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Research Article Free access | 10.1172/JCI114215

Evidence for metalloproteinase and metalloproteinase inhibitor imbalance in human osteoarthritic cartilage.

D D Dean, J Martel-Pelletier, J P Pelletier, D S Howell, and J F Woessner Jr

Department of Biochemistry & Molecular Biology, University of Miami School of Medicine, Florida 33101.

Find articles by Dean, D. in: PubMed | Google Scholar

Department of Biochemistry & Molecular Biology, University of Miami School of Medicine, Florida 33101.

Find articles by Martel-Pelletier, J. in: PubMed | Google Scholar

Department of Biochemistry & Molecular Biology, University of Miami School of Medicine, Florida 33101.

Find articles by Pelletier, J. in: PubMed | Google Scholar

Department of Biochemistry & Molecular Biology, University of Miami School of Medicine, Florida 33101.

Find articles by Howell, D. in: PubMed | Google Scholar

Department of Biochemistry & Molecular Biology, University of Miami School of Medicine, Florida 33101.

Find articles by Woessner, J. in: PubMed | Google Scholar

Published August 1, 1989 - More info

Published in Volume 84, Issue 2 on August 1, 1989
J Clin Invest. 1989;84(2):678–685. https://doi.org/10.1172/JCI114215.
© 1989 The American Society for Clinical Investigation
Published August 1, 1989 - Version history
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Abstract

Cartilage specimens from tibial plateaus, obtained from 13 osteoarthritic (OA) patients and seven controls, were selected from three regions: zone A, center of fibrillated area; zone B, area adjacent to fibrillation, and zone C, remote region of plateau. Acid and neutral metalloproteinases and tissue inhibitor of metalloproteinase (TIMP) were extracted with 2 M guanidine. Methods were developed to selectively destroy either proteinases or TIMP to prevent cross-reaction during assay. Acid and neutral proteinases were elevated approximately 150% in OA; TIMP was elevated approximately 50%. A positive correlation (r = 0.50) was found between acid and neutral proteinase activities in OA, but not in controls. Both proteinases were elevated two-to threefold in zones A, B, and C. However, the self-active form of the acid metalloproteinase was elevated only in zones A and B (200%); it correlated well with the Mankin scores, whereas the total activities did not. TIMP was elevated (50%) only in zones A and B. Both the proteinase levels and the Mankin score were elevated to a greater extent in the medial, than in the lateral, compartment. Titration of TIMP against the two metalloproteinases indicates that there is a small excess of inhibitor over enzymes in normal cartilage. In OA, TIMP does not increase to the same extent as the proteinases; the resultant excess of proteinases over TIMP may contribute to cartilage breakdown.

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