Inhibition of human liver cathepsin L by α2 cysteine-proteinase inhibitor and the low-Mr cysteine proteinase inhibitor from human serum
- 15 May 1984
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 220 (1), 147-155
- https://doi.org/10.1042/bj2200147
Abstract
The inhibition of human liver cathepsin L by two specific proteinase inhibitors present in human serum, namely alpha 2 cysteine-proteinase inhibitor and the low-Mr cysteine-proteinase inhibitor, was studied. Kinetic parameters, including inhibition constants (Ki) and rate constants for association and dissociation (k+1 and K-1), were determined. The values found are consistent with a possible physiological function of these inhibitors to control cathepsin L activity. Furthermore, a transfer of active proteinase from the complex with either cysteine-proteinase inhibitor species to alpha 2-macroglobulin was demonstrated in vitro. Given the rate of dissociation of both cathepsin-L-cysteine-proteinase inhibitor complexes, a function of transitory inhibitor can therefore be hypothesized for these proteins and might then provide an explanation of the clearance of lysosomal proteinases.This publication has 20 references indexed in Scilit:
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