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  • Title: Levels of metalloproteases and tissue inhibitor of metalloproteases in human osteoarthritic cartilage.
    Author: Dean DD, Azzo W, Martel-Pelletier J, Pelletier JP, Woessner JF.
    Journal: J Rheumatol; 1987 May; 14 Spec No():43-4. PubMed ID: 3305939.
    Abstract:
    Human articular cartilage contains 2 distinct metalloproteases which degrade proteoglycan. One protease acts optimally at pH 5.3 and the other at pH 7.2. In addition, cartilage contains a tissue inhibitor of metalloproteases (TIMP) that inhibits both proteases. Methods have been developed for the estimation of metalloproteases and TIMP in extracts of cartilage prepared in buffered 2 M guanidine-HCl. In osteoarthritic cartilage, levels of the 2 metalloproteases increase 3-fold or more, while the level of TIMP remains constant. It is postulated that a balance is maintained between inhibitor and metalloprotease levels in normal cartilage and that in osteoarthritis increased secretion of proteases upsets this balance and results in degradation of the extracellular matrix.
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