Collagen Accumulation in Osteosarcoma Cells lacking GLT25D1 Collagen Galactosyltransferase
نویسندگان
چکیده
منابع مشابه
Identification of Domains and Amino Acids Essential to the Collagen Galactosyltransferase Activity of GLT25D1
Collagen is modified by hydroxylation and glycosylation of hydroxylysine residues. This glycosylation is initiated by the β1,O galactosyltransferases GLT25D1 and GLT25D2. The structurally similar protein cerebral endothelial cell adhesion molecule CEECAM1 was previously reported to be inactive when assayed for collagen glycosyltransferase activity. To address the cause of the absent galactosylt...
متن کاملCollagen beta (1-O) galactosyltransferase 1 (GLT25D1) is required for the secretion of high molecular weight adiponectin and affects lipid accumulation
Secretion of high molecular weight (HMW) adiponectin is dependent on post-translational modification (PTM) of conserved lysines in the collagenous domain. The present study aims to characterize the enzymes responsible for the PTM of conserved lysines which leads to HMW adiponectin secretion, and to define its significance in relation to obesity. Collagen beta (1-O) galactosyltransferase 1 (GLT2...
متن کاملFibrotic Collagen Accumulation and Immune
Plasma Membrane Overgrowth Causes 1 Fibrotic Collagen Accumulation and Immune 2 Activation in Drosophila Adipocytes 3 4 Yiran Zang, Wan Ming, Min Liu, Hongmei Ke, Shuangchun Ma, Lu-Ping Liu, Jian5 Quan Ni and José Carlos Pastor-Pareja 6 7 Affiliations: 8 1 School of Life Sciences, Tsinghua University, Beijing 100084, China 9 2 Gene Regulatory Lab, School of Medicine, Tsinghua University, Beijin...
متن کاملLymphokine Stimulation of Collagen Accumulation
to cause enhanced collagen accumulation by human embryonic lung fibroblasts (WI-38), as measured by hydroxyproline content of fibroblast monolayers, ["C] proline incorporation into soluble collagen and collagenase release of radioactivity in supernates and monolayers of cultures incubated with ["C] proline. This fibroblaststimulating activity, demonstrable by suitable dilutions of the supernate...
متن کاملStudies on the glycosylation of hydroxylysine residues during collagen biosynthesis and the subcellular localization of collagen galactosyltransferase and collagen glucosyltransferase in tendon and cartilage cells.
1. The glycosylation of hydroxylysine during the biosynthesis of procollagen by embryonic chick tendon and cartilage cells was examined. When free and membrane-bound ribosomes isolated from cells labelled for 4min with [(14)C]lysine were assayed for hydroxy[(14)C]lysine and hydroxy[(14)C]lysine glycosides, it was found that hydroxylation took place only on membrane-bound ribosomes and that some...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2016
ISSN: 0021-9258
DOI: 10.1074/jbc.m116.723379