Publication: Glycosylation and cross-linking in bone type I collagen
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0
Issued Date
2014
Resource Type
File Type
application/pdf
ISSN
219258
Other identifier(s)
2-s2.0-84905994030
Rights Holder(s)
Scopus
Bibliographic Citation
Journal of Biological Chemistry. Vol 289, No.33 (2014), p.22636-22647
Suggested Citation
Terajima M., Perdivara I., Sricholpech M., Deguchi Y., Pleshko N., Tomer K.B., Yamauchi M. Glycosylation and cross-linking in bone type I collagen. Journal of Biological Chemistry. Vol 289, No.33 (2014), p.22636-22647. doi:10.1074/jbc.M113.528513 Retrieved from: https://hdl.handle.net/20.500.14740/6284
Abstract
Fibrillar type I collagen is the major organic component in bone, providing a stable template for mineralization. During collagen biosynthesis, specific hydroxylysine residues become glycosylated in the form of galactosyl- and glucosylgalactosyl-hydroxylysine. Furthermore, key glycosylated hydroxylysine residues, α1/2-87, are involved in covalent intermolecular cross-linking. Although cross-linking is crucial for the stability and mineralization of collagen, the biological function of glycosylation in cross-linking is not well understood. In this study, we quantitatively characterized glycosylation of non-cross-linked and cross-linked peptides by biochemical and nanoscale liquid chromatography-high resolution tandem mass spectrometric analyses. The results showed that glycosylation of non-cross-linked hydroxylysine is different from that involved in cross-linking. Among the cross-linked species involving α1/2-87, divalent cross-links were glycosylated with both mono- and disaccharides, whereas the mature, trivalent cross-links were primarily monoglycosylated. Markedly diminished diglycosylation in trivalent cross-links at this locus was also confirmed in type II collagen. The data, together with our recent report (Sricholpech, M., Perdivara, I., Yokoyama, M., Nagaoka, H., Terajima, M., Tomer, K. B., and Yamauchi, M. (2012) Lysyl hydroxylase 3-mediated glucosylation in type I collagen: molecular loci and biological significance. J. Biol. Chem. 287, 22998-23009), indicate that the extent and pattern of glycosylation may regulate cross-link maturation in fibrillar collagen.
Subject(s)
Bone
Collagen
Esterification
Liquid chromatography
Mineralogy
Biological functions
Biological significance
Fibrillar collagens
Intermolecular crosslinking
Mono- and disaccharides
Organic components
Tandem mass spectrometric analysis
Type II collagens
Glycosylation
Collagen type 1
Collagen type 2
Disaccharide
Hydroxylysine
Lysyl hydroxylase 3
Monosaccharide
Oxygenase
Unclassified drug
Collagen type 1
Hydroxylysine
Animal tissue
Article
Bone
Enzyme activity
Glycosylation
Liquid chromatography
Nonhuman
Priority journal
Protein cross linking
Protein glycosylation
Protein structure
Tandem mass spectrometry
Animal
Bone
Bovinae
Chemistry
Mass spectrometry
Protein stability
Animals
Bone and Bones
Cattle
Chromatography, Liquid
Collagen Type I
Glycosylation
Hydroxylysine
Mass Spectrometry
Protein Stability
Collagen
Esterification
Liquid chromatography
Mineralogy
Biological functions
Biological significance
Fibrillar collagens
Intermolecular crosslinking
Mono- and disaccharides
Organic components
Tandem mass spectrometric analysis
Type II collagens
Glycosylation
Collagen type 1
Collagen type 2
Disaccharide
Hydroxylysine
Lysyl hydroxylase 3
Monosaccharide
Oxygenase
Unclassified drug
Collagen type 1
Hydroxylysine
Animal tissue
Article
Bone
Enzyme activity
Glycosylation
Liquid chromatography
Nonhuman
Priority journal
Protein cross linking
Protein glycosylation
Protein structure
Tandem mass spectrometry
Animal
Bone
Bovinae
Chemistry
Mass spectrometry
Protein stability
Animals
Bone and Bones
Cattle
Chromatography, Liquid
Collagen Type I
Glycosylation
Hydroxylysine
Mass Spectrometry
Protein Stability