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Research Article Free access | 10.1172/JCI116547

Expression of 92-kD type IV collagenase/gelatinase (gelatinase B) in osteoarthritic cartilage and its induction in normal human articular cartilage by interleukin 1.

M Mohtai, R L Smith, D J Schurman, Y Tsuji, F M Torti, N I Hutchinson, W G Stetler-Stevenson, and G I Goldberg

Department of Functional Restoration, Stanford University School of Medicine, California 94305.

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Department of Functional Restoration, Stanford University School of Medicine, California 94305.

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Department of Functional Restoration, Stanford University School of Medicine, California 94305.

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Department of Functional Restoration, Stanford University School of Medicine, California 94305.

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Department of Functional Restoration, Stanford University School of Medicine, California 94305.

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Department of Functional Restoration, Stanford University School of Medicine, California 94305.

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Department of Functional Restoration, Stanford University School of Medicine, California 94305.

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Department of Functional Restoration, Stanford University School of Medicine, California 94305.

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Published July 1, 1993 - More info

Published in Volume 92, Issue 1 on July 1, 1993
J Clin Invest. 1993;92(1):179–185. https://doi.org/10.1172/JCI116547.
© 1993 The American Society for Clinical Investigation
Published July 1, 1993 - Version history
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Abstract

We report here that a 92-kD gelatinolytic metalloproteinase is expressed as protein and mRNA in human osteoarthritic cartilage, but not in normal adult articular cartilage. Western immunoblotting demonstrated that the 92-kD gelatinolytic activity corresponded to 92-kD type IV collagenase/gelatinase (gelatinase B); mRNA for gelatinase B was identified by Northern blotting. Chondrocytes from normal cartilage also exhibited mRNA for 72-kD type IV collagenase/gelatinase (gelatinase A), tissue collagenase, and stromelysin-1, and these mRNAs were increased in osteoarthritic cartilage. Regional analysis of osteoarthritic cartilage samples from four individuals revealed that gelatinase B mRNA was expressed in grossly fibrillated areas; two of four nonfibrillated cartilage samples failed to exhibit the mRNA, but did have increased levels of mRNA for other neutral metalloproteinases. IL-1 alpha treatment of normal human cartilage explants or isolated chondrocytes induced increased levels of gelatinase B and increased mRNA for tissue collagenase and stromelysin-1. Under identical conditions, mRNA levels for gelatinase A were not increased indicating that regulation of this enzyme in human articular chondrocytes is distinct from that of other metalloproteinases. Our data showing expression of gelatinase B in fibrillated cartilage suggest that it is a marker of progressive articular cartilage degradation in osteoarthritis.

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