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34 results on '"Brand-Arzamendi, Koroboshka"'

1. Automated in vivo compound screening with zebrafish and the discovery and validation of PD 81,723 as a novel angiogenesis inhibitor

Author

Mauro, Antonio N., Turgeon, Paul J., Gupta, Sahil, Brand-Arzamendi, Koroboshka, Chen, Hao, Malone, Jeanie H., Ng, Robin, Ho, Kevin, Dubinsky, Michelle, Di Ciano-Oliveira, Caterina, Spring, Christopher, Plant, Pamela, Leong-Poi, Howard, Marshall, John C., Marsden, Philip A., Connelly, Kim A., and Singh, Krishna K.

Published
2022
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3. Bi-allelic GOT2 Mutations Cause a Treatable Malate-Aspartate Shuttle-Related Encephalopathy

Author

van Karnebeek, Clara D.M., Ramos, Rúben J., Wen, Xiao-Yan, Tarailo-Graovac, Maja, Gleeson, Joseph G., Skrypnyk, Cristina, Brand-Arzamendi, Koroboshka, Karbassi, Farhad, Issa, Mahmoud Y., van der Lee, Robin, Drögemöller, Britt I., Koster, Janet, Rousseau, Justine, Campeau, Philippe M., Wang, Youdong, Cao, Feng, Li, Meng, Ruiter, Jos, Ciapaite, Jolita, Kluijtmans, Leo A.J., Willemsen, Michel A.A.P., Jans, Judith J., Ross, Colin J., Wintjes, Liesbeth T., Rodenburg, Richard J., Huigen, Marleen C.D.G., Jia, Zhengping, Waterham, Hans R., Wasserman, Wyeth W., Wanders, Ronald J.A., Verhoeven-Duif, Nanda M., Zaki, Maha S., and Wevers, Ron A.

Published
2019
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5. Plasma glial fibrillary acidic protein levels correlate with paramagnetic rim lesions in people with radiologically isolated syndrome.

Author

Schneider, Raphael, Brand-Arzamendi, Koroboshka, Reynold Lim, Timothy, Lee, Lisa Eunyoung, Guenette, Melanie, Suthiphosuwan, Suradech, Bharatha, Aditya, and Oh, Jiwon

Subjects
*GLIAL fibrillary acidic protein, *CERVICAL cord, *MAGNETIC resonance imaging, *SPINAL cord, *WHITE matter (Nerve tissue)
Abstract

Background: There are no specific, evidence-based recommendations for the management of individuals with radiologically isolated syndrome. Imaging and blood biomarkers may have prognostic utility. Objective: To determine whether plasma neurofilament light protein (NfL) or glial fibrillary acidic protein (GFAP) levels in people with radiologically isolated syndrome correlate with imaging measures that have been shown to be associated with negative clinical outcomes in people with multiple sclerosis. Methods: Cross-sectional analysis of people with radiologically isolated syndrome. Participants underwent magnetic resonance imaging (MRI) of the brain and cervical spinal cord, and plasma was collected. Plasma NfL and GFAP levels were measured with a single-molecule array, and correlations with MRI measures were assessed, including the number of: T1-black holes, white-matter lesions demonstrating the central vein sign, paramagnetic rim lesions, cervical spinal cord lesions and infratentorial lesions. Results: Plasma GFAP levels, but not NfL levels, showed correlations with the number of T1-black holes, white matter lesions demonstrating the central vein sign and paramagnetic rim lesions (all p < 0.05). Conclusion: We found correlations between plasma GFAP levels and imaging measures associated with poor clinical outcomes and chronic inflammation in individuals with radiologically isolated syndrome. Plasma GFAP may have prognostic utility in clinical trials and clinical practice. [ABSTRACT FROM AUTHOR]

Published
2024
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9. Iroquois homeobox gene 3 establishes fast conduction in the cardiac His–Purkinje network

Author

Zhang, Shan-Shan, Kim, Kyoung-Han, Rosen, Anna, Smyth, James W., Sakuma, Rui, Delgado-Olguín, Paul, Davis, Mark, Chi, Neil C., Puviindran, Vijitha, Gaborit, Nathalie, Sukonnik, Tatyana, Wylie, John N., Brand-Arzamendi, Koroboshka, Farman, Gerrie P., Kim, Jieun, Rose, Robert A., Marsden, Phillip A., Zhu, Yonghong, Zhou, Yu-Qing, Miquerol, Lucile, Henkelman, R. Mark, Stainier, Didier Y. R., Shaw, Robin M., Hui, Chi-chung, Bruneau, Benoit G., and Backx, Peter H.

Published
2011

13. Fetal bovine serum impacts the observed N‐glycosylation defects in TMEM165 KO HEK cells

Author

Climer, Leslie, Morelle, Willy, De Bettignies, Geoffroy, Krzewinski Recchi, Marie-Ange, Lupashin, Vladimir, Medina-Cano, Daniel, Ucuncu, Ekin, Nguyen, Lam Son, Nicouleau, Michael, Lipecka, Joanna, Bizot, Jean-Charles, Thiel, Christian, Lefort, Nathalie, Faivre-Sarrailh, Catherine, Colleaux, Laurence, Guerrera, Ida Chiara, Cantagrel, Vincent, Lebredonchel, Elodie, Garat, Anne, Legrand, Dominique, Decool, Valérie, Klein, André, Ouzzine, Mohamed, Gasnier, Bruno, Potelle, Sven, Groux‐Degroote, Sophie, Cogez, Virginie, Noel, Maxence, Portier, Lucie, Solórzano, Carlos, Dall'Olio, Fabio, Steenackers, Agata, Mortuaire, Marlène, Gonzalez‐Pisfil, Mariano, Henry, Mélanie, Heliot, Laurent, Harduin-Lepers, Anne, Berthe, Audrey, Zaffino, Marie, Muller, claire, Houdou, Marine, Schulz, Céline, Bost, Frédéric, De Fay, Elia, Mazerbourg, Sabine, Flament, Stéphane, Mouajjah, Dounia, Ashikov, Angel, Abu Bakar, Nurulamin, Wen, Xiao-Yan, Niemeijer, Marco, Rodrigues Pinto Osorio, Glentino, Brand-Arzamendi, Koroboshka, Hasadsri, Linda, Hansikova, Hana, Raymond, Kimiyo, Ondruskova, Nina, Simon, Marleen, Pfundt, Rolph, Timal, Sharita, Beumers, Roel, Smeets, Roel, Kersten, Marjan, Huijben, Karin, Linders, Peter, van den Bogaart, Geert, van Hijum, Sacha, Rodenburg, Richard, van den Heuvel, Lambertus, Van Spronsen, Francjan, Honzik, Tomas, van Scherpenzeel, Monique, Lefeber, Dirk, Mirjam, Wamelink, Han, Brunner, Helen, Mundy, Helen, Michelakakis, Peter, van Hasselt, Jiddeke, van de Kamp, Diego, Martinelli, Lars, Morkrid, Katja, Brocke Holmefjord, Jozef, Hertecant, Majid, Alfadhel, Kevin, Carpenter, Johann, te Water Naude, Delos, Maxime, Hellec, Charles, Fifre, Alexandre, Carpentier, Mathieu, Papy-Garcia, Dulce, Allain, Fabrice, Denys, Agnés, Gilormini, Pierre André, Lion, Cédric, Vicogne, Dorothée, Guerardel, Yann, Biot, Christophe, Witters, Peter, Breckpot, Jeroen, Preston, Graem, Morava, Eva, Rujano, Maria, Cannata Serio, Magda, Panasyuk, Ganna, Reunert, Janine, Hauser, Virginie, Park, Julien, Freisinger, Peter, Guida, Maria Clara, Maier, Esther, Wada, Yoshinao, Jäger, Stefanie, Krogan, Nevan, Kretz, Oliver, Nobre, Susana, Garcia, Paula, Quelhas, Dulce, Bird, Thomas, Raskind, Wendy, Schwake, Michael, Duvet, Sandrine, Marquardt, Thorsten, Simons, Matias, Blommaert, Eline, Péanne, Romain, Cherepanova, Natalia, Rymen, Daisy, Staels, Frederik, Jaeken, Jaak, Race, Valérie, Keldermans, Liesbeth, Souche, Erika, Corveleyn, Anniek, Sparkes, Rebecca, Bhattacharya, Kaustuv, Devalck, Christine, Schrijvers, Rik, Foulquier, Francois, Gilmore, Reid, Matthijs, Gert, Université Lille Nord de France (COMUE), Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS), Variabilité génétique des défenses de l'organisme face à son environnement chimique, PRES Université Lille Nord de France-Université de Lille, Droit et Santé, ANR-15-CE14-0001,SOLV_CDG,Décryptage des patients CDG (Congenital Disorders of Glyvosylation) déficients en TMEM165 - de la compréhension des mécanismes moléculaires à une thérapie(2015), ANR-15-RAR3-0004,EURO-CDG-2,A European research network directed towards improving diagnosis and treatment of inborn glycosylation disorders.(2015), European Project: 643578,H2020,H2020-HCO-2014,E-Rare-3(2014), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Université de Lille, CNRS, Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF], Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF], Centre Hospitalier Régional Universitaire [Lille] [CHRU Lille], Impact de l'environnement chimique sur la santé humaine - ULR 4483 [IMPECS], Baylor University, University of Arkansas for Medical Sciences [UAMS], Institut de Génétique Moléculaire de Montpellier (IGMM), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM), Imagine - Institut des maladies génétiques (IMAGINE - U1163), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut de psychiatrie et neurosciences (U894 / UMS 1266), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Key-Obs, JRC Institute for Energy and Transport (IET), European Commission - Joint Research Centre [Petten], Institut de Neurobiologie de la Méditerranée [Aix-Marseille Université] (INMED - INSERM U1249), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Plateforme Protéomique Necker [SFR Necker] (PPN - 3P5), Structure Fédérative de Recherche Necker (SFR Necker - UMS 3633 / US24), Assistance publique - Hôpitaux de Paris (AP-HP) (APHP)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Assistance publique - Hôpitaux de Paris (AP-HP) (APHP)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Impact de l'environnement chimique sur la santé humaine (IMPECS), Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Université de Lille, Biologie cellulaire et moléculaire de la sécrétion (BCMS), Centre National de la Recherche Scientifique (CNRS), Departamento de Bioquímica, Instituto Nacional de Enfermedades Respiratorias, Department of Experimental, Diagnostic and Specialty Medicine (DIMES) (DIMES), Università di Bologna [Bologna] (UNIBO), Laboratoire de Physique des Lasers, Atomes et Molécules - UMR 8523 (PhLAM), Biophotonique Cellulaire Fonctionelle, Institut de Recherche Interdisciplinaire, Institut de Recherche Interdisciplinaire [Villeneuve d'Ascq] (IRI), Université de Lille, Sciences et Technologies-Université de Lille, Droit et Santé-Centre National de la Recherche Scientifique (CNRS), Centre méditerranéen de médecine moléculaire (C3M), Université Nice Sophia Antipolis (UNS), Université Côte d'Azur (UCA)-Université Côte d'Azur (UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM), Department of Medicine & Physiology , University of Toronto, First Faculty of Medicine, Charles University [Prague], University Medical Center [Utrecht], Department of Human Genetics, Radboud University Medical Center [Nijmegen], Paediatrics, Beatrix Children's Hospital/University Medical Center Groningen, Université Toulouse 1 Capitole (UT1), Croissance cellulaire, réparation et régénération tissulaires (CRRET), Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12)-Centre National de la Recherche Scientifique (CNRS), Chimie Moléculaire et Formulation (EA 4478), Université de Lille, Sciences et Technologies, Unité de Catalyse et de Chimie du Solide - UMR 8181 (UCCS), Université d'Artois (UA)-Ecole Centrale de Lille-Ecole Nationale Supérieure de Chimie de Lille (ENSCL)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Department of Pediatrics, University Children's Hospital, Centre de recherche Croissance et signalisation (UMR_S 845), Reutlingen University, Department of General Pediatrics, Münster University Children Hospital, Molecular Diagnostics, Center for Human Genetics, Gasthuisberg, Katholieke Universiteit Leuven and Flanders Interuniversity Institute for Biotechnology 4, Leuven, Belgium, Catholic University of Leuven - Katholieke Universiteit Leuven (KU Leuven), Center for Human Genetics, and Laboratory of clinical immunology

Subjects
Glycosylation, Protein family, [SDV]Life Sciences [q-bio], Golgi Apparatus, FBS, manganese level, N‐glycosylation defects, TMEM165, Article, Antiporters, Glycomics, 03 medical and health sciences, chemistry.chemical_compound, symbols.namesake, Congenital Disorders of Glycosylation, 0302 clinical medicine, N-linked glycosylation, Genetics, Humans, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Cation Transport Proteins, Genetics (clinical), ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, Manganese, 0303 health sciences, Ion Transport, HEK 293 cells, Serum Albumin, Bovine, Golgi apparatus, Embryonic stem cell, Cell biology, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], carbohydrates (lipids), HEK293 Cells, chemistry, symbols, Calcium, 030217 neurology & neurosurgery, Fetal bovine serum
Abstract

TMEM165 is involved in a rare genetic human disease named TMEM165‐CDG (congenital disorders of glycosylation). It is Golgi localized, highly conserved through evolution and belongs to the uncharacterized protein family 0016 (UPF0016). The use of isogenic TMEM165 KO HEK cells was crucial in deciphering the function of TMEM165 in Golgi manganese homeostasis. Manganese is a major cofactor of many glycosylation enzymes. Severe Golgi glycosylation defects are observed in TMEM165 Knock Out Human Embryonic Kidney (KO HEK) cells and are rescued by exogenous manganese supplementation. Intriguingly, we demonstrate in this study that the observed Golgi glycosylation defect mainly depends on fetal bovine serum, particularly its manganese level. Our results also demonstrate that iron and/or galactose can modulate the observed glycosylation defects in TMEM165 KO HEK cells. While isogenic cultured cells are widely used to study the impact of gene defects on proteins' glycosylation patterns, these results emphasize the importance of the use of validated fetal bovine serum in glycomics studies. 43;2

Published
2019
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14. Glutaminase Deficiency Caused by Short Tandem Repeat Expansion in GLS

Author

van Kuilenburg, Andre B. P., Tarailo-Graovac, Maja, Richmond, Phillip A., Drogemoller, Britt I., Pouladi, Mahmoud A., Leen, Rene, Brand-Arzamendi, Koroboshka, Dobritzsch, Doreen, Dolzhenko, Egor, Eberle, Michael A., Hayward, Bruce, Jones, Meaghan J., Karbassi, Farhad, Kobor, Michael S., Koster, Janet, Kumari, Daman, Li, Meng, MacIsaac, Julia, McDonald, Cassandra, Meijer, Judith, Nguyen, Charlotte, Rajan-Babu, Indhu-Shree, Scherer, Stephen W., Sim, Bernice, Trost, Brett, Tseng, Laura A., Turkenburg, Marjolein, van Vugt, Joke J. F. A., Veldink, Jan H., Walia, Jagdeep S., Wang, Youdong, van Weeghel, Michel, Wright, Galen E. B., Xu, Xiaohong, Yuen, Ryan K. C., Zhang, Jinqiu, Ross, Colin J., Wasserman, Wyeth W., Geraghty, Michael T., Santra, Saikat, Wanders, Ronald J. A., Wen, Xiao-Yan, Waterham, Hans R., Usdin, Karen, van Karnebeek, Clara D. M., van Kuilenburg, Andre B. P., Tarailo-Graovac, Maja, Richmond, Phillip A., Drogemoller, Britt I., Pouladi, Mahmoud A., Leen, Rene, Brand-Arzamendi, Koroboshka, Dobritzsch, Doreen, Dolzhenko, Egor, Eberle, Michael A., Hayward, Bruce, Jones, Meaghan J., Karbassi, Farhad, Kobor, Michael S., Koster, Janet, Kumari, Daman, Li, Meng, MacIsaac, Julia, McDonald, Cassandra, Meijer, Judith, Nguyen, Charlotte, Rajan-Babu, Indhu-Shree, Scherer, Stephen W., Sim, Bernice, Trost, Brett, Tseng, Laura A., Turkenburg, Marjolein, van Vugt, Joke J. F. A., Veldink, Jan H., Walia, Jagdeep S., Wang, Youdong, van Weeghel, Michel, Wright, Galen E. B., Xu, Xiaohong, Yuen, Ryan K. C., Zhang, Jinqiu, Ross, Colin J., Wasserman, Wyeth W., Geraghty, Michael T., Santra, Saikat, Wanders, Ronald J. A., Wen, Xiao-Yan, Waterham, Hans R., Usdin, Karen, and van Karnebeek, Clara D. M.

Abstract

We report an inborn error of metabolism caused by an expansion of a GCA-repeat tract in the 5′ untranslated region of the gene encoding glutaminase (GLS) that was identified through detailed clinical and biochemical phenotyping, combined with whole-genome sequencing. The expansion was observed in three unrelated patients who presented with an early-onset delay in overall development, progressive ataxia, and elevated levels of glutamine. In addition to ataxia, one patient also showed cerebellar atrophy. The expansion was associated with a relative deficiency of GLS messenger RNA transcribed from the expanded allele, which probably resulted from repeat-mediated chromatin changes upstream of the GLS repeat. Our discovery underscores the importance of careful examination of regions of the genome that are typically excluded from or poorly captured by exome sequencing.

Published
2019
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15. Bi-allelic GOT2 Mutations Cause a Treatable Malate-Aspartate Shuttle-Related Encephalopathy

Author

van Karnebeek, Clara D M, Ramos, Rúben J, Wen, Xiao-Yan, Tarailo-Graovac, Maja, Gleeson, Joseph G, Skrypnyk, Cristina, Brand-Arzamendi, Koroboshka, Karbassi, Farhad, Issa, Mahmoud Y, van der Lee, Robin, Drögemöller, Britt I, Koster, Janet, Rousseau, Justine, Campeau, Philippe M, Wang, Youdong, Cao, Feng, Li, Meng, Ruiter, Jos, Ciapaite, Jolita, Kluijtmans, Leo A J, Willemsen, Michel A A P, Jans, Judith J, Ross, Colin J, Wintjes, Liesbeth T, Rodenburg, Richard J, Huigen, Marleen C D G, Jia, Zhengping, Waterham, Hans R, Wasserman, Wyeth W, Wanders, Ronald J A, Verhoeven-Duif, Nanda M, Zaki, Maha S, Wevers, Ron A, van Karnebeek, Clara D M, Ramos, Rúben J, Wen, Xiao-Yan, Tarailo-Graovac, Maja, Gleeson, Joseph G, Skrypnyk, Cristina, Brand-Arzamendi, Koroboshka, Karbassi, Farhad, Issa, Mahmoud Y, van der Lee, Robin, Drögemöller, Britt I, Koster, Janet, Rousseau, Justine, Campeau, Philippe M, Wang, Youdong, Cao, Feng, Li, Meng, Ruiter, Jos, Ciapaite, Jolita, Kluijtmans, Leo A J, Willemsen, Michel A A P, Jans, Judith J, Ross, Colin J, Wintjes, Liesbeth T, Rodenburg, Richard J, Huigen, Marleen C D G, Jia, Zhengping, Waterham, Hans R, Wasserman, Wyeth W, Wanders, Ronald J A, Verhoeven-Duif, Nanda M, Zaki, Maha S, and Wevers, Ron A

Published
2019

16. Bi-allelic GOT2 Mutations Cause a Treatable Malate-Aspartate Shuttle-Related Encephalopathy

Author

Genetica Sectie Metabole Diagnostiek, Child Health, Cancer, van Karnebeek, Clara D M, Ramos, Rúben J, Wen, Xiao-Yan, Tarailo-Graovac, Maja, Gleeson, Joseph G, Skrypnyk, Cristina, Brand-Arzamendi, Koroboshka, Karbassi, Farhad, Issa, Mahmoud Y, van der Lee, Robin, Drögemöller, Britt I, Koster, Janet, Rousseau, Justine, Campeau, Philippe M, Wang, Youdong, Cao, Feng, Li, Meng, Ruiter, Jos, Ciapaite, Jolita, Kluijtmans, Leo A J, Willemsen, Michel A A P, Jans, Judith J, Ross, Colin J, Wintjes, Liesbeth T, Rodenburg, Richard J, Huigen, Marleen C D G, Jia, Zhengping, Waterham, Hans R, Wasserman, Wyeth W, Wanders, Ronald J A, Verhoeven-Duif, Nanda M, Zaki, Maha S, Wevers, Ron A, Genetica Sectie Metabole Diagnostiek, Child Health, Cancer, van Karnebeek, Clara D M, Ramos, Rúben J, Wen, Xiao-Yan, Tarailo-Graovac, Maja, Gleeson, Joseph G, Skrypnyk, Cristina, Brand-Arzamendi, Koroboshka, Karbassi, Farhad, Issa, Mahmoud Y, van der Lee, Robin, Drögemöller, Britt I, Koster, Janet, Rousseau, Justine, Campeau, Philippe M, Wang, Youdong, Cao, Feng, Li, Meng, Ruiter, Jos, Ciapaite, Jolita, Kluijtmans, Leo A J, Willemsen, Michel A A P, Jans, Judith J, Ross, Colin J, Wintjes, Liesbeth T, Rodenburg, Richard J, Huigen, Marleen C D G, Jia, Zhengping, Waterham, Hans R, Wasserman, Wyeth W, Wanders, Ronald J A, Verhoeven-Duif, Nanda M, Zaki, Maha S, and Wevers, Ron A

Published
2019

17. Integrating glycomics and genomics uncovers SLC10A7 as essential factor for bone mineralization by regulating post-Golgi protein transport and glycosylation

Author

Ashikov, Angel, Bakar, Nurulamin Abu, Wen, Xiao Yan, Niemeijer, Marco, Osorio, Glentino Rodrigues Pinto, Brand-Arzamendi, Koroboshka, Hasadsri, Linda, Hansikova, Hana, Raymond, Kimiyo, Vicogne, Dorothée, Ondruskova, Nina, Simon, Marleen E.H., Pfundt, Rolph, Timal, Sharita, Beumers, Roel, Biot, Christophe, Smeets, Roel, Kersten, Marjan, Huijben, Karin, Linders, Peter T.A., Van Den Bogaart, Geert, Van Hijum, Sacha A.F.T., Rodenburg, Richard, Van Den Heuvel, Lambertus P., Van Spronsen, Francjan, Honzik, Tomas, Foulquier, Francois, Van Scherpenzeel, Monique, Lefeber, Dirk J., Wamelink, Mirjam, Brunner, Han, Mundy, Helen, Michelakakis, Helen, Van Hasselt, Peter, Van De Kamp, Jiddeke, Martinelli, Diego, Morkrid, Lars, Holmefjord, Katja Brocke, Hertecant, Jozef, Alfadhel, Majid, Carpenter, Kevin, Naude, Johann Te Water, and CDG group

Subjects
Genetics, Genetics(clinical), Molecular Biology
Abstract

Genomics methodologies have significantly improved elucidation of Mendelian disorders. The combination with highthroughput functional-omics technologies potentiates the identification and confirmation of causative genetic variants, especially in singleton families of recessive inheritance. In a cohort of 99 individuals with abnormal Golgi glycosylation, 47 of which being unsolved, glycomics profiling was performed of total plasma glycoproteins. Combination with whole-exome sequencing in 31 cases revealed a known genetic defect in 15 individuals. To identify additional genetic factors, hierarchical clustering of the plasma glycomics data was done, which indicated a subgroup of four patients that shared a unique glycomics signature of hybrid type N-glycans. In two siblings, compound heterozygous mutations were found in SLC10A7, a gene of unknown function in human. These included a missense mutation that disrupted transmembrane domain 4 and a mutation in a splice acceptor site resulting in skipping of exon 9. The two other individuals showed a complete loss of SLC10A7 mRNA. The patients' phenotype consisted of amelogenesis imperfecta, skeletal dysplasia, and decreased bone mineral density compatible with osteoporosis. The patients' phenotype was mirrored in SLC10A7 deficient zebrafish. Furthermore, alizarin red staining of calcium deposits in zebrafish morphants showed a strong reduction in bone mineralization. Cell biology studies in fibroblasts of affected individuals showed intracellular mislocalization of glycoproteins and a defect in post-Golgi transport of glycoproteins to the cell membrane. In contrast to yeast, human SLC10A7 localized to the Golgi. Our combined data indicate an important role for SLC10A7 in bone mineralization and transport of glycoproteins to the extracellular matrix.

Published
2018

18. Glutaminase Deficiency Caused by Short Tandem Repeat Expansion in GLS

Author

van Kuilenburg, André B.P., primary, Tarailo-Graovac, Maja, additional, Richmond, Phillip A., additional, Drögemöller, Britt I., additional, Pouladi, Mahmoud A., additional, Leen, René, additional, Brand-Arzamendi, Koroboshka, additional, Dobritzsch, Doreen, additional, Dolzhenko, Egor, additional, Eberle, Michael A., additional, Hayward, Bruce, additional, Jones, Meaghan J., additional, Karbassi, Farhad, additional, Kobor, Michael S., additional, Koster, Janet, additional, Kumari, Daman, additional, Li, Meng, additional, MacIsaac, Julia, additional, McDonald, Cassandra, additional, Meijer, Judith, additional, Nguyen, Charlotte, additional, Rajan-Babu, Indhu-Shree, additional, Scherer, Stephen W., additional, Sim, Bernice, additional, Trost, Brett, additional, Tseng, Laura A., additional, Turkenburg, Marjolein, additional, van Vugt, Joke J.F.A., additional, Veldink, Jan H., additional, Walia, Jagdeep S., additional, Wang, Youdong, additional, van Weeghel, Michel, additional, Wright, Galen E.B., additional, Xu, Xiaohong, additional, Yuen, Ryan K.C., additional, Zhang, Jinqiu, additional, Ross, Colin J., additional, Wasserman, Wyeth W., additional, Geraghty, Michael T., additional, Santra, Saikat, additional, Wanders, Ronald J.A., additional, Wen, Xiao-Yan, additional, Waterham, Hans R., additional, Usdin, Karen, additional, and van Karnebeek, Clara D.M., additional

Published
2019
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19. Zebrafish hhatla is involved in cardiac hypertrophy.

Author

Shi, Xingjuan, Zhang, Yu, Gong, Yijie, Chen, Mengying, Brand‐Arzamendi, Koroboshka, Liu, Xiangdong, and Wen, Xiao‐Yan

Subjects
CARDIAC hypertrophy, BRACHYDANIO, HEART failure, SUDDEN death, ZEBRA danio, CALCINEURIN
Abstract

Cardiac hypertrophy is a compensatory response to pathological stimuli, ultimately progresses to cardiomyopathy, heart failure, or sudden death. Although many signaling pathways have been reported to be involved in the hypertrophic process, it is still not fully clear about the underlying molecular mechanisms for cardiac hypertrophy. Hedgehog acyltransferase‐like (Hhatl), a sarcoplasmic reticulum‐resident protein, exhibits high expression in the heart and muscle. However, the biological role of Hhatl in the heart remains unknown. In this study, we first found that the expression level of Hhatl is markedly decreased in cardiac hypertrophy. We further studied the role of hhatla, homolog of Hhatl with the zebrafish model. The depletion of hhatla in zebrafish leads to cardiac defects, as well as an enhanced level of hypertrophic markers. Besides, we found that calcineurin signaling participates in hhatla depletion‐induced cardiac hypertrophy. Together, these results demonstrate a critical role for hhatla in cardiac hypertrophy. [ABSTRACT FROM AUTHOR]

Published
2021
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20. Integrating glycomics and genomics uncovers SLC10A7 as essential factor for bone mineralization by regulating post-Golgi protein transport and glycosylation

Author

Ashikov, A.M., AbuBakar, N. Bin, Wen, Xiao-Yan, Niemeijer, Marco, Osorio, Glentino Rodrigues Pinto, Brand-Arzamendi, Koroboshka, Pfundt, R.P., Smeets, R.J., Linders, P.T.A., Bogaart, G. van den, Hijum, S.A.F.T. van, Rodenburg, R.J., Heuvel, L.P.W.J. van den, Scherpenzeel, M. van, Lefeber, D.J., Ashikov, A.M., AbuBakar, N. Bin, Wen, Xiao-Yan, Niemeijer, Marco, Osorio, Glentino Rodrigues Pinto, Brand-Arzamendi, Koroboshka, Pfundt, R.P., Smeets, R.J., Linders, P.T.A., Bogaart, G. van den, Hijum, S.A.F.T. van, Rodenburg, R.J., Heuvel, L.P.W.J. van den, Scherpenzeel, M. van, and Lefeber, D.J.

Abstract

Contains fulltext : 195601.pdf (publisher's version ) (Closed access)

Published
2018

21. Integrating glycomics and genomics uncovers SLC10A7 as essential factor for bone mineralization by regulating post-Golgi protein transport and glycosylation

Author

Genetica, Genetica Klinische Genetica, Cluster C, Metabole ziekten patientenzorg, Child Health, Ashikov, Angel, Bakar, Nurulamin Abu, Wen, Xiao Yan, Niemeijer, Marco, Osorio, Glentino Rodrigues Pinto, Brand-Arzamendi, Koroboshka, Hasadsri, Linda, Hansikova, Hana, Raymond, Kimiyo, Vicogne, Dorothée, Ondruskova, Nina, Simon, Marleen E.H., Pfundt, Rolph, Timal, Sharita, Beumers, Roel, Biot, Christophe, Smeets, Roel, Kersten, Marjan, Huijben, Karin, Linders, Peter T.A., Van Den Bogaart, Geert, Van Hijum, Sacha A.F.T., Rodenburg, Richard, Van Den Heuvel, Lambertus P., Van Spronsen, Francjan, Honzik, Tomas, Foulquier, Francois, Van Scherpenzeel, Monique, Lefeber, Dirk J., Wamelink, Mirjam, Brunner, Han, Mundy, Helen, Michelakakis, Helen, Van Hasselt, Peter, Van De Kamp, Jiddeke, Martinelli, Diego, Morkrid, Lars, Holmefjord, Katja Brocke, Hertecant, Jozef, Alfadhel, Majid, Carpenter, Kevin, Naude, Johann Te Water, CDG group, Genetica, Genetica Klinische Genetica, Cluster C, Metabole ziekten patientenzorg, Child Health, Ashikov, Angel, Bakar, Nurulamin Abu, Wen, Xiao Yan, Niemeijer, Marco, Osorio, Glentino Rodrigues Pinto, Brand-Arzamendi, Koroboshka, Hasadsri, Linda, Hansikova, Hana, Raymond, Kimiyo, Vicogne, Dorothée, Ondruskova, Nina, Simon, Marleen E.H., Pfundt, Rolph, Timal, Sharita, Beumers, Roel, Biot, Christophe, Smeets, Roel, Kersten, Marjan, Huijben, Karin, Linders, Peter T.A., Van Den Bogaart, Geert, Van Hijum, Sacha A.F.T., Rodenburg, Richard, Van Den Heuvel, Lambertus P., Van Spronsen, Francjan, Honzik, Tomas, Foulquier, Francois, Van Scherpenzeel, Monique, Lefeber, Dirk J., Wamelink, Mirjam, Brunner, Han, Mundy, Helen, Michelakakis, Helen, Van Hasselt, Peter, Van De Kamp, Jiddeke, Martinelli, Diego, Morkrid, Lars, Holmefjord, Katja Brocke, Hertecant, Jozef, Alfadhel, Majid, Carpenter, Kevin, Naude, Johann Te Water, and CDG group

Published
2018

22. Sialic acid catabolism by N-acetylneuraminate pyruvate lyase is essential for muscle function

Author

Wen, Xiao-Yan, primary, Tarailo-Graovac, Maja, additional, Brand-Arzamendi, Koroboshka, additional, Willems, Anke, additional, Rakic, Bojana, additional, Huijben, Karin, additional, Da Silva, Afitz, additional, Pan, Xuefang, additional, El-Rass, Suzan, additional, Ng, Robin, additional, Selby, Katheryn, additional, Philip, Anju Mary, additional, Yun, Junghwa, additional, Ye, X. Cynthia, additional, Ross, Colin J., additional, Lehman, Anna M., additional, Zijlstra, Fokje, additional, Bakar, A. Abu, additional, Drögemöller, Britt, additional, Moreland, Jacqueline, additional, Wasserman, Wyeth W., additional, Vallance, Hilary, additional, van Scherpenzeel, Monique, additional, Karbassi, Farhad, additional, Hoskings, Martin, additional, Engelke, Udo, additional, de Brouwer, Arjan, additional, Wevers, Ron A., additional, Pshezhetsky, Alexey V., additional, van Karnebeek, Clara D.M., additional, and Lefeber, Dirk J., additional

Published
2018
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24. NANS-mediated synthesis of sialic acid is required for brain and skeletal development

Author

van Karnebeek, Clara D M, Bonafé, Luisa, Wen, Xiao-Yan, Tarailo-Graovac, Maja, Balzano, Sara, Royer-Bertrand, Beryl, Ashikov, Angel, Garavelli, Livia, Mammi, Isabella, Turolla, Licia, Breen, Catherine, Donnai, Dian, Cormier, Valerie, Heron, Delphine, Nishimura, Gen, Uchikawa, Shinichi, Campos-Xavier, Belinda, Rossi, Antonio, Hennet, Thierry, Brand-Arzamendi, Koroboshka, Rozmus, Jacob, Harshman, Keith, Stevenson, Brian J, Girardi, Enrico, Superti-Furga, Giulio, Dewan, Tammie, Collingridge, Alissa, Halparin, Jessie, Ross, Colin J, Van Allen, Margot I, et al, University of Zurich, and van Karnebeek, Clara D M

Subjects
1311 Genetics, 570 Life sciences, biology, 610 Medicine & health, 10052 Institute of Physiology
Published
2016
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25. Erratum: Corrigendum: NANS-mediated synthesis of sialic acid is required for brain and skeletal development

Author

van Karnebeek, Clara D M, primary, Bonafé, Luisa, additional, Wen, Xiao-Yan, additional, Tarailo-Graovac, Maja, additional, Balzano, Sara, additional, Royer-Bertrand, Beryl, additional, Ashikov, Angel, additional, Garavelli, Livia, additional, Mammi, Isabella, additional, Turolla, Licia, additional, Breen, Catherine, additional, Donnai, Dian, additional, Cormier, Valerie, additional, Heron, Delphine, additional, Nishimura, Gen, additional, Uchikawa, Shinichi, additional, Campos-Xavier, Belinda, additional, Rossi, Antonio, additional, Hennet, Thierry, additional, Brand-Arzamendi, Koroboshka, additional, Rozmus, Jacob, additional, Harshman, Keith, additional, Stevenson, Brian J, additional, Girardi, Enrico, additional, Superti-Furga, Giulio, additional, Dewan, Tammie, additional, Collingridge, Alissa, additional, Halparin, Jessie, additional, Ross, Colin J, additional, Van Allen, Margot I, additional, Rossi, Andrea, additional, Engelke, Udo F, additional, Kluijtmans, Leo A J, additional, van der Heeft, Ed, additional, Renkema, Herma, additional, de Brouwer, Arjan, additional, Huijben, Karin, additional, Zijlstra, Fokje, additional, Heisse, Thorben, additional, Boltje, Thomas, additional, Wasserman, Wyeth W, additional, Rivolta, Carlo, additional, Unger, Sheila, additional, Lefeber, Dirk J, additional, Wevers, Ron A, additional, and Superti-Furga, Andrea, additional

Published
2017
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27. NANS-mediated synthesis of sialic acid is required for brain and skeletal development

Author

van Karnebeek, Clara D M, primary, Bonafé, Luisa, additional, Wen, Xiao-Yan, additional, Tarailo-Graovac, Maja, additional, Balzano, Sara, additional, Royer-Bertrand, Beryl, additional, Ashikov, Angel, additional, Garavelli, Livia, additional, Mammi, Isabella, additional, Turolla, Licia, additional, Breen, Catherine, additional, Donnai, Dian, additional, Cormier-Daire, Valérie, additional, Heron, Delphine, additional, Nishimura, Gen, additional, Uchikawa, Shinichi, additional, Campos-Xavier, Belinda, additional, Rossi, Antonio, additional, Hennet, Thierry, additional, Brand-Arzamendi, Koroboshka, additional, Rozmus, Jacob, additional, Harshman, Keith, additional, Stevenson, Brian J, additional, Girardi, Enrico, additional, Superti-Furga, Giulio, additional, Dewan, Tammie, additional, Collingridge, Alissa, additional, Halparin, Jessie, additional, Ross, Colin J, additional, Van Allen, Margot I, additional, Rossi, Andrea, additional, Engelke, Udo F, additional, Kluijtmans, Leo A J, additional, van der Heeft, Ed, additional, Renkema, Herma, additional, de Brouwer, Arjan, additional, Huijben, Karin, additional, Zijlstra, Fokje, additional, Heise, Torben, additional, Boltje, Thomas, additional, Wasserman, Wyeth W, additional, Rivolta, Carlo, additional, Unger, Sheila, additional, Lefeber, Dirk J, additional, Wevers, Ron A, additional, and Superti-Furga, Andrea, additional

Published
2016
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30. Iroquois homeobox gene 3 establishes fast conduction in the cardiac His--Purkinje network.

Author

Shan-Shan Zhang, Kyoung-Han Kim, Rosen, Anna, Smyth, James W., Sakuma, Rui, Delgado-Olguín, Paul, Davis, Mark, Chi, Neil C., Puviindran, Vijitha, Gaborit, Nathalie, Sukonnik, Tatyana, Wylie, John N., Brand-Arzamendi, Koroboshka, Farman, Gerrie P., Jieun Kim, Rose, Robert A., Marsden, Phillip A., Yonghong Zhu, Yu-Qing Zhou, and Lucile Miquerol

Subjects
ELECTRIC properties of heart cells, MORPHOGENESIS -- Molecular aspects, CELL differentiation, PURKINJE cells, HEART physiology
Abstract

Rapid electrical conduction in the His-Purkinje system tightly controls spatiotemporal activation of the ventricles. Although recent work has shed much light on the regulation of early specification and morphogenesis of the His-Purkinje system, less is known about how transcriptional regulation establishes impulse conduction properties of the constituent cells. Here we show that Iroquois homeobox gene 3 (Irx3) is critical for efficient conduction in this specialized tissue by antithetically regulating two gap junction-forming connexins (Cxs). Loss of Irx3 resulted in disruption of the rapid coordinated spread of ventricular excitation, reduced levels of Cx40, and ectopic Cx43 expression in the proximal bundle branches. lrx3 directly represses Cx43 transcription and indirectly activates Cx40 transcription. Our results reveal a critical role for lrx3 in the precise regulation of intercellular gap junction coupling and impulse propagation in the heart. [ABSTRACT FROM AUTHOR]

Published
2011
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31. Corrigendum: NANS-mediated synthesis of sialic acid is required for brain and skeletal development

Author

van Karnebeek, Clara D M, Bonafé, Luisa, Wen, Xiao-Yan, Tarailo-Graovac, Maja, Balzano, Sara, Royer-Bertrand, Beryl, Ashikov, Angel, Garavelli, Livia, Mammi, Isabella, Turolla, Licia, Breen, Catherine, Donnai, Dian, Cormier, Valerie, Heron, Delphine, Nishimura, Gen, Uchikawa, Shinichi, Campos-Xavier, Belinda, Rossi, Antonio, Hennet, Thierry, Brand-Arzamendi, Koroboshka, Rozmus, Jacob, Harshman, Keith, Stevenson, Brian J, Girardi, Enrico, Superti-Furga, Giulio, Dewan, Tammie, Collingridge, Alissa, Halparin, Jessie, Ross, Colin J, Van Allen, Margot I, Rossi, Andrea, Engelke, Udo F, Kluijtmans, Leo A J, van der Heeft, Ed, Renkema, Herma, de Brouwer, Arjan, Huijben, Karin, Zijlstra, Fokje, Heisse, Thorben, Boltje, Thomas, Wasserman, Wyeth W, Rivolta, Carlo, Unger, Sheila, Lefeber, Dirk J, Wevers, Ron A, and Superti-Furga, Andrea

Published
2017
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32. Scoring Central Nervous System Inflammation, Demyelination, and Axon Injury in Experimental Autoimmune Encephalomyelitis.

Author

Ucciferri CC, Gower A, Alvarez-Sanchez N, Whetstone H, Ramaglia V, Gommerman JL, Brand-Arzamendi K, Schneider R, and Dunn SE

Subjects
Mice, Animals, Spinal Cord pathology, Inflammation pathology, Axons pathology, Myelin-Oligodendrocyte Glycoprotein, Mice, Inbred C57BL, Peptide Fragments adverse effects, Encephalomyelitis, Autoimmune, Experimental chemically induced, Multiple Sclerosis pathology
Abstract

Experimental autoimmune encephalomyelitis (EAE) is a common immune-based model of multiple sclerosis (MS). This disease can be induced in rodents by active immunization with protein components of the myelin sheath and Complete Freund's adjuvant (CFA) or by the transfer of myelin-specific T effector cells from rodents primed with myelin protein/CFA into naïve rodents. The severity of EAE is typically scored on a 5-point clinical scale that measures the degree of ascending paralysis, but this scale is not optimal for assessing the extent of recovery from EAE. For example, clinical scores remain high in some EAE models (e.g., myelin oligodendrocyte glycoprotein [MOG] peptide-induced model of EAE) despite the resolution of inflammation. Thus, it is important to complement clinical scoring with histological scoring of EAE, which also provides a means to study the underlying mechanisms of cellular injury in the central nervous system (CNS). Here, a simple protocol is presented to prepare and stain spinal cord and brain sections from mice and to score inflammation, demyelination, and axonal injury in the spinal cord. The method for scoring leukocyte infiltration in the spinal cord can also be applied to score brain inflammation in EAE. A protocol for measuring soluble neurofilament light (sNF-L) in the serum of mice using a Small Molecule Assay (SIMOA) assay is also described, which provides feedback on the extent of overall CNS injury in live mice.

Published
2024
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33. Integrating glycomics and genomics uncovers SLC10A7 as essential factor for bone mineralization by regulating post-Golgi protein transport and glycosylation.

Author

Ashikov A, Abu Bakar N, Wen XY, Niemeijer M, Rodrigues Pinto Osorio G, Brand-Arzamendi K, Hasadsri L, Hansikova H, Raymond K, Vicogne D, Ondruskova N, Simon MEH, Pfundt R, Timal S, Beumers R, Biot C, Smeets R, Kersten M, Huijben K, Linders PTA, van den Bogaart G, van Hijum SAFT, Rodenburg R, van den Heuvel LP, van Spronsen F, Honzik T, Foulquier F, van Scherpenzeel M, Lefeber DJ, Mirjam W, Han B, Helen M, Helen M, Peter VH, Jiddeke VK, Diego M, Lars M, Katja BH, Jozef H, Majid A, Kevin C, and Johann TWN

Subjects
Adult, Animals, Bone Diseases, Developmental metabolism, Bone Diseases, Developmental pathology, Cells, Cultured, Cohort Studies, Exome, Female, Fibroblasts metabolism, Fibroblasts pathology, Glycosylation, Golgi Apparatus metabolism, Golgi Apparatus pathology, Humans, Infant, Male, Organic Anion Transporters, Sodium-Dependent metabolism, Pedigree, Phenotype, Protein Transport, Symporters metabolism, Young Adult, Zebrafish genetics, Zebrafish growth & development, Zebrafish metabolism, Bone Diseases, Developmental etiology, Calcification, Physiologic, Congenital Disorders of Glycosylation complications, Genomics, Glycomics, Mutation, Organic Anion Transporters, Sodium-Dependent genetics, Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase deficiency, Symporters genetics
Abstract

Genomics methodologies have significantly improved elucidation of Mendelian disorders. The combination with high-throughput functional-omics technologies potentiates the identification and confirmation of causative genetic variants, especially in singleton families of recessive inheritance. In a cohort of 99 individuals with abnormal Golgi glycosylation, 47 of which being unsolved, glycomics profiling was performed of total plasma glycoproteins. Combination with whole-exome sequencing in 31 cases revealed a known genetic defect in 15 individuals. To identify additional genetic factors, hierarchical clustering of the plasma glycomics data was done, which indicated a subgroup of four patients that shared a unique glycomics signature of hybrid type N-glycans. In two siblings, compound heterozygous mutations were found in SLC10A7, a gene of unknown function in human. These included a missense mutation that disrupted transmembrane domain 4 and a mutation in a splice acceptor site resulting in skipping of exon 9. The two other individuals showed a complete loss of SLC10A7 mRNA. The patients' phenotype consisted of amelogenesis imperfecta, skeletal dysplasia, and decreased bone mineral density compatible with osteoporosis. The patients' phenotype was mirrored in SLC10A7 deficient zebrafish. Furthermore, alizarin red staining of calcium deposits in zebrafish morphants showed a strong reduction in bone mineralization. Cell biology studies in fibroblasts of affected individuals showed intracellular mislocalization of glycoproteins and a defect in post-Golgi transport of glycoproteins to the cell membrane. In contrast to yeast, human SLC10A7 localized to the Golgi. Our combined data indicate an important role for SLC10A7 in bone mineralization and transport of glycoproteins to the extracellular matrix.

Published
2018
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34. Disruption of pdgfra alters endocardial and myocardial fusion during zebrafish cardiac assembly.

Author

El-Rass S, Eisa-Beygi S, Khong E, Brand-Arzamendi K, Mauro A, Zhang H, Clark KJ, Ekker SC, and Wen XY

Abstract

Cardiac development in vertebrates is a finely tuned process regulated by a set of conserved signaling pathways. Perturbations of these processes are often associated with congenital cardiac malformations. Platelet-derived growth factor receptor α (PDGFRα) is a highly conserved tyrosine kinase receptor, which is essential for development and organogenesis. Disruption of Pdgfrα function in murine models is embryonic lethal due to severe cardiovascular defects, suggesting a role in cardiac development, thus necessitating the use of alternative models to explore its precise function. In this study, we generated a zebrafish pdgfra mutant line by gene trapping, in which the Pdgfra protein is truncated and fused with mRFP (Pdgfra-mRFP). Our results demonstrate that pdgfra mutants have defects in cardiac morphology as a result of abnormal fusion of myocardial precursors. Expression analysis of the developing heart at later stages suggested that Pdgfra-mRFP is expressed in the endocardium. Further examination of the endocardium in pdgfra mutants revealed defective endocardial migration to the midline, where cardiac fusion eventually occurs. Together, our data suggests that pdgfra is required for proper medial migration of both endocardial and myocardial precursors, an essential step required for cardiac assembly and development., (© 2017. Published by The Company of Biologists Ltd.)

Published
2017
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