Identification and partial characterisation of a low Mr collagen synthesised by bovine retinal pericytes: Apparent relationship to type X collagen

A E Canfield, A M Schor

    Research output: Contribution to journalArticlepeer-review

    8 Citations (Scopus)

    Abstract

    Bovine retinal pericytes (BRP) in culture synthesise a low Mr collagenous polypeptide which appears similar, but not identical, to bovine type X collagen and which we have called 'BRP collagen'. This polypeptide displays the following characteristics: (i) it is sensitive to digestion by bacterial collagenase and is resistant to pepsin digestion; (ii) it has an apparent Mr of 45 kDa (pepsinised form); (iii) it is recognised by specific antibodies to type X collagen using immunoblotting; (iv) it is present in the cell layer/matrix but not in the medium of pericyte cultures; and (v) it is not disulphide-bonded into higher Mr multimers. The latter two properties distinguish BRP collagen from bovine type X collagen. We have recently shown that pericytes calcify in vitro. We now report that this calcification is associated with an increased synthesis of BRP collagen.

    Original languageEnglish
    Pages (from-to)171-5
    Number of pages5
    JournalFEBS Letters
    Volume286
    Issue number1-2
    DOIs
    Publication statusPublished - 29 Jul 1991

    Keywords

    • Animals
    • Cattle
    • Cells, Cultured
    • Collagen/analysis
    • Electrophoresis, Polyacrylamide Gel
    • Immunoblotting
    • Molecular Weight
    • Retinal Vessels/chemistry

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