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206 results on '"Rampoldi, L"'

1. The Interaction of the Tumor Suppressor FAM46C with p62 and FNDC3 Proteins Integrates Protein and Secretory Homeostasis

Author

Fucci, C, Resnati, M, Riva, E, Perini, T, Ruggieri, E, Orfanelli, U, Paradiso, F, Cremasco, F, Raimondi, A, Pasqualetto, E, Nuvolone, M, Rampoldi, L, Cenci, S, Milan, E, Fucci C., Resnati M., Riva E., Perini T., Ruggieri E., Orfanelli U., Paradiso F., Cremasco F., Raimondi A., Pasqualetto E., Nuvolone M., Rampoldi L., Cenci S., Milan E., Fucci, C, Resnati, M, Riva, E, Perini, T, Ruggieri, E, Orfanelli, U, Paradiso, F, Cremasco, F, Raimondi, A, Pasqualetto, E, Nuvolone, M, Rampoldi, L, Cenci, S, Milan, E, Fucci C., Resnati M., Riva E., Perini T., Ruggieri E., Orfanelli U., Paradiso F., Cremasco F., Raimondi A., Pasqualetto E., Nuvolone M., Rampoldi L., Cenci S., and Milan E.

Abstract

FAM46C is a non-canonical poly(A) polymerase uniquely mutated in up to 20% of multiple myeloma (MM) patients, implying a tissue-specific tumor suppressor function. Here, we report that FAM46C selectively stabilizes mRNAs encoding endoplasmic reticulum (ER)-targeted proteins, thereby concertedly enhancing the expression of proteins that control ER protein import, folding, N-glycosylation, and trafficking and boosting protein secretion. This role requires the interaction with the ER membrane resident proteins FNDC3A and FNDC3B. In MM cells, FAM46C expression raises secretory capacity beyond sustainability, inducing ROS accumulation, ATP shortage, and cell death. FAM46C activity is regulated through rapid proteasomal degradation or the inhibitory interaction with the ZZ domain of the autophagic receptor p62 that hinders its association with FNDC3 proteins via sequestration in p62+ aggregates. Altogether, our data disclose a p62/FAM46C/FNDC3 circuit coordinating sustainable secretory activity and survival, providing an explanation for the MM-specific oncosuppressive role of FAM46C and uncovering potential therapeutic opportunities against cancer. Fucci et al. show that the poly(A) polymerase FAM46C acts as a multiple myeloma-specific tumor suppressor, increasing secretory capacity and antibody production beyond sustainability via its interaction with endoplasmic reticulum transmembrane FNDC3 proteins. Moreover, its activity is restricted through proteasomal degradation or p62-dependent aggregation and sequestration from FNDC3 proteins.

Published
2020

2. Clinical and genetic spectra of autosomal dominant tubulointerstitial kidney disease due to mutations in UMOD and MUC1

Author

Olinger, E, Hofmann, P, Kidd, K, Dufour, I, Belge, H, Schaeffer, C, Kipp, A, Bonny, O, Deltas, C, Demoulin, N, Fehr, T, Fuster, D G, Gale, D P, Goffin, E, Hodanova, K, Huynh-Do, Uyen, Kistler, Andreas, Morelle, J, Papagregoriou, G, Pirson, Y, Sandford, R, Sayer, J A, Torra, R, Venzin, C, Venzin, R, Vogt, B, Živná, M, Greka, A, Dahan, K, Rampoldi, L, Devuyst, Olivier, et al, University of Zurich, and Olinger, E

Subjects
2727 Nephrology, Nephrology, 570 Life sciences, biology, 610 Medicine & health, 10052 Institute of Physiology
Published
2020

3. Cryo-EM structure of native human uromodulin, a zona pellucida module polymer

Author

Stsiapanava, A., Xu, C., Brunati, M., Zamora-Caballero, S., Schaeffer, C., Bokhove, M., Han, L., Hebert, Hans, Carroni, M., Yasumasu, S., Rampoldi, L., Wu, B., Jovine, L., Stsiapanava, A., Xu, C., Brunati, M., Zamora-Caballero, S., Schaeffer, C., Bokhove, M., Han, L., Hebert, Hans, Carroni, M., Yasumasu, S., Rampoldi, L., Wu, B., and Jovine, L.

Abstract

Assembly of extracellular filaments and matrices mediating fundamental biological processes such as morphogenesis, hearing, fertilization, and antibacterial defense is driven by a ubiquitous polymerization module known as zona pellucida (ZP) “domain”. Despite the conservation of this element from hydra to humans, no detailed information is available on the filamentous conformation of any ZP module protein. Here, we report a cryo-electron microscopy study of uromodulin (UMOD)/Tamm–Horsfall protein, the most abundant protein in human urine and an archetypal ZP module-containing molecule, in its mature homopolymeric state. UMOD forms a one-start helix with an unprecedented 180-degree twist between subunits enfolded by interdomain linkers that have completely reorganized as a result of propeptide dissociation. Lateral interaction between filaments in the urine generates sheets exposing a checkerboard of binding sites to capture uropathogenic bacteria, and UMOD-based models of heteromeric vertebrate egg coat filaments identify a common sperm-binding region at the interface between subunits., QC 20210304

Published
2020
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5. Maternally inherited genetic variants of CADPS2 are present in Autism Spectrum Disorders and Intellectual Disability patients

Author

BONORA, ELENA, GRAZIANO, CLAUDIO, MINOPOLI, FIORELLA, BACCHELLI, ELENA, MAGINI, PAMELA, DIQUIGIOVANNI, CHIARA, LOMARTIRE, SILVIA, Bianco F, VARGIOLU, MANUELA, PARCHI, PIERO, MARASCO, ELENA, Mantovani V, Rampoldi L, Trudu M, PARMEGGIANI, ANTONIA, Battaglia A, Mazzone L, Tortora G, MAESTRINI, ELENA, SERI, MARCO, Romeo G, IMGSAC, Bonora E, Graziano C, Minopoli F, Bacchelli E, Magini P, Diquigiovanni C, Lomartire S, Bianco F, Vargiolu M, Parchi P, Marasco E, Mantovani V, Rampoldi L, Trudu M, Parmeggiani A, Battaglia A, Mazzone L, Tortora G, Maestrini E, Seri M, Romeo G, IMGSAC, Bonora, E, Graziano, C, Minopoli, F, Bacchelli, E, Magini, P, Diquigiovanni, C, Lomartire, S, Bianco, F, Vargiolu, M, Parchi, P, Marasco, E, Mantovani, V, Rampoldi, L, Trudu, M, Parmeggiani, A, Battaglia, A, Mazzone, L, Tortora, G, Maestrini, E, Seri, M, and Romeo, G

Subjects
Male, Vesicular Transport Proteins, Inbred C57BL, medicine.disease_cause, Mice, 0302 clinical medicine, autism spectrum disorders (ASDs), Receptors, Intellectual disability, Missense mutation, Developmental, Protein Interaction Maps, Child, Research Articles, Sequence Deletion, Genetics, Mutation, 0303 health sciences, monoallelic expression, Gene Expression Regulation, Developmental, Settore MED/39 - Neuropsichiatria Infantile, Pedigree, intellectual disability, Child, Preschool, DNA methylation, Molecular Medicine, CADPS2, Female, Corrigendum, Adult, Child Development Disorders, autism spectrum disorders, Nerve Tissue Proteins, Biology, 03 medical and health sciences, Young Adult, Dopamine D2, medicine, Animals, Humans, Allele, MUTATION SCREENING, Preschool, Gene, Alleles, Pervasive, 030304 developmental biology, Aged, Receptors, Dopamine D2, Calcium-Binding Proteins, Genetic Variation, Infant, DNA Methylation, medicine.disease, Mice, Inbred C57BL, Gene Expression Regulation, Child Development Disorders, Pervasive, Autism, CpG Islands, mutation screening, Intellectual Disability, 030217 neurology & neurosurgery
Abstract

Intellectual disability (ID) and autism spectrum disorders (ASDs) are complex neuropsychiatric conditions, with overlapping clinical boundaries in many patients. We identified a novel intragenic deletion of maternal origin in two siblings with mild ID and epilepsy in the CADPS2 gene, encoding for a synaptic protein involved in neurotrophin release and interaction with dopamine receptor type 2 (D2DR). Mutation screening of 223 additional patients (187 with ASD and 36 with ID) identified a missense change of maternal origin disrupting CADPS2/D2DR interaction. CADPS2 allelic expression was tested in blood and different adult human brain regions, revealing that the gene was monoallelically expressed in blood and amygdala, and the expressed allele was the one of maternal origin. Cadps2 gene expression performed in mice at different developmental stages was biallelic in the postnatal and adult stages; however, a monoallelic (maternal) expression was detected in the embryonal stage, suggesting that CADPS2 is subjected to tissue- and temporal-specific regulation in human and mice. We suggest that CADPS2 variants may contribute to ID/ASD development, possibly through a parent-of-origin effect.

Published
2014

7. Autosomal dominant tubulointerstitial kidney disease: diagnosis, classification, and management--A KDIGO consensus report

Author

Eckardt, K. -U, Alper, S. L., Antignac, C., Bleyer, A. J., Chauveau, D., Dahan, K., Constantinou-Deltas, Constantinos D., Hosking, A., Kmoch, S., Rampoldi, L., Wiesener, M., Wolf, M. T., Devuyst, O., Constantinou-Deltas, Constantinos D. [0000-0001-5549-9169], Eckardt, Ku, Alper, Sl, Antignac, C, Bleyer, Aj, Chauveau, D, Dahan, K, Deltas, C, Hosking, A, Kmoch, S, Rampoldi, L, Wiesener, M, Wolf, Mt, and Devuyst, O

Subjects
Pathology, Tamm–Horsfall protein, glomerulus filtration rate, genetic association, Gout, uromodulin, kidney disease, DNA Mutational Analysis, treatment contraindication, Disease, hyperuricemia, Medullary cystic kidney disease, preprorenin, REN gene, Tamm Horsfall glycoprotein, Pathognomonic, medical terminology, genetics, gene mutation, autosomal dominant tubulointerstitial kidney disease, pathophysiology, HNF1B gene, biology, predictive value, hepatocyte nuclear factor-1β, consensus development, genetic screening, deficiency, HNF1B, Polycystic Kidney, Autosomal Dominant, genetic code, Phenotype, Treatment Outcome, priority journal, classification, diagnostic test, Nephrology, standards, nomenclature, Kidney Diseases, medicine.medical_specialty, Consensus, phenotype, disease classification, nephrology, kidney transplantation, MUC1 gene, Hyperuricemia, Article, medication therapy management, UMOD gene, gout, Predictive Value of Tests, Terminology as Topic, Uromodulin, medicine, follow up, Humans, Genetic Predisposition to Disease, human, business.industry, practice guideline, hepatocyte nuclear factor 1beta, medicine.disease, mucin 1, clinical feature, renin, consensus, nephronophthisis, Mutation, biology.protein, Tubulointerstitial fibrosis, treatment outcome, Diagnosis Classification, genetic disorder, mutation, business, genetic predisposition, dna mutational analysis, Kidney disease, mucin-1
Abstract

Rare autosomal dominant tubulointerstitial kidney disease is caused by mutations in the genes encoding uromodulin (UMOD), hepatocyte nuclear factor-1β (HNF1B), renin (REN), and mucin-1 (MUC1). Multiple names have been proposed for these disorders, including 'Medullary Cystic Kidney Disease (MCKD) type 2', 'Familial Juvenile Hyperuricemic Nephropathy (FJHN)', or 'Uromodulin-Associated Kidney Disease (UAKD)' for UMOD-related diseases and 'MCKD type 1' for the disease caused by MUC1 mutations. The multiplicity of these terms, and the fact that cysts are not pathognomonic, creates confusion. Kidney Disease: Improving Global Outcomes (KDIGO) proposes adoption of a new terminology for this group of diseases using the term 'Autosomal Dominant Tubulointerstitial Kidney Disease' (ADTKD) appended by a gene-based subclassification, and suggests diagnostic criteria. Implementation of these recommendations is anticipated to facilitate recognition and characterization of these monogenic diseases. A better understanding of these rare disorders may be relevant for the tubulointerstitial fibrosis component in many forms of chronic kidney disease. 88 676 683 Cited By :41

Published
2014

11. UMOD gene in salt sensitivity: a new pathogenetic mechanism

Author

LANZANI C, GATTI G, RAMPOLDI L, DELLI CARPINI S, TRUDU M, SIMONINI M, CITTERIO L, ZAGATO L, MANUNTA , PAOLO, Lanzani, C, Gatti, G, Rampoldi, L, DELLI CARPINI, S, Trudu, M, Simonini, M, Citterio, L, Zagato, L, and Manunta, Paolo

Published
2013

12. UNMOD gene in salt sensitivity: a new pathogenetic mechanism

Author

Gatti G, Lanzani C, Rampoldi L, Binaggia A, Delli Carpini S, Trudu M, Simonini M, Dell’Antonio G, Ferrandi M, Citterio L, Zagato L, MANUNTA , PAOLO, Gatti, G, Lanzani, C, Rampoldi, L, Binaggia, A, Delli Carpini, S, Trudu, M, Simonini, M, Dell’Antonio, G, Ferrandi, M, Citterio, L, Zagato, L, and Manunta, Paolo

Published
2012

13. Mutant uromodulin is secreted in the urine of patients with familial hyperuricemic nephropathy and induces the formation of extracellular aggregates.]

Author

Céline SCHAEFFER, Cattaneo A, Trudu M, Santambrogio S, Bernascone I, Giachino D, Caridi G, Campo A, Murtas C, Benoni S, Izzi C, De Marchi M, Amoroso A, Gm, Ghiggeri, Scolari F, Bachi A, Rampoldi L, Schaeffer, C, Cattaneo, A, Trudu, M, Santambrogio, S, Bernascone, I, Giachino, D, Caridi, G, Campo, A, Murtas, C, Benoni, S, Izzi, C, De Marchi, M, Amoroso, A, Ghiggeri, Gm, Scolari, F, Bachi, A, and Rampoldi, L

Subjects
uromodulin, Uromodulin, medullary cystic kidney disease (MCKD), Mutation, Humans, Kidney Diseases, Hyperuricemia, Extracellular Space
Published
2012

16. Analysis of uromodulin polymerization provides new insights into the mechanisms regulating ZP domain-mediated protein assembly

Author

Schaeffer C, Santambrogio S, Perucca S, Rampoldi L., CASARI , GIORGIO NEVIO, Schaeffer, C, Santambrogio, S, Perucca, S, Casari, GIORGIO NEVIO, and Rampoldi, L.

Abstract

Uromodulin is the most abundant protein secreted in urine, in which it is found as a high-molecular-weight polymer. Polymerization occurs via its zona pellucida (ZP) domain, a conserved module shared by many extracellular eukaryotic proteins that are able to assemble into matrices. In this work, we identified two motifs in uromodulin, mapping in the linker region of the ZP domain and in between protein cleavage and glycosylphosphatidylinositol (GPI)-anchoring sites, which regulate its polymerization. Indeed, mutations in either module led to premature intracellular polymerization of a soluble uromodulin isoform, demonstrating the inhibitory role of these motifs for ZP domain-mediated protein assembly. Proteolytic cleavage separating the external motif from the mature monomer is necessary to release the inhibitory function and allow protein polymerization. Moreover, we report absent or abnormal assembly into filaments of GPI-anchored uromodulin mutated in either the internal or the external motif. This effect is due to altered processing on the plasma membrane, demonstrating that the presence of the two modules has not only an inhibitory function but also can positively regulate protein polymerization. Our data expand previous knowledge on the control of ZP domain function and suggest a common mechanism regulating polymerization of ZP domain proteins.

Published
2009

17. Allelism of medullary cystic disease, familial juvenile hyperuricemic nephropathy and glomerulocystic kidney disease caused by delayed uromodulin trafficking to plasma membrane and endoplasmic reticulum retention

Author

Rampoldi L, Lamorte G, Bernascone I, Caridi G, Santon D, Boaretto F, Tardanico R, Dagnino M, Colussi G, Scolari F, Ghiggeri GM, Amoroso A, MAZZA, DAVIDE, CASARI , GIORGIO NEVIO, Rampoldi, L, Lamorte, G, Bernascone, I, Caridi, G, Santon, D, Boaretto, F, Tardanico, R, Dagnino, M, Colussi, G, Scolari, F, Ghiggeri, Gm, Amoroso, A, Casari, GIORGIO NEVIO, and Mazza, Davide

Published
2006

18. Developments in neuroacanthocytosis: Expanding the spectrum of choreatic syndromes

Author

Walker RH, Danek A, Dobson-Stone C, Guerrini R, Jung HH, Lafontaine AL, Rampoldi L, Tison F, Andermann E, Walker, Rh, Danek, A, Dobson-Stone, C, Guerrini, R, Jung, Hh, Lafontaine, Al, Rampoldi, L, Tison, F, and Andermann, E

Abstract

As with other neurodegenerative disorders, research into the group of diseases known under the umbrella term of "neuroacanthocytosis" has greatly benefited from the identification of causative genes. The distinct and unifying aspect of these disorders is the presence of thorny deformations of circulating erythrocytes. This may be due to abnormal properties of red cell membranes, which could lead to insights into mechanisms of neurodegeneration. Research approaches in this field, in addition to examining functions and protein interactions of the affected proteins with particular respect to neurons, have also drawn upon the expertise of hematologists and red cell membrane biologists. In this article, recent developments in the field are presented. (c) 2006 Movement Disorder Society

Published
2006

22. 6C.06

Author

Marco Simonini, Laura Zagato, John M. Hamlyn, Rampoldi L, Chiara Lanzani, G. Gatti, P. Manunta, Lorena Citterio, Simona Delli Carpini, Elisabetta Messaggio, Nunzia Casamassima, and S. Pozzoli

Subjects
chemistry.chemical_classification, Blood pressure, chemistry, Biochemistry, Physiology, business.industry, Internal Medicine, Medicine, Salt (chemistry), Identification (biology), Cardiology and Cardiovascular Medicine, business, Gene
Published
2015

25. Common noncoding UMOD gene variants induce salt-sensitive hypertension and kidney damage by increasing uromodulin expression

Author

Trudu, M., Janas, S., Lanzani, C., Debaix, H., Schaeffer, C., Ikehata, M., Citterio, L., Demaretz, S., Trevisani, F., Ristagno, G., Glaudemans, B., Laghmani, K., Dell'antonio, G., Bochud, M., Burnier, M., Devuyst, O., Martin, P.Y., Mohaupt, M., Paccaud, F., Pechère-Bertschi, A., Vogt, B., Ackermann, D., Ehret, G., Guessous, I., Ponte, B., Pruijm, M., Loffing, J., Rastaldi, M.P., Manunta, P., Rampoldi, L., Swiss Kidney Project on Genes in Hypertension (SKIPOGH) team, Bochud, M., Burnier, M., Devuyst, O., Martin, PY., Mohaupt, M., Paccaud, F., Pechère-Bertschi, A., Vogt, B., Ackermann, D., Ehret, G., Guessous, I., Ponte, B., and Pruijm, M.

Subjects
Male, Tamm–Horsfall protein, Hypertension/chemically induced/genetics, Genome-wide association study, 030204 cardiovascular system & hematology, Mice, 0302 clinical medicine, Promoter Regions, Genetic, ddc:616, 0303 health sciences, Kidney, education.field_of_study, biology, General Medicine, Middle Aged, 3. Good health, Up-Regulation, medicine.anatomical_structure, Hypertension, Female, Sodium, Dietary/adverse effects/pharmacokinetics, Adult, medicine.medical_specialty, Population, Renal function, Mice, Transgenic, Renal Insufficiency, Chronic/genetics, Polymorphism, Single Nucleotide, General Biochemistry, Genetics and Molecular Biology, Uromodulin/genetics, 03 medical and health sciences, Young Adult, Internal medicine, Uromodulin, medicine, Genetic predisposition, Animals, Humans, Genetic Predisposition to Disease, Renal Insufficiency, Chronic, education, 030304 developmental biology, ddc:613, Aged, Sodium, Dietary, medicine.disease, Promoter Regions, Genetic/genetics, Endocrinology, Blood pressure, Gene Expression Regulation, biology.protein, Kidney disease, Genome-Wide Association Study
Abstract

Hypertension and chronic kidney disease (CKD) are complex traits representing major global health problems. Multiple genome-wide association studies have identified common variants in the promoter of the UMOD gene, which encodes uromodulin, the major protein secreted in normal urine, that cause independent susceptibility to CKD and hypertension. Despite compelling genetic evidence for the association between UMOD risk variants and disease susceptibility in the general population, the underlying biological mechanism is not understood. Here, we demonstrate that UMOD risk variants increased UMOD expression in vitro and in vivo. Uromodulin overexpression in transgenic mice led to salt-sensitive hypertension and to the presence of age-dependent renal lesions similar to those observed in elderly individuals homozygous for UMOD promoter risk variants. The link between uromodulin and hypertension is due to activation of the renal sodium cotransporter NKCC2. We demonstrated the relevance of this mechanism in humans by showing that pharmacological inhibition of NKCC2 was more effective in lowering blood pressure in hypertensive patients who are homozygous for UMOD promoter risk variants than in other hypertensive patients. Our findings link genetic susceptibility to hypertension and CKD to the level of uromodulin expression and uromodulin's effect on salt reabsorption in the kidney. These findings point to uromodulin as a therapeutic target for lowering blood pressure and preserving renal function.

Published
2013

26. Towards the identification of (a) gene(s) for autosomal dominant medullary cystic kidney disease

Author

Scolari, F., Viola, Bf, Gian Marco Ghiggeri, Caridi, G., Amoroso, A., Rampoldi, L., Casari, G., Scolari, F, Viola, Bf, Ghiggeri, Gm, Caridi, G, Amoroso, A, Rampoldi, L, and Casari, GIORGIO NEVIO

Subjects
Kidney Medulla, Nephritis, Autosomal Dominant, Humans, Molecular Biology, Nephritis, Interstitial, Polycystic Kidney, Autosomal Dominant, Polycystic Kidney, Interstitial
Abstract

Medullary cystic kidney disease (MCKD) belongs with nephronophthisis (NPH) in a group of inherited tubulo-interstitial nephritis, which has been referred to as the NPH-MCKD complex. Although MCKD and NPH share morphological features, they differ in several respects. The most common variant is recessive juvenile NPH, with onset in childhood and leading to end-stage renal disease (ESRD) within the 2nd decade of life; the most frequent extrarenal involvement is tapeto-retinal degeneration. MCKD is a dominant condition recognized in later life and leading to ESRD at the age of 50 years; hyperuricemia and gout can be associated features. The first sign of MCKD is polyuria; later, the clinical findings relate to renal insufficiency. Originally, NPH and MCKD were considered separate entities. Subsequently, it has been suggested that the two diseases were a single disorder due to the clinico-pathological identity. This unifying conception was later refuted due to the identification of MCKD dominant families. Recently, considerable insight has been gained into the genetics of the NPH-MCKD complex. The majority of juvenile NPH cases are due to deletion of the NPHP1 gene on chromosome 2q13. Genes for infantile and adolescent NPH have been localized respectively to chromosome 9q22-q31 and 3q22. A new locus, NPHP4, has been recently identified on chromosome 1p36. Two genes predisposing to dominant MCKD, MCKD1 and MCKD2, have been localized to chromosome 1q21 and 16p12. Independent confirmation of the locations of MCKD1 and MCKD2 in other MCKD families, with or without hyperuricemia and gout, has been reported. The gene for familial juvenile hyperuricemic nephropathy (FJHN), a phenotype that is very similar to MCKD, was recently mapped to 16p12, in a region overlapping with the MCKD2 locus, raising the question as to whether MCKD2 and FJHN are allelic variants of the same disease entity. The ultimate proof of the allelism between MCKD2 and FJHN will be provided by the identification of the responsible gene(s). Identification and characterization of the MCKD and FJHN genes will help to clarify the pathogenesis and classification of hereditary tubulo-interstitial nephritides.

Published
2002

28. A conserved sorting-associated protein is mutant in chorea-acanthocytosis RID C-2505-2009 RID A-4495-2010

Author

Rampoldi L, Dobson-Stone C, Rubio JP, Danek A, Chalmers RM, Wood NW, Verellen C, Ferrer X, Malandrini A, Fabrizi GM, Brown R, Vance J, Pericak-Vance M, Rudolf G, Carre S, Alonso E, Manfredi M, Nemeth AH, Monaco AP, Rampoldi, L, Dobson-Stone, C, Rubio, Jp, Danek, A, Chalmers, Rm, Wood, Nw, Verellen, C, Ferrer, X, Malandrini, A, Fabrizi, Gm, Brown, R, Vance, J, Pericak-Vance, M, Rudolf, G, Carre, S, Alonso, E, Manfredi, M, Nemeth, Ah, and Monaco, Ap

Published
2001

31. 6C.06

Author

Gatti, G., primary, Lanzani, C., additional, Citterio, L., additional, Messaggio, E., additional, Carpini, S. Delli, additional, Simonini, M., additional, Pozzoli, S., additional, Casamassima, N., additional, Zagato, L., additional, Rampoldi, L., additional, Hamlyn, J.M., additional, and Manunta, P., additional

Published
2015
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45. Mutational spectrum of the CHAC gene in patients with chorea-acanthocytosis

Author

DOBSON STONE, C., Danek, A., Rampoldi, L., Hardie, R., Chalmers, R. M., Wood, N. W., Bohlega, S., Dotti, M. T., Federico, A., Shizuka, M., Tanaka, M., Watanabe, M., Ikeda, Y., Brin, M., Goldfarb, L. G., Karp, B. I., Mohiddin, S., Storch, A., Fryer, A. E., Maddison, P., Sibon, I., TREVISOL BITTENCOURT, P. C., Singer, C., Requena, I., Aasly, J. O., Schmierer, K., Zeviani, M., Meiner, V., Lossos, A., Johnson, S., Mercado, F. C., Sorrentino, Giuseppe, Rouleau, G., Volkmann, J., Lees, A., Geraud, G., Chouinard, S., Nmeth, A., and AND MONACO, A. P.

Subjects
CHAC, Chorea, acanthocytosis, mutational spectrum, neuroacanthocytosis, chorein
Published
2002

46. The rediscovery of uromodulin (Tamm-Horsfall protein): from tubulointerstitial nephropathy to chronic kidney disease

Author

Rampoldi, L, Scolari, F, Amoroso, A, Ghiggeri, G, Devuyst, O, Rampoldi, L, Scolari, F, Amoroso, A, Ghiggeri, G, and Devuyst, O

Abstract

Uromodulin (Tamm-Horsfall protein) is the most abundant protein excreted in the urine under physiological conditions. It is exclusively produced in the kidney and secreted into the urine via proteolytic cleavage. Its biological function is still not fully understood. Uromodulin has been linked to water/electrolyte balance and to kidney innate immunity. Also, studies in knockout mice demonstrated that it has a protective role against urinary tract infections and renal stone formation. Mutations in the gene encoding uromodulin lead to rare autosomal dominant diseases, collectively referred to as uromodulin-associated kidney diseases. They are characterized by progressive tubulointerstitial damage, impaired urinary concentrating ability, hyperuricemia, renal cysts, and progressive renal failure. Novel in vivo studies point at intracellular accumulation of mutant uromodulin as a key primary event in the disease pathogenesis. Recently, genome-wide association studies identified uromodulin as a risk factor for chronic kidney disease (CKD) and hypertension, and suggested that the level of uromodulin in the urine could represent a useful biomarker for the development of CKD. In this review, we summarize these recent investigations, ranging from invalidation studies in mouse to Mendelian disorders and genome-wide associations, which led to a rediscovery of uromodulin and boosted the scientific and clinical interest for this long discovered molecule.

Published
2011

47. EUNEFRON, the European Network for the Study of Orphan Nephropathies.

Author

Devuyst, O., Meij, I., Jeunemaitre, X., Ronco, P., Antignac, C., Christensen, E.I., Slobbe-Knoers, V.V.A.M., Levtchenko, E.N., Deen, P.M.T., Muller, D., Wagner, C.A., Rampoldi, L., Hoff, W.G. van 't, Devuyst, O., Meij, I., Jeunemaitre, X., Ronco, P., Antignac, C., Christensen, E.I., Slobbe-Knoers, V.V.A.M., Levtchenko, E.N., Deen, P.M.T., Muller, D., Wagner, C.A., Rampoldi, L., and Hoff, W.G. van 't

Abstract

Contains fulltext : 80881.pdf (publisher's version ) (Closed access)

Published
2009

48. EUNEFRON, the European Network for the Study of Orphan Nephropathies

Author

Devuyst, O, Meij, I, Jeunemaitre, X, Ronco, P, Antignac, C, Christensen, E I, Knoers, N V, Levtchenko, E N, Deen, P M, Müller, D, Wagner, C A, Rampoldi, L, Van't Hoff, W G, Devuyst, O, Meij, I, Jeunemaitre, X, Ronco, P, Antignac, C, Christensen, E I, Knoers, N V, Levtchenko, E N, Deen, P M, Müller, D, Wagner, C A, Rampoldi, L, and Van't Hoff, W G

Published
2009

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