Low molecular weight serine proteinase inhibitors of human articular cartilage. Isolation, Characterization, and Biosynthesis
✍ Scribed by John L. Andrews; Peter Ghosh
- Publisher
- John Wiley and Sons
- Year
- 1990
- Tongue
- English
- Weight
- 894 KB
- Volume
- 33
- Category
- Article
- ISSN
- 0004-3591
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✦ Synopsis
The major low molecular weight serine proteinase inhibitor of human articular cartilage was purified to homogeneity as determined by single-peak elution with 4 high resolution techniques. The purified protein was found to be a potent inhibitor of human leukocyte elastase and cathepsin G, as well as the native serine proteinases derived from human articular cartilage and intervertebral disc. The inhibitor and lysozymes were synthesized by human articular cartilage in vitro. These properties and the ability of this cationic inhibitor to bind to cartilage matrix components suggest a possible role in the modulation of matrix catabolism in normal and pathologic states.
Proteolytic degradation of proteoglycans and collagen of the extracellular matrix occurs during a number of pathologic processes. In the inflammatory arthritides, the enzymes responsible for cartilage degradation may be derived from endogenous (14) or exogenous (5-8) sources. While some degree of synovitis may be present in the joints of osteoarthritis patients (9-1 l), a primary event in pathogenesis would appear to be cartilage failure mediated by the neutral metalloproteinases produced by activated chondrocytes (3,12-14). However, these metalloproteinases, From the Raymond Purves Research Laboratories (The University of Sydney) at the Royal North Shore Hospital of Sydney,