期刊
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE
卷 1792, 期 9, 页码 903-914出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbadis.2008.12.009
关键词
Glycosylation; Cutis laxa; V-ATPase; Congenital disorders of glycosylation; OMIM 219200; Apolipoprotein C III
资金
- European Commission [LSHM-CT2005-512131]
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 ATP6VOA2 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 ATP6VOA2 mutations, the glycosylation defect and the ARCLII phenotype is discussed. (C) 2009 Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据