Identification and partial characterisation of a low Mr collagen synthesised by bovine retinal pericytes. Apparent relationship to type X collagen.
AffiliationDepartment of Medical Oncology, Christie Hospital and Holt Radium Institute, Manchester, UK.
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AbstractBovine 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.
CitationIdentification and partial characterisation of a low Mr collagen synthesised by bovine retinal pericytes. Apparent relationship to type X collagen. 1991, 286 (1-2):171-5 FEBS Lett.
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