Cartilage oligomeric matrix protein: isolation and characterization from human articular cartilage
(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:
https://lup.lub.lu.se/record/1109421
- author
- DiCesare, Paul E ; Mörgelin, Matthias LU ; Carlson, Cathy S ; Pasumarti, Subhalakshmi and Paulsson, Mats
- publishing date
- 1995
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Orthopaedic Research
- volume
- 13
- issue
- 3
- pages
- 422 - 428
- publisher
- John Wiley & Sons Inc.
- 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
- 2016-04-01 11:55:15
- date last changed
- 2021-09-12 05:13:31
@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 Inc.}},
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}},
doi = {{10.1002/jor.1100130316}},
volume = {{13}},
year = {{1995}},
}