Furin activates Pseudomonas exotoxin A by specific cleavage in vivo and in vitro.
NM Inocencio, JM Moehring, TJ Moehring - Journal of Biological Chemistry, 1994 - ASBMB
We have demonstrated that the native proenzymatic form of Pseudomonas exotoxin A can
be cleaved at its specific activation site by furin in intact Chinese hamster ovary cells or in
vitro by furin in isolated membrane fractions from these cells. We have compared the activity
of furin in cell membrane fractions with that of purified, recombinant human furin. We have
verified that RPE. 40, a Pseudomonas toxin-resistant mutant cell strain, is mutant in the fur
gene, and we have demonstrated that these cells are deficient in cleavage of the toxin. We …
be cleaved at its specific activation site by furin in intact Chinese hamster ovary cells or in
vitro by furin in isolated membrane fractions from these cells. We have compared the activity
of furin in cell membrane fractions with that of purified, recombinant human furin. We have
verified that RPE. 40, a Pseudomonas toxin-resistant mutant cell strain, is mutant in the fur
gene, and we have demonstrated that these cells are deficient in cleavage of the toxin. We …
