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Cartilage oligomeric matrix protein and thrombospondin 1. Purification from articular cartilage, electron microscopic structure, and chondrocyte binding

DiCesare, P E; Mörgelin, Matthias LU ; Mann, K and Paulsson, M (1994) In European Journal of Biochemistry 223(3). p.927-937
Abstract
Cartilage oligomeric matrix protein (COMP) and thrombospondin 1 (TSP1) were purified in a native form from normal bovine articular cartilage. The key step in the purification scheme was selective extraction with EDTA-containing buffer. Final separation of these two molecules was achieved by heparin affinity chromatography. Particles viewed by electron microscopy after rotary shadowing and negative staining revealed structures similar to their prototype molecules; from the Swarm rat chondrosarcoma for COMP, or from platelets for TSP1. Attachment of primary bovine chondrocytes to purified matrix proteins was investigated. Cells attached to COMP but not to the structurally related TSP1 indicating separate functions for these proteins in... (More)
Cartilage oligomeric matrix protein (COMP) and thrombospondin 1 (TSP1) were purified in a native form from normal bovine articular cartilage. The key step in the purification scheme was selective extraction with EDTA-containing buffer. Final separation of these two molecules was achieved by heparin affinity chromatography. Particles viewed by electron microscopy after rotary shadowing and negative staining revealed structures similar to their prototype molecules; from the Swarm rat chondrosarcoma for COMP, or from platelets for TSP1. Attachment of primary bovine chondrocytes to purified matrix proteins was investigated. Cells attached to COMP but not to the structurally related TSP1 indicating separate functions for these proteins in cartilage. (Less)
Please use this url to cite or link to this publication:
author
publishing date
type
Contribution to journal
publication status
published
subject
in
European Journal of Biochemistry
volume
223
issue
3
pages
927 - 937
publisher
Wiley-Blackwell
external identifiers
  • pmid:8055970
  • scopus:0028064807
ISSN
0014-2956
DOI
10.1111/j.1432-1033.1994.tb19070.x
language
English
LU publication?
no
id
09b0b378-73b2-4541-8dbf-75b8d2cd066f (old id 1108341)
date added to LUP
2008-07-23 17:27:06
date last changed
2017-04-09 04:23:51
@article{09b0b378-73b2-4541-8dbf-75b8d2cd066f,
  abstract     = {Cartilage oligomeric matrix protein (COMP) and thrombospondin 1 (TSP1) were purified in a native form from normal bovine articular cartilage. The key step in the purification scheme was selective extraction with EDTA-containing buffer. Final separation of these two molecules was achieved by heparin affinity chromatography. Particles viewed by electron microscopy after rotary shadowing and negative staining revealed structures similar to their prototype molecules; from the Swarm rat chondrosarcoma for COMP, or from platelets for TSP1. Attachment of primary bovine chondrocytes to purified matrix proteins was investigated. Cells attached to COMP but not to the structurally related TSP1 indicating separate functions for these proteins in cartilage.},
  author       = {DiCesare, P E and Mörgelin, Matthias and Mann, K and Paulsson, M},
  issn         = {0014-2956},
  language     = {eng},
  number       = {3},
  pages        = {927--937},
  publisher    = {Wiley-Blackwell},
  series       = {European Journal of Biochemistry},
  title        = {Cartilage oligomeric matrix protein and thrombospondin 1. Purification from articular cartilage, electron microscopic structure, and chondrocyte binding},
  url          = {http://dx.doi.org/10.1111/j.1432-1033.1994.tb19070.x},
  volume       = {223},
  year         = {1994},
}