ArticleThe Journal of biological chemistry2014
Glycosylation and cross-linking in bone type I collagen.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed.
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- Farnesyltransferase inhibitors decrease matrix-vesicle-mediated mineralization in SaOS-2 cells.Molecular biology reports · 2025Article
- Proteomic characterization of type I collagen N-terminal crosslinked peptides.Matrix biology plus · 2025Article
- The structural basis for the human procollagen lysine hydroxylation and dual-glycosylation.Nature communications · 2025Article
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- Recent Advances in Nanotechnology-Based Strategies for Bone Tuberculosis Management.Pharmaceuticals (Basel, Switzerland) · 2024Review
- Resveratrol facilitates bone formation in high-glucose conditions.Frontiers in physiology · 2024Article
- Identification of Regulatory Molecular "Hot Spots" for LH/PLOD Collagen Glycosyltransferase Activity.International journal of molecular sciences · 2023Review
- Amino Acid Composition of a Chum Salmon (Foods (Basel, Switzerland) · 2023Article
- Oestrogen and Vibration Improve Intervertebral Disc Cell Viability and Decrease Catabolism in Bovine Organ Cultures.International journal of molecular sciences · 2023Article
- Upregulation of GLT25D1 in Hepatic Stellate Cells Promotes Liver Fibrosis via the TGF-β1/SMAD3 PathwayJournal of clinical and translational hepatology · 2023Article
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- Triple-gene deletion for osteocalcin significantly impairs the alignment of hydroxyapatite crystals and collagen in mice.Frontiers in physiology · 2023Article
- Lysyl hydroxylase 2 mediated collagen post-translational modifications and functional outcomes.Scientific reports · 2022Article
- Experimental and Computational Models of Transport of Galectin-3 Through Glycosylated Matrix.Annals of biomedical engineering · 2022Article
- Intervertebral disc degeneration in warmblood horses: Histological and biochemical characterization.Veterinary pathology · 2022Article
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7 authors.
Funding
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.
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