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- W1759884410 abstract "The bait region of the general protease inhibitor α2-macroglobulin (α2M) was mutated by introducing a recognition sequence of furin. This did not interfere with folding, S-ester formation or tetramerization of the mutant recombinant α2M (rα2M). Mutant rα2M inhibited furin in vitro, by a similar mechanism to that used by plasma α2M to inhibit high-molecular-mass proteases. The mutant α2M was intracellularly active in COS-1 cells in inhibiting the endogenous processing of the soluble substrates for furin (von Willebrand factor, transforming growth factor β1 and a soluble form of the envelope glycoprotein gp160 from HIV-1) but not the membrane-bound form of gp160. The intracellular activity of mutant α2M strongly indicated that α2M attains its native conformation, and thus that the unusual internal S-ester is formed, before α2M passes through the cleavage compartment(s). Our results show for the first time that modulation of the bait region of α2M allows the creation of an inhibitor against membrane-bound proteases. It can be expected that the use of α2M-bait mutants will become important as a technique for the study of various proteolytic processes and for the identification of the proteases involved." @default.
- W1759884410 created "2016-06-24" @default.
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- W1759884410 date "1997-09-01" @default.
- W1759884410 modified "2023-10-14" @default.
- W1759884410 title "Inhibition of intracellular proteolytic processing of soluble proproteins by an engineered <i>α</i>2-macroglobulin containing a furin recognition sequence in the bait region" @default.
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- W1759884410 doi "https://doi.org/10.1042/bj3260507" @default.
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