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

2.50
Hdl Handle:
http://hdl.handle.net/10541/104683
Title:
Identification and partial characterisation of a low Mr collagen synthesised by bovine retinal pericytes. Apparent relationship to type X collagen.
Authors:
Canfield, Ann E; Schor, Ana M
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.
Affiliation:
Department of Medical Oncology, Christie Hospital and Holt Radium Institute, Manchester, UK.
Citation:
Identification 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.
Journal:
FEBS Letters
Issue Date:
29-Jul-1991
URI:
http://hdl.handle.net/10541/104683
DOI:
10.1016/0014-5793(91)80967-8
PubMed ID:
1864364
Type:
Article
Language:
en
ISSN:
0014-5793
Appears in Collections:
All Paterson Institute for Cancer Research

Full metadata record

DC FieldValue Language
dc.contributor.authorCanfield, Ann Een
dc.contributor.authorSchor, Ana Men
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.en
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

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