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

FEBS Letters

Schor, A.M.¹  Canfield, A.E.¹ 

[1] Cancer Research Campaign Department of Medical Oncology, Christie Hospital and Holt Radium Institute, Manchester, M20 9BX, UK

关键词: Collagen;    Pericyte;    Calcification;   

DOI  :  10.1016/0014-5793(91)80967-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Bovine retinal pericytes (BRP) in culture synthesise a low M _r 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 M _r 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 M _r 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.

【 授权许可】

Unknown