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Title: | Glycosylation of Type I Collagen |
Authors: | Yamauchi M. Sricholpech M. Terajima M. Tomer K.B. Perdivara I. |
Keywords: | collagen type 1 galactose glucose hydroxyl group hydroxylysine lysine structural protein amino acid collagen type 1 amino acid analysis cell culture cell function collagen synthesis controlled study endoplasmic reticulum enzyme activity high performance liquid chromatography human hydroxylation liquid chromatography-mass spectrometry protein cross linking protein degradation protein glycosylation protein hydrolysis protein processing protein purification quantitative analysis tandem mass spectrometry cell line chemistry glycosylation hydrolysis liquid chromatography mass spectrometry metabolism protein domain Amino Acids Cell Line Chromatography, High Pressure Liquid Chromatography, Liquid Collagen Type I Glycosylation Hydrolysis Hydroxylysine Mass Spectrometry Protein Domains Protein Processing, Post-Translational |
Issue Date: | 2019 |
Abstract: | Fibrillar type I collagen is the most abundant structural protein in most tissues and organs. One of the unique and functionally important characteristics of collagen is sequential posttranslational modifications of lysine (Lys) residues. In the endoplasmic reticulum, hydroxylation of specific Lys occurs producing 5-hydroxylysine (Hyl). Then, to the 5-hydroxyl group of Hyl, a single galactose unit can be attached to form galactosyl-Hyl (Gal-Hyl) and further glucose can be added to Gal-Hyl to form glucosylgalactosyl-Hyl (GlcGal-Hyl). These are the only two O-linked glycosides found in mature type I collagen. It has been shown that this modification is critically involved in a number of biological and pathological processes likely through its regulatory roles in collagen fibrillogenesis, intermolecular cross-linking, and collagen-cell interaction. Recently, with the advances in molecular/cell biology and analytical chemistry, the molecular mechanisms of collagen glycosylation have been gradually deciphered, and the type and extent of glycosylation at the specific molecular loci can now be quantitatively analyzed. In this chapter, we describe quantitative analysis of collagen glycosylation by high-performance liquid chromatography (HPLC) and semiquantitative, site-specific analysis by HPLC-tandem mass spectrometry. © 2019, Springer Science+Business Media, LLC, part of Springer Nature. |
URI: | https://ir.swu.ac.th/jspui/handle/123456789/12672 https://www.scopus.com/inward/record.uri?eid=2-s2.0-85068192939&doi=10.1007%2f978-1-4939-9055-9_9&partnerID=40&md5=00340cfede8a8b7494732036c5cf655a |
ISSN: | 10643745 |
Appears in Collections: | Scopus 1983-2021 |
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