Abstract
One of the most surprising features of living systems is their use of proteases for many physiological functions apart from digestion of food, for when protease function becomes uncontrolled, cell autolysis occurs, with widespread destruction of tissues and later death of the organism. In cells proteases are segregated in special compartments, lysosomes, which offer partial protection for the rest of the cell contents. But the frequency of entry of proteases into the blood stream and their utilisation for a number of protective functions show that compartmentation is not necessary for controlled action of proteases. Control of protease action in the plasma depends on (a) localisation of the site of release of the protease, (b) the control of the amount released and (c) the control of the duration of action of the protease. Here we are only concerned with (c). A major feature controlling the duration of action of proteases in the circulation is reaction with protease inhibitors. The importance of these is well illustrated by the effects of genetic abnormalities which reduce levels or activity of circulating antiproteases. Thus, a low level of alpha-1 proteinase inhibitor is often associated with emphysema, probably from alveolar destruction by white cell elastases1; a low level of Cī inhibitor, with recurrent attacks of angioneurotic oedema2; and a low level of antithrombin III (AT), with recurrent attacks of deep venous thrombosis3,4.
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References
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Reeve, E.B., Bies, R.D., Leonard, B.D., Stephens, A. (1984). Studies of antithrombin turnover. In: Mariani, G. (eds) Pathophysiology of Plasma Protein Metabolism. Palgrave, London. https://doi.org/10.1007/978-1-349-06680-3_14
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DOI: https://doi.org/10.1007/978-1-349-06680-3_14
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