Identification and partial characterisation of a low Mr collagen synthesised by bovine retinal pericytes. Apparent relationship to type X collagen.
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.
Canfield
A E
AE
Department of Medical Oncology, Christie Hospital and Holt Radium Institute, Manchester, UK.
Schor
A M
AM
D000818:Animals; D002417:Cattle; D002478:Cells, Cultured; D003094:Collagen / Q000032:analysis* / Q000096:biosynthesis; D004591:Electrophoresis, Polyacrylamide Gel; D015151:Immunoblotting; D008970:Molecular Weight; D012171:Retinal Vessels / Q000737:chemistry* / Q000166:cytology / Q000378:metabolism
D003094:Collagen