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

A E Canfield; A M Schor

doi:10.1016/0014-5793(91)80967-8

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

A E Canfield
, A M Schor

Research output: Contribution to journal › Article › peer-review

10 Citations (Scopus)

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.

Original language	English
Pages (from-to)	171-5
Number of pages	5
Journal	FEBS Letters
Volume	286
Issue number	1-2
DOIs	https://doi.org/10.1016/0014-5793(91)80967-8
Publication status	Published - 29 Jul 1991

Keywords

Animals
Cattle
Cells, Cultured
Collagen/analysis
Electrophoresis, Polyacrylamide Gel
Immunoblotting
Molecular Weight
Retinal Vessels/chemistry

Access to Document

10.1016/0014-5793(91)80967-8

Cite this

@article{35f1fd72c3af46a9b94576c72bf4138b,

title = "Identification and partial characterisation of a low Mr collagen synthesised by bovine retinal pericytes: Apparent relationship to type X collagen",

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.",

keywords = "Animals, Cattle, Cells, Cultured, Collagen/analysis, Electrophoresis, Polyacrylamide Gel, Immunoblotting, Molecular Weight, Retinal Vessels/chemistry",

author = "Canfield, \{A E\} and Schor, \{A M\}",

year = "1991",

month = jul,

day = "29",

doi = "10.1016/0014-5793(91)80967-8",

language = "English",

volume = "286",

pages = "171--5",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Wiley",

number = "1-2",

}

TY - JOUR

T1 - Identification and partial characterisation of a low Mr collagen synthesised by bovine retinal pericytes

T2 - Apparent relationship to type X collagen

AU - Canfield, A E

AU - Schor, A M

PY - 1991/7/29

Y1 - 1991/7/29

N2 - 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.

AB - 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.

KW - Animals

KW - Cattle

KW - Cells, Cultured

KW - Collagen/analysis

KW - Electrophoresis, Polyacrylamide Gel

KW - Immunoblotting

KW - Molecular Weight

KW - Retinal Vessels/chemistry

U2 - 10.1016/0014-5793(91)80967-8

DO - 10.1016/0014-5793(91)80967-8

M3 - Article

C2 - 1864364

SN - 0014-5793

VL - 286

SP - 171

EP - 175

JO - FEBS Letters

JF - FEBS Letters

IS - 1-2

ER -

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

Abstract

Keywords

Access to Document

Fingerprint

Cite this