Primary structure of the helical domain of porcine collagen X

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

    Research output: Contribution to journalArticle

    17 Citations (Scopus)

    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.

    Primary structure of the helical domain of porcine collagen X. / Bos, K J ; Rucklidge, G J ; Dunbar, B ; Robins, S P .

    In: Matrix Biology, Vol. 18, 1999, p. 149-153.

    Research output: Contribution to journalArticle

    Bos, KJ, Rucklidge, GJ, Dunbar, B & Robins, SP 1999, 'Primary structure of the helical domain of porcine collagen X', Matrix Biology, vol. 18, pp. 149-153.
    Bos KJ, Rucklidge GJ, Dunbar B, Robins SP. Primary structure of the helical domain of porcine collagen X. Matrix Biology. 1999;18:149-153.
    Bos, K J ; Rucklidge, G J ; Dunbar, B ; Robins, S P . / Primary structure of the helical domain of porcine collagen X. In: Matrix Biology. 1999 ; Vol. 18. pp. 149-153.
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    AU - Bos, K J

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    AU - Dunbar, B

    AU - Robins, S P

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    AB - 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.

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    KW - glycosylation

    KW - lysine-derived crosslinks

    KW - primary structure

    KW - FIBRIL ASSOCIATION

    KW - CARTILAGE MATRIX

    KW - LOCALIZATION

    KW - TISSUE

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