Show simple item record

dc.contributor.authorCanfield, Ann E
dc.contributor.authorSchor, Ana M
dc.date.accessioned2010-06-11T10:46:44Z
dc.date.available2010-06-11T10:46:44Z
dc.date.issued1991-07-29
dc.identifier.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.en
dc.identifier.issn0014-5793
dc.identifier.pmid1864364
dc.identifier.doi10.1016/0014-5793(91)80967-8
dc.identifier.urihttp://hdl.handle.net/10541/104683
dc.description.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.
dc.language.isoenen
dc.subject.meshAnimals
dc.subject.meshCattle
dc.subject.meshCells, Cultured
dc.subject.meshCollagen
dc.subject.meshElectrophoresis, Polyacrylamide Gel
dc.subject.meshImmunoblotting
dc.subject.meshMolecular Weight
dc.subject.meshRetinal Vessels
dc.titleIdentification and partial characterisation of a low Mr collagen synthesised by bovine retinal pericytes. Apparent relationship to type X collagen.en
dc.typeArticleen
dc.contributor.departmentDepartment of Medical Oncology, Christie Hospital and Holt Radium Institute, Manchester, UK.en
dc.identifier.journalFEBS Lettersen
html.description.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.


Files in this item

This item appears in the following Collection(s)

Show simple item record