Advanced

Aggrecan degradation in osteoarthritis and rheumatoid arthritis

Lark, Michael W.; Bayne, Ellen K. and Lohmander, L. Stefan LU (1995) In Acta Orthopaedica 66(S266). p.92-97
Abstract

Aggrecan turnover is critically important to maintain extracellular matrix homeostasis in articular cartilage. Cartilage aggrecan metabolism has been studied in chondrocyte cell cultures, cartilage explant cultures, and in whole animal models. In many of these studies, matrix metalloproteinases (MMPs) are proposed to degrade cartilage aggrecan. MMP expression appears elevated in joint tissues from patients with osteoarthritis (OA) and rheumatoid arthritis (RA) (Dean et al. 1989, Wolfe et al. 1993) and inhibitors of both MMPs and thiol proteinases have been shown to block aggrecan (Buttle et al. 1992) and type II collagen (Mort et al. 1993) degradation in cartilage explant cultures. Using antibodies and cDNA probes, elevations in... (More)

Aggrecan turnover is critically important to maintain extracellular matrix homeostasis in articular cartilage. Cartilage aggrecan metabolism has been studied in chondrocyte cell cultures, cartilage explant cultures, and in whole animal models. In many of these studies, matrix metalloproteinases (MMPs) are proposed to degrade cartilage aggrecan. MMP expression appears elevated in joint tissues from patients with osteoarthritis (OA) and rheumatoid arthritis (RA) (Dean et al. 1989, Wolfe et al. 1993) and inhibitors of both MMPs and thiol proteinases have been shown to block aggrecan (Buttle et al. 1992) and type II collagen (Mort et al. 1993) degradation in cartilage explant cultures. Using antibodies and cDNA probes, elevations in expression and concentration of many of these enzymes in animal models and in OA and RA have been described. Human cartilage aggrecan has now been cloned and sequenced (Doege et al. 1991). This information, in combination with the ability to sequence aggrecan and aggrecan fragments at the protein level, has resulted in the identification of several aggrecan fragments which appear to result from proteinase degradation. In this report, we describe data which suggest that MMPs may in part be responsible for aggrecan catabolism in normal articular cartilage, as well as in the elevated catabolism seen in OA and RA. © 1995 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted.

(Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Acta Orthopaedica
volume
66
issue
S266
pages
6 pages
publisher
Taylor & Francis
external identifiers
  • Scopus:0029385397
ISSN
1745-3674
DOI
10.3109/17453679509157660
language
English
LU publication?
yes
id
42f61329-e53f-46dd-b6f4-83ec15791c65
date added to LUP
2016-05-04 23:47:51
date last changed
2016-07-04 13:56:51
@misc{42f61329-e53f-46dd-b6f4-83ec15791c65,
  abstract     = {<p>Aggrecan turnover is critically important to maintain extracellular matrix homeostasis in articular cartilage. Cartilage aggrecan metabolism has been studied in chondrocyte cell cultures, cartilage explant cultures, and in whole animal models. In many of these studies, matrix metalloproteinases (MMPs) are proposed to degrade cartilage aggrecan. MMP expression appears elevated in joint tissues from patients with osteoarthritis (OA) and rheumatoid arthritis (RA) (Dean et al. 1989, Wolfe et al. 1993) and inhibitors of both MMPs and thiol proteinases have been shown to block aggrecan (Buttle et al. 1992) and type II collagen (Mort et al. 1993) degradation in cartilage explant cultures. Using antibodies and cDNA probes, elevations in expression and concentration of many of these enzymes in animal models and in OA and RA have been described. Human cartilage aggrecan has now been cloned and sequenced (Doege et al. 1991). This information, in combination with the ability to sequence aggrecan and aggrecan fragments at the protein level, has resulted in the identification of several aggrecan fragments which appear to result from proteinase degradation. In this report, we describe data which suggest that MMPs may in part be responsible for aggrecan catabolism in normal articular cartilage, as well as in the elevated catabolism seen in OA and RA. © 1995 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted.</p>},
  author       = {Lark, Michael W. and Bayne, Ellen K. and Lohmander, L. Stefan},
  issn         = {1745-3674},
  language     = {eng},
  number       = {S266},
  pages        = {92--97},
  publisher    = {ARRAY(0x7b3d9a0)},
  series       = {Acta Orthopaedica},
  title        = {Aggrecan degradation in osteoarthritis and rheumatoid arthritis},
  url          = {http://dx.doi.org/10.3109/17453679509157660},
  volume       = {66},
  year         = {1995},
}