Human gelatinase B,a marker enzyme in rheumatoid arthritis,is inhibited by D-penicillamine: Anti-rheumatic activity by protease inhibition |
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Authors: | K. Norga B. Grillet S. Masure L. Paemen G. Opdenakker |
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Affiliation: | (1) From the Rega Institute for Medical Research, Minderbroedersstraat 10, B-3000 Leuven, Belgium;(2) the Division of Rheumatology, Faculty of Medicine, University of Leuven, Belgium |
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Abstract: | Summary The direct and indirect inhibitory potential of D-penicillamine toward human neutrophil and synovial fluid gelatinase B, a marker enzyme for disease severity in RA, was investigated. Gelatinase and plasminogen activator activities were assessed by SDS-polyacrylamide gel electrophoresis zymography. D-penicillamine significantly inhibits purified and synovial fluid gelatinase Bin vitro at concentrations attainablein vivo and also blocksin vitro plasminogen activation. Protease inhibition may be a mechanism of action for D-penicillamine as DMARD. |
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Keywords: | Gelatinase Matrix Metalloproteinases Penicillamine Protease Inhibitor Plasminogen Activator Rheumatoid Arthritis |
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