Primary structure of the helical domain of porcine collagen X

K J Bos, G J Rucklidge, B Dunbar, S P Robins

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    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 languageEnglish
    Pages (from-to)149-153
    Number of pages5
    JournalMatrix Biology
    Volume18
    Publication statusPublished - 1999

    Keywords

    • collagen X
    • glycosylation
    • lysine-derived crosslinks
    • primary structure
    • FIBRIL ASSOCIATION
    • CARTILAGE MATRIX
    • LOCALIZATION
    • TISSUE

    Cite this

    Bos, K. J., Rucklidge, G. J., Dunbar, B., & Robins, S. P. (1999). Primary structure of the helical domain of porcine collagen X. Matrix Biology, 18, 149-153.