Abstract
The entire primary structure of the collagen X helical region is presented, including identification of the extensive post-ribosomal modifications by amino acid sequencing and mass spectrometry. As in collagen I, a single residue of 3-hydroxyproline was identified, but for collagen X this was located near the N-terminal end of the helix. Lysine residues in collagen X are extensively hydroxylated/glycosylated: at least 11 sites were localized and shown to be fully glycosylated, exclusively as glucosyl-galactosyl derivatives. The lysine-derived crosslinks, dihydroxylysinonorleucine and hydroxylysinonorleucine, were shown to be present in a 3:2 molar ratio primarily within the C-terminal portion of the helix. (C) 1999 Elsevier Science B.V./International Society of Matrix Biology. All rights reserved.
Original language | English |
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Pages (from-to) | 149-153 |
Number of pages | 5 |
Journal | Matrix Biology |
Volume | 18 |
Publication status | Published - 1999 |
Keywords
- collagen X
- glycosylation
- lysine-derived crosslinks
- primary structure
- FIBRIL ASSOCIATION
- CARTILAGE MATRIX
- LOCALIZATION
- TISSUE