help button home button Am J Pathol ASIP 2008 Summer Academy, Molecular Methcanisms of Human Disease: Injury, Inflammation, and Tissue Repair
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS

This Article
Right arrow Order Full text via Infotrieve
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hembry, R. M.
Right arrow Articles by Reynolds, J. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hembry, R. M.
Right arrow Articles by Reynolds, J. J.

American Journal of Pathology, Vol 143, 628-642, Copyright © 1993 by American Society for Investigative Pathology


REGULAR ARTICLES

Rabbit models of arthritis: immunolocalization of matrix metalloproteinases and tissue inhibitor of metalloproteinase in synovium and cartilage

RM Hembry, MR Bagga, G Murphy, B Henderson and JJ Reynolds
Cell and Molecular Biology Department, Strangeways Research Laboratory, Cambridge, England.

The distribution of the matrix metalloproteinases, collagenase, stromelysin, gelatinases A and B, and the tissue inhibitor of metalloproteinases in cartilage and synovium removed from rabbits up to 27 days after induction of two models of arthritis was investigated by immunolocalization. Following intra-articular injection of poly-D- lysine/hyaluronic acid coacervate, collagenase and stromelysin were found bound to cartilage matrix, but there was little increase in chondrocyte synthesis of these enzymes. The synovium underwent a complex wound healing response involving invagination and encapsulation of the coacervate and inflammatory cell debris, during which all four metalloproteinases and tissue inhibitor of metalloproteinase could be immunolocalized. The second model, intra-articular injection of ovalbumin into sensitized rabbits, caused considerable chondrocyte necrosis; collagenase was found bound to cartilage matrix on day 13, although again there was little evidence of synthesis by chondrocytes. Inflammatory cell infiltration of meniscoid synovia took place initially, followed by fibrosis involving macrophagelike cells secreting gelatinase A. In both models there was rapid loss of glycosaminoglycan metachromasia from the cartilage matrix. These results are discussed in relation to current knowledge of metalloproteinase involvement in the chronic rheumatoid synovial pannus erosion of cartilage in humans. The data suggest that there are considerable differences between rheumatoid arthritis and these models, and their use must therefore be carefully defined.


This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
N. C. M. Caterina, L. J. Windsor, A. E. Yermovsky, M. K. Bodden, K. B. Taylor, H. Birkedal-Hansen, and J. A. Engler
Replacement of Conserved Cysteines in Human Tissue Inhibitor of Metalloproteinases-1
J. Biol. Chem., December 19, 1997; 272(51): 32141 - 32149.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
E. Guerin, M.-G. Ludwig, P. Basset, and P. Anglard
Stromelysin-3 Induction and Interstitial Collagenase Repression by Retinoic Acid. THERAPEUTICAL IMPLICATION OF RECEPTOR-SELECTIVE RETINOIDS DISSOCIATING TRANSACTIVATION AND AP-1-MEDIATED TRANSREPRESSION
J. Biol. Chem., April 25, 1997; 272(17): 11088 - 11095.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
P. Hill, G Murphy, A. Docherty, R. Hembry, T. Millican, J. Reynolds, and M. Meikle
The effects of selective inhibitors of matrix metalloproteinases (MMPs) on bone resorption and the identification of MMPs and TIMP-1 in isolated osteoclasts
J. Cell Sci., January 11, 1994; 107(11): 3055 - 3064.
[Abstract] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1993 by the American Society for Investigative Pathology.