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Glycosylation and cross-linking in bone type I collagen
Masahiko Terajima1, Irina Perdivara2, Marnisa Sricholpech3
1North Carolina Oral Health Institute, School of Dentistry, University of North Carolina, Chapel Hill, North Carolina 27599.
The Journal of Biological Chemistry
|June 25, 2014
Summary
Glycosylation patterns on collagen hydroxylysine residues differ between non-cross-linked and cross-linked peptides. This suggests glycosylation may regulate collagen cross-link maturation, impacting bone stability.
Area of Science:
- Biochemistry
- Molecular Biology
- Biomineralization
Background:
- Fibrillar type I collagen is essential for bone structure and mineralization.
- Hydroxylysine residues in collagen undergo glycosylation and are critical for cross-linking.
- The role of glycosylation in collagen cross-linking and its impact on stability remain unclear.
Purpose of the Study:
- To quantitatively analyze glycosylation patterns on non-cross-linked and cross-linked collagen peptides.
- To investigate the relationship between glycosylation and collagen cross-link maturation.
- To understand the biological significance of hydroxylysine glycosylation in fibrillar collagens.
Main Methods:
- Biochemical analyses of collagen peptides.
- Nanoscale liquid chromatography-high resolution tandem mass spectrometry (LC-MS/MS).
- Quantitative characterization of glycosylation sites.
Main Results:
- Glycosylation profiles differ significantly between non-cross-linked and cross-linked hydroxylysine residues.
- Divalent cross-links at the α1/2-87 locus are decorated with both mono- and disaccharides.
- Mature trivalent cross-links at this locus are predominantly monoglycosylated, with diminished diglycosylation in type I and II collagens.
Conclusions:
- The extent and pattern of hydroxylysine glycosylation vary depending on the cross-linking state.
- Glycosylation may act as a regulatory mechanism controlling the maturation of collagen cross-links.
- These findings contribute to understanding collagen structure-function relationships in bone.
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