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Interaction of cartilage matrix protein with aggrecan. Increased covalent cross-linking with tissue maturation

Hauser, Nik; Paulsson, Mats; Heinegård, Dick LU and Mörgelin, Matthias LU (1996) In Journal of Biological Chemistry 271(50). p.32247-32252
Abstract
Cartilage matrix protein (CMP) is a trimeric protein present in many types of cartilage extracellular matrix. It has recently been purified under native conditions that allowed the proposal of a structural model (Hauser, N., and Paulsson, M. (1994) J. Biol. Chem. 269, 25747-25753). To examine the functional properties of CMP we studied its interaction with aggrecan within cartilage extracellular matrix. Aggrecan-enriched fractions were purified from bovine tracheal cartilage of different ages under nondenaturing and denaturing conditions, respectively, and characterized by a combination of biochemical methods and electron microscopy. The fractions contained a pool of CMP noncovalently associated with aggrecan as well as a pool of CMP that... (More)
Cartilage matrix protein (CMP) is a trimeric protein present in many types of cartilage extracellular matrix. It has recently been purified under native conditions that allowed the proposal of a structural model (Hauser, N., and Paulsson, M. (1994) J. Biol. Chem. 269, 25747-25753). To examine the functional properties of CMP we studied its interaction with aggrecan within cartilage extracellular matrix. Aggrecan-enriched fractions were purified from bovine tracheal cartilage of different ages under nondenaturing and denaturing conditions, respectively, and characterized by a combination of biochemical methods and electron microscopy. The fractions contained a pool of CMP noncovalently associated with aggrecan as well as a pool of CMP that appears covalently cross-linked to the aggrecan core protein. Only about two thirds of the CMP subunits could be released even upon reduction under denaturing conditions. It appears that CMP is attached by a nonreducible covalent interaction of one of its subunits with the protein core. The amount of CMP strongly bound to aggrecan increases with age. Electron microscopy revealed interaction sites for CMP in the extended chondroitin-sulfate attachment domain E2. In old tissue five distinct binding sites for CMP were found while in young cartilage only three of these were occupied. The extent of decoration of E2 with CMP increases with age. (Less)
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author
organization
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type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
271
issue
50
pages
32247 - 32252
publisher
ASBMB
external identifiers
  • pmid:8943283
  • scopus:0029752015
ISSN
1083-351X
language
English
LU publication?
yes
id
7a09f475-f1e0-4aa7-9b58-bbd8295adc9d (old id 1110698)
alternative location
http://www.jbc.org/cgi/content/full/271/50/32247
date added to LUP
2008-07-23 11:20:35
date last changed
2017-08-06 03:35:40
@article{7a09f475-f1e0-4aa7-9b58-bbd8295adc9d,
  abstract     = {Cartilage matrix protein (CMP) is a trimeric protein present in many types of cartilage extracellular matrix. It has recently been purified under native conditions that allowed the proposal of a structural model (Hauser, N., and Paulsson, M. (1994) J. Biol. Chem. 269, 25747-25753). To examine the functional properties of CMP we studied its interaction with aggrecan within cartilage extracellular matrix. Aggrecan-enriched fractions were purified from bovine tracheal cartilage of different ages under nondenaturing and denaturing conditions, respectively, and characterized by a combination of biochemical methods and electron microscopy. The fractions contained a pool of CMP noncovalently associated with aggrecan as well as a pool of CMP that appears covalently cross-linked to the aggrecan core protein. Only about two thirds of the CMP subunits could be released even upon reduction under denaturing conditions. It appears that CMP is attached by a nonreducible covalent interaction of one of its subunits with the protein core. The amount of CMP strongly bound to aggrecan increases with age. Electron microscopy revealed interaction sites for CMP in the extended chondroitin-sulfate attachment domain E2. In old tissue five distinct binding sites for CMP were found while in young cartilage only three of these were occupied. The extent of decoration of E2 with CMP increases with age.},
  author       = {Hauser, Nik and Paulsson, Mats and Heinegård, Dick and Mörgelin, Matthias},
  issn         = {1083-351X},
  language     = {eng},
  number       = {50},
  pages        = {32247--32252},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Interaction of cartilage matrix protein with aggrecan. Increased covalent cross-linking with tissue maturation},
  volume       = {271},
  year         = {1996},
}