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Structure, Specificity And Localization Of The Serine Proteases Of Connective Tissue

R. Woodbury, H. Neurath
Published 1980 · Chemistry, Medicine

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It is the purpose of this review to describe several well characterized proteases present in tissues and cells which appear to be related to the pancreatic serine proteases. Much of the early work concerning the nature of tissue proteases was done during the late 19th century by German physiologists who were studying tissue autolysis [ 11. Hedin and Rowland [2] examined homogenates of various mammalian organs for proteolytic activity and observed that, with the exception of muscle, autolysis was greatest at acid pH. The term ‘cathepsin’ was introduced by Willsttitter and Bamann [3] in 1929 to describe proteolytic activity of tissues in the weakly acid pH range. In recent years, however, this term has sometimes been applied to include tissue proteases in general, such as cathepsin G which has an optimum activity at pH 8 and cathepsin E which is most active at pH 2.5. The rapidly growing literature dealing with tissue and cellular proteases has been recently reviewed by Barrett [4]. respiratory and gastrointestinal diseases [4]. Malignant tissues also show significant changes in proteolytic activity compared to normal, particularly that due to collagenases [ 111. As important as abnormal proteolytic activity in tissues may be in disease states, intraand extracellular proteases are necessary for maintaining normal tissue homeostasis. The steady-state concentration of proteins in cells and tissues is controlled by the rates of their synthesis and degradation [ 12,131 and although lysosomal proteases play a major role in intracellular protein degradation [ 141, there is considerable evidence that other proteases are of equal importance [15].
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