Genre
Journal articleDate
2021-01-04Author
Terajima, MasahikoPerdivara, Irina
Sricholpech, Marnisa
Deguchi, Yoshizumi
Pleshko, Nancy

Tomer, Kenneth B.
Yamauchi, Mitsuo
Group
Tissue Imaging and Spectroscopy Laboratory (Temple University)Department
BioengineeringPermanent link to this record
http://hdl.handle.net/20.500.12613/8395
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https://doi.org/10.1074/jbc.m113.528513Abstract
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.Citation to related work
ElsevierHas part
Journal of Biological Chemistry, Vol. 289, Iss. 33ADA compliance
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http://dx.doi.org/10.34944/dspace/8362