[CITATION][C] Elastase secreted by activated polymorphonuclear leukocytes causes chondrocyte damage and matrix degradation in intact articular cartilage

J Schalkwijk, LAB Joosten, WB Van den Berg… - Agents and Actions, 1988 - Springer
J Schalkwijk, LAB Joosten, WB Van den Berg, LBA Van de Putte
Agents and Actions, 1988Springer
Leukocyte proteinases have been implied as factors causing tissue damage in various
disorders including lung emphysema and rheumatoid arthritis. Experimental studies have
shown that joint inflammation can cause both degradation of cartilage matrix and inhibition
of chondrocyte biosynthesis [1, 2]. In vitro studies using purified enzymes, often under non-
physiologic conditions, have shown that serine proteases such as elastase and cathepsin-G
are potent cartilage-degrading enzymes [3]. In this study we use activated …
Leukocyte proteinases have been implied as factors causing tissue damage in various disorders including lung emphysema and rheumatoid arthritis. Experimental studies have shown that joint inflammation can cause both degradation of cartilage matrix and inhibition of chondrocyte biosynthesis [1, 2]. In vitro studies using purified enzymes, often under non-physiologic conditions, have shown that serine proteases such as elastase and cathepsin-G are potent cartilage-degrading enzymes [3]. In this study we use activated polymorphonuclear cells (PMNs) as a source of lysosomal proteinases. We applied physiologic conditions (pH, ionic strength) and we tested the effect of alpha-l-proteinase inhibitor (alpha-l-PI) in this system. It is shown that elastase secreted by PMNs causes both matrix degradation and inhibition ofchondrocyte metabolism, even in the presence of a physiologic concentration of alpha-1-PI.
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