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Protein disulfide isomerase activity is released by activated platelets
K Chen, Y Lin and TC Detwiler
Department of Biochemistry, State University of New York Health Science
Center, Brooklyn 11203.
The release of protein disulfide isomerase by activated platelets was
hypothesized on the basis of reported intermolecular and intramolecular
thiol-disulfide exchange and disulfide reduction involving released
thrombospondin in the supernatant solution of activated platelets
(Danishefsky, Alexander, Detwiler: Biochemistry, 23:4984, 1984; Speziale,
Detwiler: J Biol Chem, 265:17859, 1990; Speziale, Detwiler: Arch Biochem
Biophys 286:546, 1991). Protein disulfide isomerase activity, measured by
catalysis of the renaturation of ribonuclease inactivated by randomization
of disulfide bonds, was detected in the supernatant solution after platelet
activation. The activity was inhibited by peptides known to inhibit protein
disulfide isomerase; the peptides also inhibited formation of
disulfide-linked thrombospondin- thrombin complexes. The reaction catalyzed
by the supernatant solution showed a pH dependence distinct from that of
the uncatalyzed reaction. The activity was excluded by a 50-Kd dialysis
membrane, and it was eluted in the void volume of a gel-filtration column,
indicating that it was associated with a macromolecule. The activity was
not removed by centrifugation at 100,000 g for 150 minutes indicating that
it was not associated with membrane microvesicles. Possible functions for
the release of protein disulfide isomerase by activated platelets are
discussed.
Volume 79,
Issue 9,
pp. 2226-2228,
05/01/1992
Copyright © 1992 by The American Society of Hematology
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