Vacuolar H+-ATPase meets glycosylation in patients with cutis laxa
| العنوان: | Vacuolar H+-ATPase meets glycosylation in patients with cutis laxa |
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| المؤلفون: | Björn Fischer, Aikaterini Dimopoulou, Uwe Kornak, Eva Morava, Maïlys Guillard, Dirk J. Lefeber, Ron A. Wevers |
| المصدر: | Biochimica et Biophysica Acta. Molecular Basis of Disease, 1792, 903-14 Biochimica et Biophysica Acta. Molecular Basis of Disease, 1792, 9, pp. 903-14 |
| سنة النشر: | 2009 |
| مصطلحات موضوعية: | Models, Molecular, Vacuolar Proton-Translocating ATPases, Glycosylation, Energy and redox metabolism [NCMLS 4], Occipital horn syndrome, OMIM 219200, V-ATPase, Genes, Recessive, Biology, Cutis Laxa, 03 medical and health sciences, chemistry.chemical_compound, Mice, 0302 clinical medicine, Congenital Disorders of Glycosylation, Apolipoprotein C III, medicine, Animals, Humans, Molecular Biology, Gene, 030304 developmental biology, Genetics, 0303 health sciences, Apolipoprotein C-III, Cell Membrane, Transferrin, Glycostation disorders [IGMD 4], medicine.disease, Phenotype, 3. Good health, Protein Subunits, Proton-Translocating ATPases, chemistry, Molecular Medicine, Functional Neurogenomics [DCN 2], 030217 neurology & neurosurgery, Cutis laxa, Subcellular Fractions |
| الوصف: | Contains fulltext : 80992.pdf (Publisher’s version ) (Closed access) Glycosylation of proteins is one of the most important post-translational modifications. Defects in the glycan biosynthesis result in congenital malformation syndromes, also known as congenital disorders of glycosylation (CDG). Based on the iso-electric focusing patterns of plasma transferrin and apolipoprotein C-III a combined defect in N- and O-glycosylation was identified in patients with autosomal recessive cutis laxa type II (ARCL II). Disease-causing mutations were identified in the ATP6V0A2 gene, encoding the a2 subunit of the vacuolar H(+)-ATPase (V-ATPase). The V-ATPases are multi-subunit, ATP-dependent proton pumps located in membranes of cells and organels. In this article, we describe the structure, function and regulation of the V-ATPase and the phenotypes currently known to result from V-ATPase mutations. A clinical overview of cutis laxa syndromes is presented with a focus on ARCL II. Finally, the relationship between ATP6V0A2 mutations, the glycosylation defect and the ARCLII phenotype is discussed. |
| وصف الملف: | application/pdf |
| تدمد: | 0925-4439 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c81bb80275980e7ddd9dc08e12b9f6caTest https://doi.org/10.1016/j.bbadis.2008.12.009Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....c81bb80275980e7ddd9dc08e12b9f6ca |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 09254439 |
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