buendía, J. P., Zamora, J., Castillo, M., Schaupp, L., Ellmerer, M., Brunner, G. A., Sendlhofer, G., Schlack, Ch., Skrabal, F., Wach, P., Pieber, T. R., Heinemann, L., Krämer, U., Klötzer, H. M., Hermann, M., Cosgrove, K. E., Chapman, J. C., Shepherd, R. M., McIntyre, S., Butler, P. C., Dunne, M. J., Brekardin, E., Dörschner, H., Schwanstecher, C., Schwanstecher, M., Uhde, I., Emmanouilidou, E., Teschemacher, A. G., Pouli, A. E., Gylfe, E., Tengholm, A., Hellman, B., Perfetti, R., Aggarwal, S., Müller, Günter, Welte, Stefan, Wied, Susanne, Valverde, A. M., Mur, C., Kahn, C. R., Benito, M., Rondinone, C. M., Peterson, T., Laviola, L., Belsanti, G., Logoluso, F., Napoli, R., Davalli, A. M., Weir, G. C., Giorgino, R., Giorgino, F., Flesch, S., Hompesch, B., Rave, K., Susanto, F., Kühn-Velten, W. N., Heise, T., Rendell, M., Dole, J., Esper, R. J., Stein, E., Lemme, L., Rubinstein, A., Maritz, F. J., Soule, S., Market, A., Chajek-Shaul, T., Maislos, M., Tal, S., Stolero, D., Josefsen, K., Beckmann, H., Petersen, C., Ekman, R., Efanova, I., Zaitsev, S., Berggren, P. O., Birkenbach, M., Holl, R. W., Rosenbauer, J., Grabert, M., Icks, A., Schwab, O., Reile, K., Janssen, M. M. J., de Jongh, R. T., Casteleijn, S., Masurel, N., Hoogma, R. P. L. M., Santeusanio, F., Brunetti, P., Fanelli, C. G., Laureti, S., Bartocci, L., Maran, A., Crepaldi, C., Trupiani, S., Macdonald, I. A., Avogaro, A., Bouman, S. D., Keitz, M., Bruggink, J. E., Scheurink, A. J. W., Strubbe, J. H., Steffens, A. B., Ferguson, S. C., McCrimmon, R. J., Perros, P., Best, J. J. K., Deary, I. J., Frier, B. M., Robinson, R. T. C. E., Ireland, N. H., Bedford, C., Fairclough, E., Hudson, S., Heller, S. R., Borch-Johnsen, K., Berger, M., Overmann, H., Bender, R., Blank, M., Sawicki, P., Jörgens, V., Mühlhauser, I., Nosadini, R., Sailer, A., Dalla Vestra, M., Brocco, E., Piarulli, F., Frigato, F., Sambataro, M., Velussi, M., Baggio, B., Fioretto, P., Jager, A., van Hinsbergh, V. W. M., Kostense, P. J., Nrjpels, G., Gæde, P., Pedersen, O., Andrysiak-Mamos, E., Majkowska, L., Krzyżanowska, B., Pilarska, K., Czekalski, S., Mazzon, C., Brocco, S., Field, L. L., Nejentsev, S., Gombos, Z., Veijola, R., Knip, M., Simell, O., Vaarala, O., Åkerblom, H. K., Ilonen, J., Krokowski, M., Bodalski, J., Andrzejewski, W., Ławnik, M., Teodorczyk, A., Heinrich, A., Caillat-Zucman, S., Buzzetti, R., Petrone, A., Mesturino, C., Giorgi, G., Fiori, R., Nisticò, L., Di Genova, G., Cascino, I., Klöting, I., Kovacs, P., McKinney, P. A., Okasha, M., Parslow, R. C., Law, G. R., Gurney, K. A., Williams, R., Bodansky, H. J., Herzig, P., Giani, G., Vervoort, G., Lutterman, J. A., Berden, J. H. M., Wetzels, J. F. 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C., Kaya, F., Süsleyici, B., Öztürk, M., Eisner, M., Guldbakke, B., Karpenko, N., Brizgalova, G., Alesina, M., Røder, M. E., Schwartz, R. S., Prigeon, R., Kahn, S. E., Kendereški, A., Micić, D., Šumarac, M., Macut, Dj., Zonć, S., Čolić, M., Cvijović, G., Gligorović, P., Courtney, C. H., Atkinson, A. B., Ennis, C., Sheridan, B., Bell, P. M., Jolly, M., Amin, R., Godsland, I., Horvoka, R., Anyaoku, V., Lawrence, N., Krasova, N., Sergienko, L., Mingrone, G., Plat, L., Balasse, E. O., Zykova, T., Jenssen, T., Strelkova, A., Zykova, S., Tipisova, E., Féry, F., Wijenaike, A. N., Watt, P. W., Jung, R. T., Bolton-Smith, C., Rennie, M. J., Ludvik, B., Aigmueller, Th., Waldhaeusl, W., Courtois, P., Bource, F., Guenat, E., Philippe, J., Jéquier, E., Tappy, L., Benny, Santosa, Grönemeyer, Dietrich, Aygen, Sitke, Scholz, Nicole, Busch, Martin, Tauveron, I., Rochon, C., Dejax, C., Benoit, P., Capitan, P., Bayle, G., Prugnaud, J., Fabricio, A., Champredon, C., Thieblot, P., Grizard, J., Nielsen, M. F., Nyholm, B., Chandramouli, V., Schumann, W. C., Landau, B. R., Rizza, R. A., Mitrakou, A., Meyer, C., Tolias, A., Platanisiotis, D., Vlachos, L., Gerich, J., Wajngot, A., Sprangers, F., Jellema, W. T., Lopuhaä, C. E., van Lieshout, J. J., van der Zee, J. S., Mithieux, G., Croset, M., Zitoun, C., Hurot, J. M., Rajas, F., Montano, S., Willem, R., Verbruggen, I., Grue-Sørensen, G., Björkling, F., Watson, N. D., Burns, S. P., Murphy, H. C., Iles, R. A., Cohen, R. D., Rooney, K., Swan, V., Phuyal, J., Millar, J., Bryson, J., Denyer, G., Caterson, I., Thompson, C., Gaster, M., Handberg, Aa., Schrøder, H. D., Alzaid, A., Sobki, S., Thye-Rønn, P., Alford, F., Christopher, M., Gras, F., Brunmair, B., Neschen, S., Py, G., Lambert, K., Raynaud, E., Mercier, J., Tsuchihashi, K., Sumida, Y., Fujimoto, H., Nakamura, M., Miyata, E., Furuta, M., Katsuki, A., Ito, K., Sasaki, R., Hori, Y., Yano, Y., Adachi, Y., Lauritz, J., Eriksson, J. W., Burén, J., Zhao, L. J., Li, Z.-C., Kullin, M., Karlsson, F. A., Redondo, A., Puente, J., Clemente, F., González, N., Moberg, E., Amer, P., Hagström-Toft, E., Bolinder, J., Björnholm, M., Krook, A., Galuska, D., Myers, M., Zierath, J. R., Wallberg-Henriksson, H., Niklasson, M., Strindberg, L., Sternberg, F., Hebeda, S., Kratzer, W., Salgado, M. I., Hoss, U., Kalatz, B., Lohmann, S., Fussgänger, R., Khomazjuk, A. I., Ncscheret, A. P., Gonchar, I. V., Quinones-Galvan, A., Sironi, A. M., Cominacini, L., Nagai, Y., Yamashita, H., Takamura, T., Kobayashi, K., Szanto, I., Peth, J. A., Kinnick, T. R., Youngblood, E. B., Tritschler, H. J., Henriksen, E. J., Gašperíková, D., Rufo, C., Teran-Garcia, M., Nakamura, M. T., Clarke, S. D., Pye, S., Zhang, Z., Radziuk, J., Guignot, L., Bell, K. S., Lim-Fraser, M., Cooney, G., Kraegen, E. W., Takayama, S., Legare, D. J., Macedo, M. P., Lautt, W. W., Bradley, B., Barron, P., Davies, J., Ader, M., Richey, J. M., Ait El Mkadem, S., Macari, F., Renard, E., Méchaly, I., Brun, J. F., Cros, G., Bringer, J., del Aguila, L. F., Krishnan, R. K., Farrell, P. A., Ulbrecht, J., Correll, P. H., Kirwan, J. P., Mei, J., Rahn-Landström, T., Brindley, D., Manganiello, V., Degerman, E., Ziv, E., Shafrir, E., Kaiman, R., Galer, S., Bar-On, H., Gerő, L., Földes, K., Janssen, J., Járay, J., Perner, F., Haap, M., Houdali, B., Schmit, M. B., Dietze, G. J., Perrini, S., Natalicchio, A., Montrone, C., de Robertis, O., De Pergola, G., Strack, V., Kellerer, M., Kausch, C., Condorelli, G., Beguinot, F., Häring, H.-U., Song, X. M., Chibalin, A. V., Ryder, J. W., Jiang, X. J., Alessi, D. R., Hennige, A. M., Metzinger, E., Seipke, G., Trüb, T., Hey, A., Sørensen, A. R., Schäffer, L., Drejer, K., Kurtzhals, P., Hansen, B. F., Matozaki, T., Noguchi, T., Yamao, T., Takada, T., Ochi, F., Takeda, H., Inagaki, K., Hosoka, T., Kasuga, M., Schürt, M., Meier, M., Drenckhan, M., Meyer, M., Aries, S. P., Klein, H. H., Telting, D., van der Zon, G. C. M., Dorrestijn, J., Maassen, J. A., Clapham, J. C., Holder, J. C., Tomlinson, K. M., Pickavance, L., Buckingham, R., Wilding, J., Jacinto, S. M., Harrold, J., Ljung, B., Kjellstedt, A., Thalén, P., Widdowson, P., Williams, G., Oakes, N., Aoki, K., Saito, T., Satoh, S., Mukasa, K., Kaneshiro, M., Kawasaki, S., Hoshino, K., Okamura, A., Sekihara, H., Smith, U., Johansson, A., Nilsson, E., Olausson, T., Nakazawa, T., Suzuki, M., Martinez, J., Murado, P., Azal, Ö., Yönem, A., Çakır, B., Polat, Z., Kutlu, M., Çorakçı, A., Bayraktar, M., Gürlek, A., Koray, Z., Damian, M. S., Linn, T., Laube, H., Arzner, S., Meißner, H.-P., Giunti, S., Comune, M., Cassader, M., Conte, M. R., Sacchi, C., Musso, G., Mecca, F., Depetris, N., Gambino, R., Perin, P. Cavallo, Kawakami, S., Sandqvist, M., Jansson, P.-A., Šindelka, G., Widimský, J., Haas, T., Prázný, M., Mari, A., Nolan, J. J., Uusitupa, M. I. J., Karşıdağ, K., Hacıhanefioğlu, B., Dinççağ, N., Drivsholm, T., Palacios, R. T., Vølund, A., Pedersen, Oluf B., Letiexhe, M. R., Scheen, A. J., Quiñones Galvan, A., Simeoni, M., Basu, A., Uosukainen, A., Mäkimattila, S., Schlenzka, A., Adler, A. I., Levy, J., Stevens, R., Matthews, D., Holman, R., Boland, B. J., Jeanjean, M., Hermans, M. P., Maudoigt, C., Tonglet, R., Robert, A., Quiñones-Galvan, A., Cini, G., Galetta, F., Sanna, G., Gernone, F., Janssen, M. J., Gonera, R. K., Wolffenbuttel, B. H. R., de Leeuw, P. W., Schaper, N. C., Molęda, P., Kuczerowski, R., Czech, A., Tatoń, J., Taddei, S., Patiag, D., Qu, X., Wilkes, M., Gray, S., Seale, J. P., Donnelly, R., Campión, J., Maestro, B., Dávila, N., Carranza, M. C., Calle, C., Hales, C. N., Fernández-Real, J. M., Grasa, M., Pugeat, M., Barret, C., Ricart, W., Lindmark, S., Olsson, T., Tufvesson, M., Loeblein, K., Mehnert, B., Haering, H. U., Rave, Klaus, Heise, Tim, Clauson, Per, Hirschberger, Sabine, Heinemann, Lutz, Claret, M., Nadal, B., Truc, A., Rossi, L., Hildebrand, P., Ketterer, S., Beglinger, C., Keller, U., Gyr, K., Parvin, S., Overkamp, D., Vayreda, M., González-Huix, F., G-Huix, F., Zavaroni, I., Gasparini, P., Massironi, P., Zuccarelli, A., Delsignore, R., Reaven, G. M., Sheu, W. H. H., Lee, W. J., Chen, Y.-T., Iraklianou, S., Tournis, S., Volonakis, I., Spylopoulou, M., Bilianou, E., Melidonis, A., Foussas, S., Güler, Serdar, çakir, Bekir, Demi̇rbaş, Berrin, Gürsoy, Gül, Serter, Rüştü, Aral, Yalçin, Morton, G., Lee, S., Fahey, R., de Silva, A., Cai, X. J., Buckingham, R. E., Arch, J. R. S., Wilson, S., Clausen, J. T., Kristensen, P., Nielsen, P. F., Wulff, B. S., Thim, L., Holness, M. J., Sugden, M. C., Fryer, L. G. D., Munns, M. J., Mannucci, E., Ognibene, A., Cremasco, F., Bardini, G., Mencucci, A., Ciani, S., Pierazzuoli, E., Tsuchihashil, K., Rigalleau, V., Delafaye, C., Baillet, L., Vergnot, V., Brunou, P., Gatta, B., Gin, H., Felber, J. P., Munger, R., Assimacopoulos, F., Bobbioni, E., Golay, A., Wilken, M., Larsen, F. S., Buckley, D., Molina, L. M., Marquez, L., Arbeo, A., Hernandez, C., Kofod, H., Damholt, A. B., Buchan, A., Márquez, L., Luque, M. A., Sarti, L., Sutton, P. J., Behle, K., Heimesaat, M. M., Hüfner, M., Gravholt, Claus Højbjerg, Mølier, Niels, Christiansen, Jens Sandahl, Schmitz, Ole, Deacon, C. F., Brock, B., Knudsen, L. B., Agersø, H., Huusfeldt, P. O., Kelly, C. M. N., Brunn, C., Schioos, J., Sewing, S., Lemansky, P., Wawro, S., Mest, H. J., Taguchi, T., Motoshima, H., Yoshizato, K., Guenifi, Amel, Henriksson, M., Johansson, J., Shafqat, J., Tally, M., Wahren, J., Jömvall, H., Ekberg, K., Rigler, R., Pramanik, A., Kratz, G., Johansson, B.-L., Uhlén, M., Jörnvall, H., Forst, T., Dufayet De La Tour, D., Kunt, T., Pfützner, A., Goitom, K., Pohlmann, T., Schneider, S., Johansson, B. L., Löbig, M., Engelbach, M., Beyer, J., Ekman, Bertil, Nyström, Fredrik, Arnqvist, Hans J., Halvatsiotis, P. G., Meek, S., Bigelow, M., Nair, K. S., Maghsoudi, S., Fisker, S., Vølund, A. A., Jörgensen, J. O. L., Christiansen, J. S., Hilsted, J., Mazerkina, N. A., Tiulpakov, A. N., Gorelyshev, S. K., Peterkova, V. A., Macut, D. J., Dieguez, C., Casanueva, F. F., Catalina, P. F., Mallo, F., Andrade, A., García-Mayor, R. V. G., Popova, V. V., ter Maaten, J. C., Popp-Snijders, C., Madsen, L., Ukropec, J., Bergene, E., Rnstan, A. C., Berge, R., Arner, P., Wahl, G., Häring, H., Bryson, J. M., Curtis, S. E., Caterson, I. D., Winzell, M. Sörhede, Svensson, H., Ahnén, B., Holm, C., Phillips, C., Madigan, C., Owens, D., Collins, P., Johnson, A., Tomkin, G. H., Cabezas, M. Castro, van Oostrom, A. J. H. H. M., Erkelens, D. W., Summers, L. K. M., Fielding, B. A., Ilic, V., Clark, M. L., Frayn, K. N., Pietzsch, J., Julius, U., Nitzsche, S., Fischer, S., Lindgren, C., Amrot-Fors, L., Hoffmann, M. M., Luft, D., Schmülling, R.-M., D’Adamo, M., Leonetti, F., Paoloni, A., Ribaudo, M. C., Basso, M. S., Elmore, U., Restuccia, A., Sbraccia, P., Emilsson, V., O’Dowd, J., Heyman, R., Cawthorne, M. A., Pelikánová, T., Kazdová, L., Žák, A., Chvojková, Š., Özer, E. M., Kadıoğlu, P., Korugan, Ü., Hatemi, H., Rivellese, A. A., Dullaart, R. P. F., Riemens, S. C., Sluiter, W. J., van Tol, A., Farnier, M., Megnien, S., Turpin, G., Stulp, B. K., Brambilla, P., Brunelli, A., Riva, M. C., Manzoni, P., de Poli, S., Riboni, S., Stolk, R. P., Meijer, R., Wink, O., Zelissen, P. M. J., van Gils, A. P. G., Grobbee, D. 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W., Taverna, M., Guerre-Millo, M., Chevalier, A., Pacher, N., Slama, G., Gorshunska, M., Buyken, A. E., Heitkamp, G., Kabir, M., Oppert, J. M., Wursch, P., Bruzzo, F., Rahman, M. H., Fatima, K., Ahmed, S., Mondal, H. N., Yilmaz, M., Öztok, U., Karakoç, A., Çakır, N., Düzgün, E., Yetkin, İ., Arslan, M., Şardaş, S., Wilding, John, Géloën, A., Baret, G., Dalmaz, Y., Peyronnet, J., Clémenceau, B., Martignat, L., Lalain, S., Gouin, E., Kenda-Ropson, N., Miller, A. O. A., You, S., Aguilera, E., Recasens, M., Flores, L., Ricart, M. J., Fernández-Cruz, L., Esmatjes, E., Crenier, L., Noël, C., Le Moine, A., Mahy, M., Danguy, A., Kiss, R., Goldman, M., Bracci, C., De Haan, B., Nilsson, K., Deschamps, J. Y., Glagoličová, A., Smrčková, I., Dieterle, C., Illner, W. D., Land, W., Feldmeier, H., Scheuer, R., Lalli, C., Di Loreto, C., Ellringmann, U., Balks, H. J., v. zur Mühlen, A., Dengler, R., Weissenborn, K., Rasmussen, B. M., Ørskov, L., Watson, J., Owen, G., Barrett, G., Ingleby, J., Weiss, M., Deary, I., Cavan, D., Kerr, D., Bruneiii, A., Cuce’, A., Elsing, H. G., Kühne, D., Quinn, N. D., Warner, D. P., Buysschaert, M., Jamal, R., O’Brien, T., Latare, P., Mullen, J., Rein, A., Wargo, M., Parkes, J. L., Ginsberg, B., Sotiropoulos, A., Peppas, Th. A., Kotsini, V., Apostolou, O., Bousboulas, S., Michailidis, E., Sawala, M., Pappas, S., Nilsson, P. M., Nilsson, J. Å., Berglund, G., Molins, T., Esteban, J. I., Genescà, J., Paris, I., Haufroid, V., Selvais, Ph., Petit, J. M., Duong, M., Grappin, M., Guiguet, M., Rudoni, S., Portier, H., Brun, J. M., Bagg, W., Plank, L., Drury, P. L., Sharpe, N., Braatvedt, G. D., Carrascosa, J. M., Molero, J. C., Fermίn, Y., Andrés, A., Satrústegui, J., Rietzsch, H., Patzak, A., Schwanebeck, U., Simpson, H., Robertson-Mackay, F., Montegriffo, E., Fox, C., Chiasson, J.-L., Josse, R. G., Dorman, J. M., Gerstein, H. C., Lau, D., Leiter, L. A., Maheux, P., Meneilly, G. S., Murphy, L., Rodger, N. W., Ross, S. A., Ryan, E., Yale, J.-F., Wolever, T. M. S., Haller, T., Elias, I., Segal, P., Standi, E., Rybka, J., Sencer, E., Satman, I., Schlcnzka, A., Vakkilainen, J., Tsaglis, H., Ioannidis, I., Giakoumaki, A., Amantou, A., Komitopoulos, N., Georgiou, S., Varsamis, E., Katsilambros, N., El Gayar, M., Shereba, N., Botros, R., Fikry, R., Jackson, D., Balme, M., Silva-Nunes, J., Alves, J., Bogalho, P., Gardete-Correia, L., Nunes-Corrêa, J., Kot’átková, A., Němcová, D., Vrbíková, J., Zamrazil, V., Meyer, L., Delbachian, I., Lehert, P., Cugnardey, N., Drouin, P., Guerci, B., Wagner, O. F., Jones, N. P., Vallance, S. E., Thompson, K. A., Miller, A. K., Inglis, A. M. L., Patterson, S., Jorkasky, D., Freed, M. I., Mathisen, A. L., Schneider, R., Rubin, C., Houser, V., Beebe, K. L., Kortboyer, J. M., Eckland, D. J. A., Cranmer, H., Mori, Y., Kurokawa, N., Komiya, H., Horikoshi, H., Yokoyama, J., Tajima, N., Ikeda, Y., Bakst, A., Hemyari, P., Lönnqvist, F., Owen, S., Vikramadithyan, R. K., Chakrabarti, R., Misra, P., Prem Kumar, M., Sunil Kumar, K. B., Ghosh, A., Rajagopalan, R., Goldstein, B., Katoh, S., Tsuruoka, N., Hata, S., Matsushima, M., Ikemoto, S., Inoue, Y., Edwards, G., Fonseca, V., Biswas, N., Bakris, G., Viberti, G., Rebuck, A. S., Weill, S., Abel, M. G., Klappoth, W., Brodesser, A., Linkeschowa, R., Pushparaj, P., Tan, C. H., Tan, B. K. H., Bahner, A., Parker, J., Waite, G., Lipson, V., Nahar, N., Rokeya, B., Parveen, S., Nur-e-Alam, M., Mosihuzzaman, M., Hansen, A. Kornerup, Lepore°, M., Kurzhals, R., Pampanelli°, S., Fanelli°, C. G., Bolli°, G. B., Ratner, R. E., Hirsch, I. B., Mecca, T. E., Wilson, C. A., Mohideen, P., Mudaliar, S., Deutsch, R., Ciaraldi, T., Armstrong, D., Kim, B., Morrill, B., Sha, X., Henry, R., Meyer, B. H., Scholtz, H. 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1999
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35. 35th Annual Meeting of the European Association for the Study of Diabetes : Brussels, Belgium, 28 September-2 October 1999

Author

Melander, A., Olsson, J., Lindberg, G., Salzman, A., Howard, T., Stang, P., Lydick, E., Emslie-Smith, A., Boyle, D. I. R., Evans, J. M. M., Macdonald, T. M., Bain, J., Sullivan, F., Ad Darts Memo, Morris For The Collaboration, Juhl, C., Porksen, N., Sturis, J., Hollingdal, M., Pincus, S., Veldhuis, J., Dejgaard, A., Schmitz, O., Kristensen, J. S., Frandsen, K. B., Bayer, Th, Muller, P., Dunning, B. E., Paladini, S., Gutierrez, C., Deacon, R., Valentin, M., Grunberger, G., Weston, W. M., Patwardhan, R., Rappaport, E. B., Sargeant, L. A., Wareham, N. J., Khaw, K. T., Zethelius, Bjorn, Lithell, Hans, Hales, C. Nicholas, Berne, Christian, Lakka, H-M, Oksanen, L., Tuomainen, T-P, Kontula, K., Salonen, J. T., Dekker, J. M., Boks, P., Vegt, F., Stehouwer, C. D. A., Nijpels, G., Bouter, L. M., Heine, R. J., Bruno, G., Cavallo-Perin, P., Bargero, G., D Errico, N., Borra, M., Macchia, G., Pagano, G., Newton, R. W., Ruta, D. A., New, J. P., Wallace, C., Roxburgh, M. A., Young, R. J., Vaughan, N. J. A., Elliott, P., Brennan, G., Devers, M., Macalpine, R., Steinke, D., Lawson, D. H., Decallonne, B., Casteels, K., Gysemans, C., Bouillon, R., Mathieu, C., Linn, Thomas, Strate, Christine, Schneider, Kerstin, Funda, D. P., Jirsa, M. Jr, Kozakova, H., Kaas, A., Kofronova, O., Tlaskalova-Hogenova, H., Buschard, K., Wanka, H., Hartmann, A., Kuttler, B., Rasmussen, S. B., Sorensen, T. S., Markholst, H., Petersen, J. S., Karounos, D., Dyrberg, T., Mabley, J. G., Hasko, G., Szabo, C., Seissler, J., Nguyen, T. B. T., Steinbrenner, H., Scherbaum, W. A., Cipriani, R., Gabriele, A., Sensi, M., Guidobaldi, L., Pantellini, F., Cerrito, M. G., Scarpa, S., Di Mario, U., Morano, S., Ceolotto, G., Iori, E., Baritono, E., Del Prato, S., Semplicini, A., Trevisan, R., Zerbini, G., Meregalli, G., Asnaghi, V., Tentori, F., Maestroni, A., Mangili, R., Marescotti, C., Vedovato, M., Tiengo, A., Tadjieva, J., Mankovsky, B. N., Aken, S., Raes, A., Vande Walle, J., Matthys, D., Craen, M., Hansen, H. P., Lund, S. S., Rossing, P., Jensen, T., Parving, H-H, Genediab, Study Group, Andersen, S., Tarnow, L., Hansen, B. V., Trautner, C., Haastert, B., Ennenbach, N., Willich, S., Tabak, A. Gy, Orchard, T. J., Spranger, J., Preissner, K. T., Schatz, H., Pfeiffer, A., Canton, A., Burgos, R., Hernandez, C., Lecube, A., Mesa, J., Segura, R. M., Mateo, C., Simo, R., Fathallah, L., Greene, D. A., Obrosova, I., Gilbert, R. E., Kelly, D. J., Cox, A. J., Berka-Wilkinson, J. L., Taylor, H. R., Panagiotopoulos, S., Lee, V., Jerums, G., Cooper, M. E., Hitman, G. A., Aganna, E., Ogunkolade, W. B., Rema, M., Deepa, R., Shanthi-Rani, C. S., Barakat, K., Kumarajeewa, T. R., Cassell, P. G., Mcdermott, M. F., Mohan, V., Ways, K., Bursell, S., Devries, T., Woodworth, J., Alatorre, C., King, G., Aiello, L. P., Karisen, A. E., Pavlovic, D., Nielsen, K., Jensen, J., Andersen, H. U., Pociot, F., Mandrup-Poulsen, T., Eizirik, D. L., Nerup, J., Lortz, S., Tiedge, M., Lenzen, S., Lally, F. J., Bone, A. J., Darville, M. I., Ho, Y-S, Sternesjo, J., Sandler, S., Chen, M-C, Schuit, F., Pipeleers, D. G., Merezak, S., Hardikar, A., Hoet, J. J., Remacle, C., Reusens, B., Breant, B., Garofano, A., Czernichow, P., Kubota, N., Terauchi, Y., Miki, H., Tamemoto, H., Yamauchi, T., Nakano, R., Komeda, K., Eto, K., Tobe, K., Kimura, S., Kadowaki, T., Ide, T., Murakami, K., Tsunoda, M., Mochizuki, T., Ozanne, S. E., Nave, B. T., Wang, C. L., Dorling, M. W., Petry, C. J., Koopmans, S. J., Bent, C., Que, I., Radder, J. K., Sebokova, E., Sana, A. K., Klimes, I., Ruderman, N., Morviducci, L., Pastore, L., Morelli, S., Sagratella, E., Zorretta, D., Buongiomo, A., Tamburrano, G., Giaccari, A., Martinenghi, Sabina, Angelis, Gabriella Cusella, Ravasi, Flavio, Bifari, Francesco, Bordignon, Claudio, Falqui, Luca, Kessler, A., Dransfeld, O., Sasson, S., Tomas, E., Zorzano, A., Eckel, J., Thorsby, P., Rosenfalck, A. M., Kjems, L., Hanssen, K. F., Madsbad, S., Birkeland, K. I., Hamilton-Wessler, M., Markussen, J., Bergman, R. N., Melki, V., Hanaire-Broutin, H., Bessieres-Lacombe, S., Gedec, Study Group, Tauber, J-P, Home, P. D., Lindholm, A., Riis, A., European Insulin Aspart Study Group, Rosenstock, J., Schwartz, S., Clark, C., Edwards, M., Donley, D., Us Dm, Study Group Of Insulin Glargine In Type, Swift, P., Mortensen, H. B., Lynggaard, H., Hougaard, P., Hvidore Study group on Childhood Diabetes, Cull, C. A., Neil, H. A. W., Frighi, V., Manley, S. E., Holman, R. R., Turner, R. C., Ukpds, Group, Steiner, G., Dais, Project Group, Davis, W. A., Weeraratna, T., Bruce, D. G., Davis, T. M. E., Verges, B., Duvillard, L., Pont, F., Florentin, E., Gambert, Ph, Benko, B., Ljubic, S., Turk, Z., Granic, M., Marz, W., Wollschlager, H., Klein, G., Neiss, A., Wehling, M., Huxtable, S. J., Saker, P. J., Walker, M., Frayling, T. M., Levy, J. C., O Rahilly, S., Hattersley, A. T., Mccarthy, M. I., Orecchio, A., Giacchini, A., Dominici, R., Canettieri, G., Trinti, B., Zani, M., Andreoli, M., Sciacchitano, S., Silva, A. M., Whitecross, K., Pasco, J., Kotowicz, M., Nicholson, G., Zimmet, P., Boyko, E. J., Collier, G. R., Frittitta, L., Pizzuti, A., Argiolas, A., Graci, S., Goldfine, I. D., Bozzali, M., Ercolino, T., Costanzo, B., Iacoviello, L., Tassi, V., Trischitta, V., Wauters, M., Rankinen, T., Mertens, I., Chagnon, M., Bouchard, C., Gaal, L., Sivenius, K., Valve, R., Hakkarainen, V., Niskanen, L., Laakso, M., Uusitupa, M., Beridze, N., Japaridze, M., Kurashvili, R., Dundua, M., Kebuladze, G., Kazakhashvili, N., Offley-Shore, B., Thomas, B., Ghebremeskel, K., Crawford, M., Lowy, C., Eriksson, Ulf J., Martin Siman, C., Wisse, Bert, Gittenberger-De Groot, Adriana C., Wentzel, P., Eriksson, U. J., Wender-Ozegowska, E., Drews, K., Biczysko, R., Bronisz, A., Rosc, D., Graczykowska-Koczorowska, A., Kotschy, M., Sokup, A., Kohnert, K. D., Besch, W., Strese, J., Frick, U., Zander, E., Kemer, W., Skrha, J., Kvasnicka, J., Kalvodova, B., Hilgertova, J., Schatteman, K., Goossens, F., Scharpe, S., Leeuw, I., Hendriks, D., Legakis, I. N., Panayiotou, D., Mountokalakis, Th D., Enderle, M. D., Beckmann, P., Balletshofer, B., Rittig, K., Maerker, E., Volk, A., Meisner, C., Jacob, S., Matthaei, S., Haring, H. U., Rett, K., Ueda, K., Nakagawa, T., Shimajiri, Y., Kokawa, M., Matsumoto, E., Sasaki, H., Sanke, T., Nanjo, K., Mckinnon, Caroline M., Macfarlane, Wendy M., Docherty, Kevin, Furukawa, N., Shirotani, T., Kishikawa, H., Kaneko, K., Araki, E., Shichiri, M., Prentki, M., Roduit, R., Susini, S., Buteau, J., Ejrnas, A. M., Andersen, N. Aa, Osterhoff, M., Mohlig, M., Ortmann, J., Bikashaghi, F., Mayer, C., Bikashagi, F., Ackermans, M. T., Pereira Arias, A. M., Bisschop, P. H. L. T., Endert, E., Sauerwein, H. P., Romijn, J. A., Gastaldelli, A., Baldi, S., Pettiti, M., Natali, A., Frascerra, S., Camastra, S., Toschi, E., Ferrannini, E., Stingl, H., Krssak, M., Bischof, M. G., Krebs, M., Furnsinn, C., Nowotny, P., Waldhausl, W., Roden, M., Neeft, M., Meijer, A. J., Bavenholm, P., Pigon, J., Efendic, S., Kastenbauer, T., Sauseng, S., Sokol, G., Auinger, M., Irsigler, K., Abbott, C. A., Carrington, A. L., Faragher, B., Kulkarni, J., Ross, E. R. E., Boulton, A. J. M., Armstrong, D. G., Hadi, S., Nguyen, H. C., Harkless, L. B., Jirkovska, A., Kasalicky, P., Hosova, J., Skibova, J., Uccioli, L., Caselli, A., Giacomozzi, C., Macellari, V., Giurato, L., Lardieri, L., Menzinger, G., Pham, H. T., Rosenblum, B. I., Lyons, T. E., Giurini, J. M., Smakowski, P., Chrzan, J. S., Habershaw, G. M., Veves, A., Foster, A. M., Bates, M., Doxford, M., Edmonds, M. E., Kecha, O., Winkler, R., Martens, H., Collette, J., Lefebvre, P. J., Greiner, D., Geenen, V., Atlan-Gepner, C., Naspetti, M., Valero, R., Barad, M., Lepault, F., Vialettes, B., Naquet, P., Galan, B., Netea, M. G., Hancu, N., Smits, P., Meer, J. W. M., Osterbye, T., Jorgensen, K. H., Tranum-Jensen, J., Fredman, P., Hoy, M., Bokvist, K., Olsen, H. L., Horn, T., Gromada, J., Laub, R., Lohmann, T., Hahn, H. J., Adler, T., Emmrich, F., Rabuazzo, A. M., Lupi, R., Dotta, F., Patane, G., Marselli, L., Realacci, M., Piro, S., Del Guerra, S., Santangelo, C., Navalesi, R., Purrello, F., Marchetti, P., Vos, P., Visser, L., Haan, B. J., Klok, P., Schilfgaarde, R., Poppema, S., Juang, J-H, Kuo, C-H, Hsu, B. R-S, Nacher, V., Perez, M., Biarnes, M., Raurell, M., Soler, J., Montanya, E., Ritzel, R., Maubach, J., Busing, M., Becker, T., Klempnauer, J., Hucking, K., Schmiegel, W. H., Nauck, M. A., Boucek, P., Saudek, F., Adamec, M., Kozitarova, R., Jedinakova, T., Vlasakova, Z., Bartos, V., Maffi, P., Bertuzzi, F., Aldrighetti, L., Taglietti, M. V., Castelnuovo, A., Pozza, G., Di Carlo, V., Secchi, A., Renier, G., Mamputu, J-C, Gillespie, J. S., Mcmaster, D., Mercer, C., Trimble, E. R., Lecomte, M., Vericel, E., Paget, C., Ruggiero, D., Lagarde, M., Wiernsperger, N., Pricci, F., Leto, G., Amadio, L., Cordone, S., Iacobini, C., Catalano, S., Violi, F., Rotella, C. M., Pugliese, G., Zicari, A., Gradini, R., Sale, P., Pala, L., Cresci, B., Giannini, S., Manuelli, C., Dahlfors, G., Arnqvist, H. J., Gonelle-Gispert, C., Halnan, P. A., Sadoul, K., Wolter, S., Lang, J., Niwa, T., Yu, W., Hidaka, H., Senda, T., Niki, I., Fukasawa, T., Renstrom, E., Barg, S., Seward, E., Rorsman, P., Rutter, G. A., Molinete, M., Lilla, V., Ravazzola, M., Halban, P. A., Efanov, A. M., Bertorello, A. M., Zaitsev, S. V., Zwiller, J., Berggren, P-O, Msengul, A., Salman, F., Sargrn, M., Ozer, E., Karsidaǧ, K., Salman, S., Gedik, S., Satman, I., Dinccaǧ, N., Yilmaz, M. T., Lloyd, A., Hopkinson, P. K., Testa, M. A., Blonde, L., Turner, R. R., Hayes, J., Simonson, D. C., Ven, N. C. W., Lubach, C. H. C., Snoek, F. J., Mollema, E. D., Ploeg, H. M., Danne, T., Hoey, H., Mcgee, H., Fitzgerald, H., Lernmark, B., Thernlund, G., Fredin, K., Hagglof, B., Lugari, R., Anna, C., Ugolotti, D., Dei Cas, A., Barilli, A. L., Sard, L., Marani, B., Iotti, M., Zandomeneghi, R., Gnudi, A., Kjems, L. L., Volund, Aa, Toft-Nielsen, M., Damholt, M. B., Hilsted, L., Hughes, T. E., Krarup, T., Holst, J. J., Young, A., Gottlieb, A., Fineman, M., Kolterman, O., Cancelas, J., Garcia-Martinez, J. A., Villanueva-Penacarrillo, M. L., Valverde, I., Malaisse, W. J., Filipsson, K., Ahren, B., Balkan, B., Kwasnik, L., Battle, B., Li, X., Egan, J. M., Clocquet, A. R., Elahi, D., Petrella, E., Pricket, K., Petersen, K. F., Sullivan, J. T., Amatruda, J. M., Livingston, J. N., Shulman, G. I., Freyse, E-J, Knospe, S., Glund, K., Demuth, H-U, Walker, D., Malik, R. A., Reljanovic, M., Barada, A., Milicevic, Z., Tack, Cees J., Croatian Study Group for Diabetic Amyotrophy, Goldstein, David S., Huysen, C., Stevens, M. J., Cao, X., Sundkvist, G., Dahlin, L-B, Eriksson, K-F, Rosen, I., Lattimer, S. A., Sima, A. A. F., Sullivan, K., Shaw, J. E., Courten, M. P., Zimmet, P. Z., Gourdy, P., Ruidavets, J. B., Arveiler, D., Amouyel, Ph, Bingham, A., Tauber, J. P., Lam, K. S. L., Wat, N. M. S., Lam, T. H., Janus, E. D., Pablos, P., Rodriguez, F., Martinez, J., Sanchez, V., Santana, C., Garcia, I., Macias, A., Levin, K., Hother-Nielsen, O., Henriksen, J. E., Beck-Nielsen, H., Brechtel, K., Machann, J., Koch, M., Nielsen, M., Loblein, K., Becker, R., Denignger, M., Renn, W., Machicao, F., Claussen, C. D., Schick, F., Diraison, F., Moulin, P., Beylot, M., Thams, P., Capito, K., Eliasson, Lena, Barg, Sebastian, Gopel, Sven, Kanno, Takahiro, Renstrom, Erik, Meda, P., Charollais, A., Gjnovci, A., Calabrese, A., Wonkam, A., Caton, D., Wisznievski, L., Serre, V., Cogne, F., Bauquis, J., Bosco, D., Huarte, J., Herrera, P., Gotfredsen, C. F., Vessby, B., Kanwu, Study Group, Manuel Y Keenoy, B., Engelen, W., Vertommen, J., Schrans, S., Louheranta, A., Lindstrom, J., Tuomilehto, J., Finnish Diabetes Prevention Study Group, Segal, K. R., Heymsfield, S., Hauptman, J., Boldrin, M., Lucas, C., Pandolfi, A., Cetrullo, D., Polishchuck, R., Alberta, M., Pellegrini, G., Calafiore, A., Vitacolonna, E., Capani, F., Consoli, A., Halleux, C. M., Gillot, E. F., Brichard, S. M., Planken, M., Corthouts, B., Peiffer, F., Scholten, D., Walke, M., Assert, R., Pirags, V., Pedula, K. L., Hillier, T. A., Brown, J. B., Eurodiab, Prospective Complications Study Group, Santini, S. A., Marra, G., Cotroneo, P., Manto, A., Di Leo, M. A. S., Di Gregorio, S., Tordi, A., Pitocco, D., Ruotolo, V., Ghirlanda, G., Temelkova-Kurktschiev, T., Schaper, F., Koehler, C., Henkel, E., Hanefeld, M., Mancini, L., Citterio, F., Cotroneo, A., Ceroone, S., Castagneto, M., Rajbhandari, S. M., Dent, M. T., Plater, M. E., Harris, N. D., Tesfaye, S., Ward, J. D., Dupuy, O., Mayaudon, H., Lecoules, S., Bauduceau, B., Palou, M., Farret, O., Molinie, C., Antonelli-Incalzi, R., Fuso, L., Giordano, A., Calcagni, M. L., Todaro, L., Basso, S., Tramaglino, L. M., Troncone, L., Pistelli, R., Guillot, R., Bringuier, A., Porokhov, B., Guillausseau, P. J., Feldmann, G., Zivanic, S., Cizmic, M., Dragojevic, R., Vanovic, M., Borghouts, L. B., Kranenburg, G. P. J., Schaart, G., Keizer, H. A., Niess, A. M., Dickuth, H. H., Lutz, O., Barbe, P., Calazel-Fournier, C., Hernandez, G., Saint-Martin, F., Galitzky, J., Goncalves, A. A., Da Silva, E. C., Brito, I. J. L., Da Silva, C. A., Lawrence, N. J., Kousta, E., Mulnier, H., Penny, A., Millauer, B., Johnston, D. G., Robinson, S., Perriello, G., Pimenta, W., Pampanelli, S., Lucidi, P., Lepore, M., Porcellati, F., Cordoni, M. C., Feo, P., Bolli, G. B., Sjostrand, M., Holmang, A., Lonnroth, P., Hauer, B., Grauer, P., Artzner, S., Lang, R., Stumvoll, M., Monti, L. D., Piatti, P. M., Gemone, F., Valsecchi, G., Magni, M., Barbieri, E., Setola, E., Sandoli, E. P., Galli-Kienle, M., Pontiroli, A. E., Nichols, Gregory A., Brown, Jonathan B., Salzsieder, E., Boltz, H., Ramirez, J. C., Rutscher, A., Fischer, U., Koenig, Ch, Friske, M., Schramm, W., Landgraf, R., Bachmann, W., Bangemann, M., Groeneveld, G., Edvell, Anders, Lindstrom, Per, Tsiotra, P., Koukourava, A., Raptis, S. A., Tsigos, C., Boutou, E., Triandaffilopoulou, A., Egido, E. M., Rodriguez-Gallardo, J., Gutierrez, E., Garcia, P., Silvestre, R. A., Marco, J., Khan, Akhtar, Ling, Zong-Chao, Ahren, Bo, Efendic, Suad, Bunting, C., Du, X., Zhi Sui, G., Rosen, P., Koschinsky, T., Kearney, T. M., Sharp, P. S., Lapolla, A., Fedele, D., Martano, L., Garbeglio, M., Seraglia, R., Favretto, D., Traldi, P., Meerwaldt, R., Smit, A. J., Links, Th P., V Roon, A. M., Graaf, R., Gans, R. O. B., Deyneli, O., Ersoz, H. O., Gogas, D., Fak, A. S., Akalin, S., Veglio, M., Sivieri, R., Chinaglia, A., Scaglione, L., Neuropathy Study Group of the Italian Society of the Study of Diabetes, Le, T., Wong, N., Detrano, R., Charles, M. A., Colhoun, H. M., Francis, D. P., Rubens, M., Underwood, S. R., Fuller, J. H., Knudsen, E., Sato, A., Nielsen, F. S., Bonora, E., Kiechl, S., Willeit, J., Oberhollenzer, F., Egger, G., Bonadonna, R., Muggeo, M., Festa, A., D Agostino, R. Jr, Howard, G., Mykkanen, L., Tracy, R. P., Haffner, S. M., Poulsen, P., Vach, K., European Group for the Study of Insulin Resistance (EGIR), Ijzerman, R. G., Bakker, S. J. L., Truster, J., Crowther, N. J., Cameron, N., Gray, I. P., Chaillous, L., Carel, J. C., Thivolet, C., Boitard, C., Charbonnel, B., Sai, P., Study Group, D. I. O. R., Decochez, K., Keymeulen, B., Somers, G., Dorchy, H., Rottiers, R., Winnock, F., Ver Elst, K., Weets, I., Pipeleers, D., Gorus, F., Seebaum, S., Schumm-Draeger, P-M, Petzoldt, R., Federlin, K., Bonnevie-Nielsen, V., Martensen, P. M., Justesen, J., Worsaa, A., Karlsson, Maria, Sederholm, Sofia, Ludvigsson, Johnny, Belicar, P., Dale, C., Vague, Ph, Alessis, C., Lassmann-Vague, V., Bode, B. W., Gross, T. M., Ghegan, M., Steed, R. D., Davidson, P. C., Ordonez, A., Rubio, J. L., Sulleiro, J. M., Buendia, J. P., Zamora, J., Castillo, M., Schaupp, L., Ellmerer, M., Brunner, G. A., Sendlhofer, G., Schlack, Ch, Skrabal, F., Wach, P., Pieber, T. R., Heinemann, L., Kramer, U., Klotzer, H. M., Hermann, M., Non-Invasive Task Force, Cosgrove, K. E., Chapman, J. C., Shepherd, R. M., Mcintyre, S., Butler, P. C., Dunne, M. J., Brekardin, E., Dorschner, H., Schwanstecher, C., Schwanstecher, M., Uhde, I., Emmanouilidou, E., Teschemacher, A. G., Pouli, A. E., Gylfe, E., Tengholm, A., Hellman, B., Perfetti, R., Aggarwal, S., Muller, Gunter, Welte, Stefan, Wied, Susanne, Valverde, A. M., Mur, C., Kahn, C. R., Benito, M., Rondinone, C. M., Peterson, T., Laviola, L., Belsanti, G., Logoluso, F., Napoli, R., Davalli, A. M., Weir, G. C., Giorgino, R., Giorgino, F., Flesch, S., Hompesch, B., Rave, K., Susanto, F., Kuhn-Velten, W. N., Heise, T., Rendell, M., Dole, J., Rosiglitazone Study Group, Esper, R. J., Stein, E., Lemme, L., Cerivastatin/Bezafibrate Latin America Study Group, Rubinstein, A., Maritz, F. J., Soule, S., Market, A., Chajek-Shaul, T., Maislos, M., Tal, S., Stolero, D., Hidm, Investigators, Josefsen, K., Beckmann, H., Petersen, C., Ekman, R., Efanova, I., Zaitsev, S., Berggren, P. O., Birkenbach, M., Holl, R. W., Rosenbauer, J., Grabert, M., German Working Group on Quality Control, Icks, A., Schwab, O., Reile, K., German Pediat. Working Group, Janssen, M. M. J., Jongh, R. T., Casteleijn, S., Masurel, N., Hoogma, R. P. L. M., Santeusanio, F., Brunetti, P., Fanelli, C. G., Laureti, S., Bartocci, L., Maran, A., Crepaldi, C., Trupiani, S., Macdonald, I. A., Avogaro, A., Bouman, S. D., Keitz, M., Bruggink, J. E., Scheurink, A. J. W., Strubbe, J. H., Steffens, A. B., Ferguson, S. C., Mccrimmon, R. J., Perros, P., Best, J. J. K., Deary, I. J., Frier, B. M., Robinson, R. T. C. E., Ireland, N. H., Bedford, C., Fairclough, E., Hudson, S., Heller, S. R., Borch-Johnsen, K., Berger, M., Overmann, H., Bender, R., Blank, M., Sawicki, P., Jorgens, V., Muhlhauser, I., Nosadini, R., Sailer, A., Dalla Vestra, M., Brocco, E., Piarulli, F., Frigato, F., Sambataro, M., Velussi, M., Baggio, B., Fioretto, P., Jager, A., Hinsbergh, V. W. M., Kostense, P. J., Nrjpels, G., Gade, P., Pedersen, O., Andrysiak-Mamos, E., Majkowska, L., Krzyzanowska, B., Pilarska, K., Czekalski, S., Mazzon, C., Brocco, S., Field, L. L., Nejentsev, S., Gombos, Z., Veijola, R., Knip, M., Simell, O., Vaarala, O., Akerblom, H. K., Ilonen, J., Krokowski, M., Bodalski, J., Andrzejewski, W., Lawnik, M., Teodorczyk, A., Heinrich, A., Caillat-Zucman, S., Buzzetti, R., Petrone, A., Mesturino, C., Giorgi, G., Fiori, R., Nistico, L., Di Genova, G., Cascino, I., Kloting, I., Kovacs, P., Mckinney, P. A., Okasha, M., Parslow, R. C., Law, G. R., Gurney, K. A., Williams, R., Bodansky, H. J., Herzig, P., Giani, G., Vervoort, G., Lutterman, J. A., Berden, J. H. M., Wetzels, J. F. M., Paniagua, O., Shaw, L., Austin, C., Heagerty, A. M., Seppala-Lindroos, A., Vehkavaara, S., Yki-Jarvinen, H., Caballero, A. E., Lim, S. C., Logerfo, F. W., Horton, E. S., Zembowicz, A., Fragasso, G., Caumo, A., Phan, V. C., Costa, S., Conti, M., Chierchia, S. 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J., Quinones Galvan, A., Simeoni, M., Basu, A., Uosukainen, A., Makimattila, S., Schlenzka, A., Adler, A. I., Levy, J., Stevens, R., Matthews, D., Holman, R., Boland, B. J., Jeanjean, M., Hermans, M. P., Maudoigt, C., Tonglet, R., Robert, A., Cini, G., Galetta, F., Sanna, G., Gernone, F., Janssen, M. J., Gonera, R. K., Wolffenbuttel, B. H. R., Leeuw, P. W., Schaper, N. C., Moleda, P., Kuczerowski, R., Czech, A., Taton, J., Taddei, S., Patiag, D., Qu, X., Wilkes, M., Gray, S., Seale, J. P., Donnelly, R., Campion, J., Maestro, B., Davila, N., Carranza, M. C., Calle, C., Hales, C. N., Fernandez-Real, J. M., Grasa, M., Pugeat, M., Barret, C., Ricart, W., Lindmark, S., Olsson, T., Tufvesson, M., Loeblein, K., Mehnert, B., Haering, H. 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S., Murphy, L., Rodger, N. W., Ross, S. A., Ryan, E., Yale, J-F, Wolever, T. M. S., Haller, T., Elias, I., Segal, P., Standi, E., Rybka, J., Sencer, E., Schlcnzka, A., Vakkilainen, J., Tsaglis, H., Ioannidis, I., Giakoumaki, A., Amantou, A., Komitopoulos, N., Georgiou, S., Varsamis, E., Katsilambros, N., El Gayar, M., Shereba, N., Botros, R., Fikry, R., Jackson, D., Balme, M., Silva-Nunes, J., Alves, J., Bogalho, P., Gardete-Correia, L., Nunes-Correa, J., Kot Atkova, A., Nemcova, D., Vrbikova, J., Zamrazil, V., Meyer, L., Delbachian, I., Lehert, P., Cugnardey, N., Drouin, P., Guerci, B., Wagner, O. F., Jones, N. P., Vallance, S. E., Thompson, K. A., Miller, A. K., Inglis, A. M. L., Patterson, S., Jorkasky, D., Freed, M. I., Mathisen, A. L., Schneider, R., Rubin, C., Houser, V., Beebe, K. L., Kortboyer, J. M., Eckland, D. J. 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E., Niekerk, N., Rosenkranz, B., Schoenle, E., Hoe, Study Group, Witthaus, Elke, Bradley, Clare, Stewart, John, Barbeau, M., Myers, S., Flora, D., Dimarchi, R., Chance, R., Plum, A., Larsen, P. S., Larsen, U. D., Kristensen, J. B., Jansen, J. A., Olsen, B., Mortensen, H., Hylleberg, B., Jacobsen, L. V., Gall, M-A, Sogaard, B., Ewing, F. M., Ireland, R. H., Hoogwerf, B., Raskin, P., Jovanovic, L., Leiter, L., Boss, A. H., Bott, U., Ebrahim, S., Hirschberger, S., Leukel, P., Sieber, H. J., Mcgill, J., Kilo, C., Kamp, N. M., Wutte, A., Le Thai, F., Balarac, N., Allicar, M. P., Cazeneuve, B., Augendre, B., Wise, S. D., Seah, E. S., Koivisto, V., Torlone, E., Del Sindaco, P., Ciofetta, M., Hedman, C., Orre Pettersson, A-C, Lindstrom, T., Cernigoi, A. M., Kong, N., Kitchen, M. M., Ryder, R. E. 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36. Exocytosis and protein secretion in Trypanosoma

Author

Rossignol Michel, Gargani Daniel, Centeno Delphine, Bellard Eric, Bécue Thierry, Hirtz Christophe, Geiger Anne, Cuny Gérard, and Peltier Jean-Benoit

Subjects
Microbiology, QR1-502
Abstract

Abstract Background Human African trypanosomiasis is a lethal disease caused by the extracellular parasite Trypanosoma brucei. The proteins secreted by T. brucei inhibit the maturation of dendritic cells and their ability to induce lymphocytic allogenic responses. To better understand the pathogenic process, we combined different approaches to characterize these secreted proteins. Results Overall, 444 proteins were identified using mass spectrometry, the largest parasite secretome described to date. Functional analysis of these proteins revealed a strong bias toward folding and degradation processes and to a lesser extent toward nucleotide metabolism. These features were shared by different strains of T. brucei, but distinguished the secretome from published T. brucei whole proteome or glycosome. In addition, several proteins had not been previously described in Trypanosoma and some constitute novel potential therapeutic targets or diagnostic markers. Interestingly, a high proportion of these secreted proteins are known to have alternative roles once secreted. Furthermore, bioinformatic analysis showed that a significant proportion of proteins in the secretome lack transit peptide and are probably not secreted through the classical sorting pathway. Membrane vesicles from secretion buffer and infested rat serum were purified on sucrose gradient and electron microscopy pictures have shown 50- to 100-nm vesicles budding from the coated plasma membrane. Mass spectrometry confirmed the presence of Trypanosoma proteins in these microvesicles, showing that an active exocytosis might occur beyond the flagellar pocket. Conclusions This study brings out several unexpected features of the secreted proteins and opens novel perspectives concerning the survival strategy of Trypanosoma as well as possible ways to control the disease. In addition, concordant lines of evidence support the original hypothesis of the involvement of microvesicle-like bodies in the survival strategy allowing Trypanosoma to exchange proteins at least between parasites and/or to manipulate the host immune system.

Published
2010
Full Text
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37. Proteins and proteolysis in pre-term and term human milk and possible implications for infant formulae

Author

Emanuele Armaforte, C. Anthony Ryan, R. Paul Ross, Erika Curran, Maria Fiorenza Caboni, Thom Huppertz, Alan L. Kelly, François Chevalier, Nicolas Sommerer, Paula M. O'Connor, Christophe Hirtz, Department of Food and Nutritional Sciences, University College Cork (UCC), University of Bologna, NIZO [Ede, Netherlands], Cork University Hospital, Moorepark Food Research Centre, Teagasc - The Agriculture and Food Development Authority (Teagasc), Unité de Recherche Protéomique (PROTEOMIQUE), Institut National de la Recherche Agronomique (INRA), Plateforme de protéomique, Institut de radiobiologie cellulaire et moléculaire (iRCM), NIZO FOOD RESEARCH (NIZO), Nizo food research, Armaforte E., Curran E., Huppertz T., Ryan C. A., Caboni M. F., O’Connor P. M., Ross R. P., Hirtz C., Sommerer N., Chevalier F., and Kelly A. L.

Subjects
030309 nutrition & dietetics, Plasmin, PROTEINS, Proteolysis, Biology, Applied Microbiology and Biotechnology, 03 medical and health sciences, fluids and secretions, Protein digestibility, Casein, PRETERM INFANTS, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], medicine, Food science, HUMAN MILK, ELECTROPHORESYS, ComputingMilieux_MISCELLANEOUS, Full Term, 2. Zero hunger, chemistry.chemical_classification, 0303 health sciences, medicine.diagnostic_test, 0402 animal and dairy science, food and beverages, 04 agricultural and veterinary sciences, 040201 dairy & animal science, HYDROLYSIS, Term (time), Enzyme, chemistry, Infant formula, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, Food Science, medicine.drug
Abstract

UMR LPF; International audience; Understanding the differences between the protein system of human milk and bovine milk is critical in the development of infant formulae. In this study, the proteins of bovine milk and a bovine-based whey-dominant infant formula were compared with those of human milk for infants born prematurely (pre-term) or at full term (term). The protein distribution of infant formula differed significantly from that of either type of human milk. A proteomic comparison between pre-term and term human milk showed a reduction of levels of β-casein and αs-casein and appearance of additional products, corresponding to low molecular weight hydrolysis products of the caseins, in pre-term milk. Pre-term milk samples also had higher total nitrogen concentration and plasmin activity, consistent with the proteomic data. These results suggest the operation of a physiological mechanism that may adjust enzyme and/or protein expression to modify protein digestibility, and may facilitate design of infant formulae, closer to maternal milk, particularly for premature infants.

Published
2010

38. Dual CRALBP isoforms unveiled: iPSC-derived retinal modelling and AAV2/5-RLBP1 gene transfer raise considerations for effective therapy.

Author

Damodar K, Dubois G, Guillou L, Mamaeva D, Pequignot M, Erkilic N, Sanjurjo-Soriano C, Boukhaddaoui H, Bernex F, Bocquet B, Vialaret J, Arsenijevic Y, Redmond TM, Hirtz C, Meunier I, Brabet P, and Kalatzis V

Abstract

Inherited retinal diseases (IRDs) are characterised by progressive vision loss. There are over 270 causative IRD genes and variants within the same gene can cause clinically distinct disorders. One example is RLBP1 that encodes CRALBP. CRALBP is an essential protein in the rod and cone visual cycles that take place primarily in the retinal pigment epithelium (RPE) but also in Müller cells of the neuroretina. RLBP1 variants lead to three clinical subtypes: Bothnia dystrophy, retinitis punctata albescens and Newfoundland rod-cone dystrophy. We modelled RLBP1-IRD subtypes using patient-specific iPSC-derived RPE and identified pathophysiological markers that served as pertinent therapeutic read-outs. We developed an AAV2/5-mediated gene supplementation strategy and performed a proof-of-concept study in the human models, which was validated in vivo in an Rlbp1 -/- murine model. Most importantly, we identified a previously unsuspected smaller CRALBP isoform that is naturally and differentially expressed both in the human and murine retina. This previously unidentified isoform is produced from an alternative methionine initiation site. This work provides further insights into CRALBP expression and RLBP1-associated pathophysiology and raises important considerations for successful gene supplementation therapy., (Copyright © 2024 The Author(s). Published by Elsevier Inc. All rights reserved.)

Published
2024
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39. Clarifying the association of CSF Aβ, tau, BACE1, and neurogranin with AT(N) stages in Alzheimer disease.

Author

Lehmann S, Schraen-Maschke S, Buée L, Vidal JS, Delaby C, Hirtz C, Blanc F, Paquet C, Allinquant B, Bombois S, Gabelle A, and Hanon O

Subjects
Humans, Aged, Male, Female, Middle Aged, Aged, 80 and over, Alzheimer Disease cerebrospinal fluid, tau Proteins cerebrospinal fluid, Amyloid Precursor Protein Secretases cerebrospinal fluid, Amyloid Precursor Protein Secretases metabolism, Amyloid beta-Peptides cerebrospinal fluid, Neurogranin cerebrospinal fluid, Aspartic Acid Endopeptidases cerebrospinal fluid, Biomarkers cerebrospinal fluid
Abstract

Background: Current AT(N) stratification for Alzheimer's disease (AD) accounts for complex combinations of amyloid (A), tau proteinopathy (T) and neurodegeneration (N) signatures. Understanding the transition between these different stages is a major challenge, especially in view of the recent development of disease modifying therapy., Methods: This is an observational study, CSF levels of Tau, pTau181, pTau217, Aβ38/40/42, sAPPα/β, BACE1 and neurogranin were measured in the BALTAZAR cohort of cognitively impaired patients and in the Alzheimer's Disease Neuroimaging Initiative (ADNI). Biomarkers levels were related to the AT(N) framework. (A) and (T) were defined in BALTAZAR with CSF Aβ42/40 ratio and pTau217 respectively, and in ADNI with amyloid and tau PET. (N) was defined using total CSF tau in both cohorts., Results: As expected, CSF Aβ42 decreased progressively with the AD continuum going from the A-T-N- to the A + T + N + profile. On the other hand, Tau and pTau181 increased progressively with the disease. The final transition from A + T + N- to A + T + N + led to a sharp increase in Aβ38, Aβ42 and sAPP levels. Synaptic CSF biomarkers BACE1 and neurogranin, were lowest in the initial A + T-N- stage and increased with T + and N + . CSF pTau181 and total tau were closely related in both cohorts., Conclusions: The early transition to an A + phenotype (A + T-N-) primarily impacts synaptic function. The appearance of T + and then N + is associated with a significant and progressive increase in pathological Alzheimer's disease biomarkers. Our main finding is that CSF pTau181 is an indicator of N + rather than T + , and that N + is associated with elevated levels of BACE1 protein and beta-amyloid peptides. This increase may potentially fuel the amyloid cascade in a positive feedback loop. Overall, our data provide further insights into understanding the interconnected pathological processes of amyloid, tau, and neurodegeneration underlying Alzheimer's disease., (© 2024. The Author(s).)

Published
2024
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40. A candidate reference measurement procedure for the quantification of α-synuclein in cerebrospinal fluid using an SI traceable primary calibrator and multiple reaction monitoring.

Author

Zhang L, Illes-Toth E, Cryar A, Drinkwater G, Di Vagno L, Pons ML, Mateyka J, McCullough B, Achtar E, Clarkson C, Göschel L, Körtvélyessy P, Mussell C, Hopley CJ, Flöel A, Hirtz C, Lehmann S, and Quaglia M

Subjects
Humans, Calibration, Reference Standards, Mass Spectrometry methods, Parkinson Disease cerebrospinal fluid, Parkinson Disease diagnosis, Biomarkers cerebrospinal fluid, Biomarkers analysis, alpha-Synuclein cerebrospinal fluid, alpha-Synuclein analysis
Abstract

α-synuclein aggregation is an important hallmark of neurodegenerative diseases such as Parkinson's disease (PD) and Lewy body dementia. α-synuclein has been increasingly used as a diagnostic biomarker in PD and other synucleinopathies. Current clinical assays rely on antibody-based immunoassays to detect α-synuclein, which possess high sensitivity, afford high throughput and require small sample volumes. The utility of these assays, however, may be compounded by the specificity, selectivity and batch-to-batch heterogeneity of the antibody used, which can lead to deviations in the total amount of the protein measured when comparing results among different laboratories. Similarly, current mass spectrometry-based quantification methods for α-synuclein lack well-defined, value assigned calibrators to ensure comparability of measurements. Therefore, there is still an unmet need for the standardisation of clinical measurements for α-synuclein that can be achieved by the development of reference measurement procedures (RMPs) utilising calibrators traceable to the SI (International System of Units). Here, we report a candidate RMP for α-synuclein, using an SI traceable primary calibrator and an isotope dilution mass spectrometry (IDMS) approach to address this need. The gravimetrically prepared primary calibrator was traceably quantified utilising a combination of amino acid analysis (AAA) and quantitative nuclear magnetic resonance (qNMR) for value assignment. An optimised targeted sample clean-up procedure involving a non-denaturing Lys-C digestion and solid-phase extraction strategy was devised, followed by the development of a targeted multiple reaction monitoring (MRM) method for the quantification of α-synuclein in cerebrospinal fluid (CSF). This candidate RMP was then deployed for the sensitive detection and accurate quantification of multiple proteotypic α-synuclein peptides in patient derived CSF samples. The LC-MS based results were subsequently compared to immunoassay data to assess the overall performance of our approach. The development and adoption of this candidate RMP, along with the availability of the SI traceable primary calibrator will allow for reliable quantifications of α-synuclein in CSF by an LC-MS based assay. The RMP will potentially contribute towards the standardisation of this important biomarker and may lead to future interlaboratory comparisons.

Published
2024
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41. Serum NfL and GFAP are weak predictors of long-term multiple sclerosis prognosis: A 6-year follow-up.

Author

Ayrignac X, Aouinti S, Vincent T, Carra-Dallière C, Charif M, Duflos C, Hirtz C, Dos Santos A, Menjot de Champfleur N, Labauge P, and Lehmann S

Subjects
Humans, Male, Female, Adult, Prognosis, Follow-Up Studies, Middle Aged, Multiple Sclerosis, Chronic Progressive blood, Multiple Sclerosis, Chronic Progressive diagnostic imaging, Multiple Sclerosis, Chronic Progressive diagnosis, Glial Fibrillary Acidic Protein blood, Neurofilament Proteins blood, Disease Progression, Biomarkers blood, Multiple Sclerosis, Relapsing-Remitting blood, Multiple Sclerosis, Relapsing-Remitting diagnostic imaging, Multiple Sclerosis, Relapsing-Remitting diagnosis
Abstract

Background: Serum neurofilament light chain (sNfL) and glial fibrillary acidic protein (sGFAP) are promising biomarkers that might be associated with clinical and radiological markers of multiple sclerosis (MS) severity. However, it is not known whether they can accurately identify patients at risk of disability progression in the medium and long term., Objectives: We wanted to determine the association between sNfL and sGFAP, Expanded Disability Status Scale score changes, and conversion to secondary progressive MS (SPMS) in a cohort of 133 patients with relapsing remitting MS., Methods: Blood samples were collected at inclusion to measure SNfL and sGFAP by single molecule array and their prognostic value was assessed using a linear mixed model., Results: In this cohort, 37 patients (27.8 % of 133) experienced disability progression and 12 patients (9.0 %) converted to SPMS during the follow-up (mean follow-up duration: 6.4 years). Only sNfL (p = 0.03) was associated with conversion to SPMS, and neither SNfL nor sGFAP was associated with disability progression., Conclusion: Serum NfL and GFAP do not seem to accurately predict MS outcome in the long term. More studies are needed to determine how serum biomarkers, associated with other clinical and MRI biomarkers, might be used to improve MS prognostication., Competing Interests: Declaration of competing interest None., (Copyright © 2024. Published by Elsevier B.V.)

Published
2024
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42. Inherited mitochondrial dysfunction triggered by OPA1 mutation impacts the sensory innervation fibre identity, functionality and regenerative potential in the cornea.

Author

Meneux L, Feret N, Pernot S, Girard M, Sarkis S, Caballero Megido A, Quiles M, Müller A, Fichter L, Vialaret J, Hirtz C, Delettre C, and Michon F

Subjects
Animals, Mice, Regeneration, GTP Phosphohydrolases genetics, GTP Phosphohydrolases metabolism, Cornea innervation, Mutation, Mitochondria metabolism
Abstract

Mitochondrial dysfunctions are detrimental to organ metabolism. The cornea, transparent outmost layer of the eye, is prone to environmental aggressions, such as UV light, and therefore dependent on adequate mitochondrial function. While several reports have linked corneal defects to mitochondrial dysfunction, the impact of OPA1 mutation, known to induce such dysfunction, has never been studied in this context. We used the mouse line carrying OPA1 delTTAG mutation to investigate its impact on corneal biology. To our surprise, neither the tear film composition nor the corneal epithelial transcriptomic signature were altered upon OPA1 mutation. However, when analyzing the corneal innervation, we discovered an undersensitivity of the cornea upon the mutation, but an increased innervation volume at 3 months. Furthermore, the fibre identity changed with a decrease of the SP + axons. Finally, we demonstrated that the innervation regeneration was less efficient and less functional in OPA1 +/- corneas. Altogether, our study describes the resilience of the corneal epithelial biology, reflecting the mitohormesis induced by the OPA1 mutation, and the adaptation of the corneal innervation to maintain its functionality despite its morphogenesis defects. These findings will participate to a better understanding of the mitochondrial dysfunction on peripheral innervation., (© 2024. The Author(s).)

Published
2024
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43. Enabling population protein dynamics through Bayesian modeling.

Author

Lehmann S, Vialaret J, Gabelle A, Bauchet L, Villemin JP, Hirtz C, and Colinge J

Subjects
Humans, Computational Biology methods, Bayes Theorem, Proteins metabolism, Proteins chemistry
Abstract

Motivation: The knowledge of protein dynamics, or turnover, in patients provides invaluable information related to certain diseases, drug efficacy, or biological processes. A great corpus of experimental and computational methods has been developed, including by us, in the case of human patients followed in vivo. Moving one step further, we propose a novel modeling approach to capture population protein dynamics using Bayesian methods., Results: Using two datasets, we demonstrate that models inspired by population pharmacokinetics can accurately capture protein turnover within a cohort and account for inter-individual variability. Such models pave the way for comparative studies searching for altered dynamics or biomarkers in diseases., Availability and Implementation: R code and preprocessed data are available from zenodo.org. Raw data are available from panoramaweb.org., (© The Author(s) 2024. Published by Oxford University Press.)

Published
2024
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44. Modeling the Simultaneous Dynamics of Proteins in Blood Plasma and the Cerebrospinal Fluid in Human In Vivo .

Author

Giroux P, Vialaret J, Kindermans J, Gabelle A, Bauchet L, Hirtz C, Lehmann S, and Colinge J

Subjects
Humans, Models, Biological, Alzheimer Disease cerebrospinal fluid, Alzheimer Disease blood, Blood Proteins metabolism, Cerebrospinal Fluid Proteins analysis, Cerebrospinal Fluid Proteins metabolism
Abstract

The analysis of protein dynamics or turnover in patients has the potential to reveal altered protein recycling, such as in Alzheimer's disease, and to provide informative data regarding drug efficacy or certain biological processes. The observed protein dynamics in a solid tissue or a fluid is the net result of not only protein synthesis and degradation but also transport across biological compartments. We report an accurate 3-biological compartment model able to simultaneously account for the protein dynamics observed in blood plasma and the cerebrospinal fluid (CSF) including a hidden central nervous system (CNS) compartment. We successfully applied this model to 69 proteins of a single individual displaying similar or very different dynamics in plasma and CSF. This study puts a strong emphasis on the methods and tools needed to develop this type of model. We believe that it will be useful to any researcher dealing with protein dynamics data modeling.

Published
2024
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45. Surfaceome: a new era in the discovery of immune evasion mechanisms of circulating tumor cells.

Author

Masmoudi D, Vialaret J, Hirtz C, and Alix-Panabières C

Abstract

Circulating tumor cells (CTCs) are cancer cells that detach from the original site and reach the bloodstream. The most aggressive CTCs survive various immune system attacks and initiate metastasis formation. Importantly, CTCs are not specifically targeted by the current immunotherapies due to the limited knowledge on specific targets. Proteomic profiling can be a powerful tool for understanding some of the immune evasion mechanisms used by cancer cells and particularly CTCs. These mechanisms are generally linked to the expression of specific surface proteins/peptides (i.e. the surfaceome). The study of the peptides that bind to class I molecules of the major histocompatibility complex (MHC-I) and of the various glycoproteins expressed on CTC surface may open a completely new avenue for the discovery of novel mechanisms of immune evasion. In this review, we discuss how immunopeptidomic and glycoproteomic studies of CTCs that interact with immune cells could help to better understand how metastasis-initiator CTCs escape the host immune response. We also describe how immunopeptidomic and glycoproteomic studies are carried out., (© 2024 The Authors. Molecular Oncology published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.)

Published
2024
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46. Post-polio syndrome is not a dysimmune condition.

Author

Laffont I, Duflos C, Hirtz C, Bakhti K, Gelis A, Palayer C, Macioce V, Soler M, Pradalier F, Galtier F, Jentzer A, Lozano C, Vincent T, and Morales RJ

Subjects
Humans, Cross-Sectional Studies, Quality of Life, Pain, Fatigue complications, Muscle Weakness rehabilitation, Immunologic Factors, Postpoliomyelitis Syndrome, Poliomyelitis complications
Abstract

Background: Poliomyelitis is a global disabling disease affecting 12-20 million of people. Post poliomyelitis syndrome (PPS) may affect up to 80% of polio survivors: increased muscle weakness, pain, fatigue, functional decline. It relies on aging of an impaired neuro-muscular system with ongoing denervation processes. A late involvement of humoral or cellular pro-inflammatory phenomena is also suspected., Aim: To assess the dysimmune hypothesis of PPS by comparing lymphocyte subpopulations and humoral immune factors between PPS patients and controls., Design: Cross-sectional study., Setting: Montpellier University Hospital., Population: Forty-seven PPS and 27 healthy controls., Methods: PPS patients and controls were compared on their lymphocyte subpopulations and humoral immune factors (IL-1β, IL-6, IL-8, IL-17, IL-21, IL-22, IL-23, IFN-γ, TNF-α, GM-CSF, RANTES, MCP1, MIP-3a, IL-10, TGF-β, IL4, IL13). Patients were further compared according to their dominant clinical symptoms. Sample size guaranteed a power >90% for all comparisons., Results: PPS patients and controls were comparable in gender, age and corpulence. Most patients had lower limb motor sequelae (N.=45, 95.7%), a minority had upper limb motor impairment (N.=16, 34.0%). Forty-five were able to walk (94%), 35/45 with technical aids. The median of the two-minute walking test was 110 meters (interquartile range 55; 132). Eighteen (38%) required help in their daily life. Their quality of life was low (SF36). All described an increased muscular weakness, 40 (85%) a general fatigue, and 39 (83%) muscular or joint pain. Blood count, serum electrolytes, T and B lymphocyte subpopulations and cytokines were comparable between patients and controls, except for creatine phospho kinase that was significantly higher in PPS patients. None of these variables differed between the 20/47 patients whose late main symptoms were pain or fatigue, and other patients., Conclusions: Our results suggest that PPS is not a dysimmune disease., Clinical Rehabilitation Impact: Our results do not sustain immunotherapy for PPS. Our work suggest that PPS may be mostly linked to physiological age-related phenomena in a disabled neuromuscular condition. Thus, our results emphasize the role of prevention and elimination of aggravating factors to avoid late functional worsening, and the importance of rehabilitation programs that should be adapted to patients' specific conditions.

Published
2024
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47. Inflammation biomarkers in the intracranial blood are associated with outcome in patients with ischemic stroke.

Author

Dargazanli C, Blaquière M, Moynier M, de Bock F, Labreuche J, Ter Schiphorst A, Derraz I, Radu RA, Gascou G, Lefevre PH, Rapido F, Fendeleur J, Arquizan C, Bourcier R, Marin P, Machi P, Cagnazzo F, Hirtz C, Costalat V, and Marchi N

Abstract

Background: Performing endovascular treatment (EVT) in patients with acute ischemic stroke (AIS) allows a port of entry for intracranial biological sampling., Objective: To test the hypothesis that specific immune players are molecular contributors to disease, outcome biomarkers, and potential targets for modifying AIS., Methods: We examined 75 subjects presenting with large vessel occlusion of the anterior circulation and undergoing EVT. Intracranial blood samples were obtained by microcatheter aspiration, as positioned for stent deployment. Peripheral blood samples were collected from the femoral artery. Plasma samples were quality controlled by electrophoresis and analyzed using a Mesoscale multiplex for targeted inflammatory and vascular factors., Results: We measured 37 protein biomarkers in our sample cohort. Through multivariate analysis, adjusted for age, intravenous thrombolysis, pretreatment National Institutes of Health Stroke Scale and Alberta Stroke Program Early CT scores, we found that post-clot blood levels of interleukin-6 (IL-6) were significantly correlated (adjusted P value <0.05) with disability assessed by the modified Rankin Scale (mRS) score at 90 days, with medium effect size. Chemokine (C-C) ligand 17 CCL17/TARC levels were inversely correlated with the mRS score. Examination of peripheral blood showed that these correlations did not reach statistical significance after correction. Intracranial biomarker IL-6 level was specifically associated with a lower likelihood of favorable outcome, defined as a mRS score of 0-2., Conclusions: Our findings show a signature of blood inflammatory factors at the cerebrovascular occlusion site. The correlations between these acute-stage biomarkers and mRS score outcome support an avenue for add-on and localized immune modulatory strategies in AIS., Competing Interests: Competing interests: None declared., (© Author(s) (or their employer(s)) 2024. No commercial re-use. See rights and permissions. Published by BMJ.)

Published
2024
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48. Increasing the sensitivity of Simoa via bead count reduction facilitates the quantification of pTau-181 in dried plasma spots.

Author

Mohaupt P, Vialaret J, Hirtz C, and Lehmann S

Abstract

Introduction: The exclusion of affected populations from Alzheimer's disease (AD) clinical research limits our understanding of disease heterogeneity and its impact on clinical care. While micro sampling with dried plasma spots (DPS) can promote inclusivity by enabling sample collection in remote areas, current techniques lack the sensitivity required for the quantification of phosphorylated tau at Thr181 (pTau-181) in DPS extracts., Methods: We developed an assay for pTau-181 with reduced bead count and improved bead read efficiency (BRE) using a prototype Simoa instrument. This novel assay's performance was evaluated against standard pTau-181 assays on two Simoa platforms, and DPS extracts were tested for pTau-181 quantification feasibility., Results: The novel assay quantifies pTau-181 at concentrations up to 16x lower than traditional pTau-181 assays on HD-X and SR-X platforms. DPS extracts tested with our low-bead assay were quantified considerably above the lower limit of quantification (LLOQ), indicating the suitability of this assay for future DPS extract measurements., Discussion: Implementing DPS sampling and pTau-181 quantification could increase participation from underrepresented groups in AD research. However, additional assay optimization and an in-depth study of preanalytical sample stability are essential for the transition to clinical applicability., Competing Interests: The authors declare no conflicts of interest. Author disclosures are available in the supporting information., (© 2024 The Authors. Alzheimer's & Dementia: Translational Research & Clinical Interventions published by Wiley Periodicals LLC on behalf of Alzheimer's Association.)

Published
2024
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49. Mass Spectrometry-Based Pipeline for Identifying RNA Modifications Involved in a Functional Process: Application to Cancer Cell Adaptation.

Author

Amalric A, Attina A, Bastide A, Buffard M, Mateus S, Planque C, Rivals E, Hirtz C, and David A

Subjects
Chromatography, Liquid, Tandem Mass Spectrometry, RNA genetics, RNA metabolism, RNA, Transfer genetics, RNA, Transfer metabolism, RNA Processing, Post-Transcriptional, Neoplasms genetics
Abstract

Cancer onset and progression are known to be regulated by genetic and epigenetic events, including RNA modifications (a.k.a. epitranscriptomics). So far, more than 150 chemical modifications have been described in all RNA subtypes, including messenger, ribosomal, and transfer RNAs. RNA modifications and their regulators are known to be implicated in all steps of post-transcriptional regulation. The dysregulation of this complex yet delicate balance can contribute to disease evolution, particularly in the context of carcinogenesis, where cells are subjected to various stresses. We sought to discover RNA modifications involved in cancer cell adaptation to inhospitable environments, a peculiar feature of cancer stem cells (CSCs). We were particularly interested in the RNA marks that help the adaptation of cancer cells to suspension culture, which is often used as a surrogate to evaluate the tumorigenic potential. For this purpose, we designed an experimental pipeline consisting of four steps: (1) cell culture in different growth conditions to favor CSC survival; (2) simultaneous RNA subtype (mRNA, rRNA, tRNA) enrichment and RNA hydrolysis; (3) the multiplex analysis of nucleosides by LC-MS/MS followed by statistical/bioinformatic analysis; and (4) the functional validation of identified RNA marks. This study demonstrates that the RNA modification landscape evolves along with the cancer cell phenotype under growth constraints. Remarkably, we discovered a short epitranscriptomic signature, conserved across colorectal cancer cell lines and associated with enrichment in CSCs. Functional tests confirmed the importance of selected marks in the process of adaptation to suspension culture, confirming the validity of our approach and opening up interesting prospects in the field.

Published
2024
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50. A sensitive high-resolution mass spectrometry method for quantifying intact M-protein light chains in patients with multiple myeloma.

Author

Muccio S, Hirtz C, Descloux S, Fedeli O, Macé S, Lehmann S, and Vialaret J

Subjects
Humans, Neoplasm, Residual, Mass Spectrometry methods, Immunoglobulin Light Chains, Antibodies, Monoclonal, Blood Proteins, Multiple Myeloma
Abstract

To determine the disease status and the response to treatment for patients with multiple myeloma, measuring serum M-protein levels is a widely used alternative to invasive punctures to count malignant plasma cells in the bone marrow. However, the quantification of this monoclonal antibody, which varies from patient to patient, poses significant analytical challenges. This paper describes a sensitive and specific mass spectrometry assay that addresses two objectives: to overcome the potential interference of biotherapeutics in the measurement of M-proteins, and to determine the depth of response to treatment by assessing minimal residual disease. After immunocapture of immunoglobulins and free light chains in serum, heavy and light chains were dissociated by chemical reduction and separated by liquid chromatography. M-proteins were analyzed by high-resolution mass spectrometry using a method combining a full MS scan for isotyping and identification and a targeted single ion monitoring scan for quantification. This method was able to discriminate M-protein from the therapeutic antibody in all patient samples analyzed and allowed quantification of M-protein with a LLOQ of 2.0 to 3.5 µg/ml in 5 out of 6 patients. This methodology appears to be promising for assessing minimal residual disease with sufficient sensitivity, specificity, and throughput., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2023 Elsevier B.V. All rights reserved.)

Published
2024
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