The new collagenase, collagenase-3, is expressed and synthesized by human chondrocytes but not by synoviocytes. A role in osteoarthritis.
- 1 May 1996
- journal article
- Published by American Society for Clinical Investigation in Journal of Clinical Investigation
- Vol. 97 (9), 2011-2019
- https://doi.org/10.1172/jci118636
Abstract
Recently, a new human collagenase, collagenase-3 has been identified. Since collagen changes are of particular importance in cartilage degeneration, we investigated if collagenase-3 plays a role in osteoarthritis (OA). Reverse transcriptase-PCR analysis revealed that in articular tissues collagenase-3 was expressed by the chondrocytes but not by the synoviocytes. Northern blot analysis of the chondrocyte mRNA revealed the presence of two major gene transcripts of 3.0 and 2.5 kb, and a third one of 2.2 kb was occasionally present. Compared to normal, OA showed a significantly higher (3.0 kb, P < or = 0.05; 2.5 kb, P < or = 0.03) level of collagenase-3 mRNA expression. Collagenase-3 had a higher catalytic velocity tate (about fivefold) than collagenase-1 on type II collagen. With the use of two specific antibodies, we showed that human chondrocytes had the ability to produce collagenase-3 as a proenzyme and as a glycosylated doublet. The chondrocyte collagenase-3 protein is produced in a significantly higher (P < or = 0.04) level in OA (approximately 9.5-fold) than in normal. The synthesis and expression of this new collagenase could also be modulated by two proinflammatory cytokines, IL-1 beta and TNF-alpha, in a time- and dose-dependent manner. This study provides novel and interesting data on collagenase-3 expression and synthesis in human cartilage cells and suggest its involvement in human OA cartilage patho-physiology.This publication has 52 references indexed in Scilit:
- Characterization of Rat Uterine Matrilysin and Its cDNA: RELATIONSHIP TO HUMAN PUMP-1 AND ACTIVATION OF PROCOLLAGENASESPublished by Elsevier ,1995
- Constitutive Production of 92-kDa Gelatinase B Can Be Suppressed by Alterations in Cell ShapeExperimental Cell Research, 1995
- The human collagenase-3 (CLG3) gene is located on chromosome 11q22.3 clustered to other members of the matrix metalloproteinase gene familyGenomics, 1995
- Matrix Metalloproteinase-2 Is an Interstitial CollagenaseJournal of Biological Chemistry, 1995
- Excess of metalloproteases over tissue inhibitor of metalloprotease may contribute to cartilage degradation in osteoarthritis and rheumatoid arthritis.1994
- Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomasJournal of Biological Chemistry, 1994
- Analysis of the role of the COOH-terminal domain in the activation, proteolytic activity, and tissue inhibitor of metalloproteinase interactions of gelatinase B.Journal of Biological Chemistry, 1994
- Increased damage to type II collagen in osteoarthritic articular cartilage detected by a new immunoassay.Journal of Clinical Investigation, 1994
- Differential in vivo expression of collagenase messenger RNA in synovium and cartilage. Quantitative comparison with stromelysin messenger rna levels in human rheumatoid arthritis and osteoarthritis patients and in two animal models of acute inflammatory arthritisArthritis & Rheumatism, 1993
- Localization of matrix metalloproteinase 3 (stromelysin) in osteoarthritic cartilage and synovium.1992