Advanced

Cartilage oligomeric matrix protein: isolation and characterization from human articular cartilage

DiCesare, Paul E; Mörgelin, Matthias LU ; Carlson, Cathy S; Pasumarti, Subhalakshmi and Paulsson, Mats (1995) In Journal of Orthopaedic Research 13(3). p.422-428
Abstract
Cartilage oligomeric matrix protein was purified in a native form from normal adult human articular cartilage. The key steps in the purification scheme were selective extraction with buffer containing EDTA, wheat germ agglutinin affinity chromatography, and removal of the related protein thrombospondin by heparin affinity chromatography. Particles of cartilage oligomeric matrix protein viewed by electron microscopy after rotary shadowing revealed structures similar to the prototype molecule purified from Swarm rat chondrosarcoma. The protein demonstrated a bouquet-like five-armed structure, with peripheral globular domains connected by thin flexible strands to a central assembly domain. Immunohistochemistry revealed age-dependent... (More)
Cartilage oligomeric matrix protein was purified in a native form from normal adult human articular cartilage. The key steps in the purification scheme were selective extraction with buffer containing EDTA, wheat germ agglutinin affinity chromatography, and removal of the related protein thrombospondin by heparin affinity chromatography. Particles of cartilage oligomeric matrix protein viewed by electron microscopy after rotary shadowing revealed structures similar to the prototype molecule purified from Swarm rat chondrosarcoma. The protein demonstrated a bouquet-like five-armed structure, with peripheral globular domains connected by thin flexible strands to a central assembly domain. Immunohistochemistry revealed age-dependent differences in the protein's distribution in cartilage. In normal human adult articular cartilage, there was a relatively uniform distribution throughout the interterritorial extracellular matrix, whereas in fetal articular cartilage, immunostaining was localized to the extracellular matrix directly adjacent to the chondrocytes. The isolation and characterization of human cartilage oligomeric matrix protein will facilitate its study in pathological conditions of human 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
Journal of Orthopaedic Research
volume
13
issue
3
pages
422 - 428
publisher
John Wiley & Sons
external identifiers
  • pmid:7602403
  • scopus:0029012466
ISSN
1554-527X
DOI
10.1002/jor.1100130316
language
English
LU publication?
no
id
817d0ef6-e2b1-4471-9bbc-0ca3734d0be6 (old id 1109421)
date added to LUP
2008-07-28 14:27:19
date last changed
2017-09-17 04:52:22
@article{817d0ef6-e2b1-4471-9bbc-0ca3734d0be6,
  abstract     = {Cartilage oligomeric matrix protein was purified in a native form from normal adult human articular cartilage. The key steps in the purification scheme were selective extraction with buffer containing EDTA, wheat germ agglutinin affinity chromatography, and removal of the related protein thrombospondin by heparin affinity chromatography. Particles of cartilage oligomeric matrix protein viewed by electron microscopy after rotary shadowing revealed structures similar to the prototype molecule purified from Swarm rat chondrosarcoma. The protein demonstrated a bouquet-like five-armed structure, with peripheral globular domains connected by thin flexible strands to a central assembly domain. Immunohistochemistry revealed age-dependent differences in the protein's distribution in cartilage. In normal human adult articular cartilage, there was a relatively uniform distribution throughout the interterritorial extracellular matrix, whereas in fetal articular cartilage, immunostaining was localized to the extracellular matrix directly adjacent to the chondrocytes. The isolation and characterization of human cartilage oligomeric matrix protein will facilitate its study in pathological conditions of human cartilage.},
  author       = {DiCesare, Paul E and Mörgelin, Matthias and Carlson, Cathy S and Pasumarti, Subhalakshmi and Paulsson, Mats},
  issn         = {1554-527X},
  language     = {eng},
  number       = {3},
  pages        = {422--428},
  publisher    = {John Wiley & Sons},
  series       = {Journal of Orthopaedic Research},
  title        = {Cartilage oligomeric matrix protein: isolation and characterization from human articular cartilage},
  url          = {http://dx.doi.org/10.1002/jor.1100130316},
  volume       = {13},
  year         = {1995},
}