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Localization of protein disulfide isomerase to the external surface of the
platelet plasma membrane
DW Essex, K Chen and M Swiatkowska
Department of Medicine, State University of New York, Health Science Center
at Brooklyn 11203, USA.
Protein disulfide isomerase (PDI) is an enzyme that catalyzes the formation
as well as the isomerization of disulfide bonds. In this study, antibodies
against PDI were used to show PDI antigen on the platelet surface by
indirect immunofluorescence microscopy and by flow cytometry. The platelets
were not activated, as evidenced by the absence of staining by an antibody
against P-selectin. Permeabilized platelets showed little cytosolic PDI by
indirect immunofluorescence microscopy, suggesting that the majority of
platelet PDI is localized to the platelet surface. PDI activity against
"scrambled" RNase was shown with intact platelets. The activity was
inhibited by inhibitors of PDI and by an antibody against PDI. Other blood
cells showed little PDI. Platelet surface PDI may play a role in the
various physiological and pathophysiologic processes in which platelets are
involved.
Volume 86,
Issue 6,
pp. 2168-2173,
09/15/1995
Copyright © 1995 by The American Society of Hematology

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