Association of chondroadherin with collagen type II
Månsson, Bengt LU
; Wenglén, Christina
LU
; Mörgelin, Matthias
LU
; Saxne, Tore
LU
and Heinegård, Dick
LU
(2001)
In Journal of Biological Chemistry
276(35).
p.32883-32888
- Abstract
- Chondroadherin is a cell binding, leucine-rich repeat protein found in the territorial matrix of articular cartilage. Several members of the leucine-rich repeat protein family present in the extracellular matrix of e.g. cartilage have been shown to interact with collagen and influence collagen fibrillogenesis. We show that complexes of monomeric collagen type II and chondroadherin can be released under non-denaturing conditions from articular cartilage treated with p-aminophenylmercuric acetate to activate resident matrix metalloproteinases. Purified complexes as well as complexes formed in vitro between recombinant chondroadherin and collagen type II were studied by electron microscopy. Chondroadherin was shown to bind to two sites on... (More)
- Chondroadherin is a cell binding, leucine-rich repeat protein found in the territorial matrix of articular cartilage. Several members of the leucine-rich repeat protein family present in the extracellular matrix of e.g. cartilage have been shown to interact with collagen and influence collagen fibrillogenesis. We show that complexes of monomeric collagen type II and chondroadherin can be released under non-denaturing conditions from articular cartilage treated with p-aminophenylmercuric acetate to activate resident matrix metalloproteinases. Purified complexes as well as complexes formed in vitro between recombinant chondroadherin and collagen type II were studied by electron microscopy. Chondroadherin was shown to bind to two sites on collagen type II. The interaction was characterized by surface plasmon resonance analysis showing K(D) values in the nanomolar range. Both chondroadherin and collagen interact with chondrocytes, partly via the same receptor, but give rise to different cellular responses. By also interacting with each other, a complex system is created which may be of functional importance for the communication between the cells and its surrounding matrix and/or in the regulation of collagen fibril assembly. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1121080
- author
- Månsson, Bengt
LU
; Wenglén, Christina
LU
; Mörgelin, Matthias
LU
; Saxne, Tore
LU
and Heinegård, Dick
LU
- organization
- publishing date
- 2001
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 276
- issue
- 35
- pages
- 32883 - 32888
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- pmid:11445564
- scopus:0035980090
- pmid:11445564
- ISSN
- 1083-351X
- DOI
- 10.1074/jbc.M101680200
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Connective Tissue Biology (013230151), Division of Infection Medicine (BMC) (013024020)
- id
- 3094a151-3926-413a-8215-037bad539a24 (old id 1121080)
- date added to LUP
- 2016-04-01 11:53:48
- date last changed
- 2022-01-26 19:53:47
@article{3094a151-3926-413a-8215-037bad539a24,
abstract = {{Chondroadherin is a cell binding, leucine-rich repeat protein found in the territorial matrix of articular cartilage. Several members of the leucine-rich repeat protein family present in the extracellular matrix of e.g. cartilage have been shown to interact with collagen and influence collagen fibrillogenesis. We show that complexes of monomeric collagen type II and chondroadherin can be released under non-denaturing conditions from articular cartilage treated with p-aminophenylmercuric acetate to activate resident matrix metalloproteinases. Purified complexes as well as complexes formed in vitro between recombinant chondroadherin and collagen type II were studied by electron microscopy. Chondroadherin was shown to bind to two sites on collagen type II. The interaction was characterized by surface plasmon resonance analysis showing K(D) values in the nanomolar range. Both chondroadherin and collagen interact with chondrocytes, partly via the same receptor, but give rise to different cellular responses. By also interacting with each other, a complex system is created which may be of functional importance for the communication between the cells and its surrounding matrix and/or in the regulation of collagen fibril assembly.}},
author = {{Månsson, Bengt and Wenglén, Christina and Mörgelin, Matthias and Saxne, Tore and Heinegård, Dick}},
issn = {{1083-351X}},
language = {{eng}},
number = {{35}},
pages = {{32883--32888}},
publisher = {{American Society for Biochemistry and Molecular Biology}},
series = {{Journal of Biological Chemistry}},
title = {{Association of chondroadherin with collagen type II}},
url = {{http://dx.doi.org/10.1074/jbc.M101680200}},
doi = {{10.1074/jbc.M101680200}},
volume = {{276}},
year = {{2001}},
}