title: [Proteinases and antiproteinases: biomedical correlations].
abstract: Both degradative and limited proteolysis are involved in physiological processes. Once activated, proteinases are controlled by endogenous inhibitors (antiproteinases). A variety of genetic disorders and exogenous microbial proteinases disturb the balance between proteinases and cognate inhibitors. alpha 1-Antitrypsin deficiency is a model disorder resulting in an insufficient control of leukocyte elastase with a subsequent alveolar tissue damage. It appears that the manifold molar excess of inhibitor required to compensate the deficiency, is the consequence of both the local relative inaccessibility of the serpin, and the mode of proteinase-serpin interaction, in accord with the "branched pathway" mechanism. Slow-binding kinetics and the leak of native proteinase from the complex is illustrated by the peptidolytic action of porcine elastase in the presence of human alpha 1-antitrypsin and by gelatin zymography, respectively. (Tab. 2, Fig. 5, Ref. 44.)
authors.affiliation: Dpt of Biochemistry, Faculty of Medicine, Karlovarska 48, CZ-301 66 Plzen, Czech Republic. kotyza@lfp.cuni.cz
authors.forename: J
authors.initials: J
authors.lastname: Kotyza
mesh_terms: D010450:Endopeptidases / Q000378:metabolism*; D011480:Protease Inhibitors / Q000378:metabolism*
chemical_list: D011480:Protease Inhibitors; D010450:Endopeptidases