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A form of protease nexin I is expressed on the platelet surface during
platelet activation
RS Gronke, DJ Knauer, S Veeraraghavan and JB Baker
Department of Biochemistry, University of Kansas, Lawrence.
A protein that has several similarities to protease nexin I, a fibroblast
thrombin and urokinase inhibitor, has been detected on platelets (Gronke
RS, Bergman BL, and Baker JB: J Biol Chem 262:3030, 1987). On incubation of
platelets with 125I-thrombin, this platelet protein forms complexes with
125I-thrombin that are found both in the incubation medium and, as
demonstrated here, associated with purified platelet plasma membranes. The
present results indicate that interaction with the platelet surface may
modulate the conformation and function of this platelet form of protease
nexin I (PNIp) because: (a) an antibody against protease nexin I inhibited
released PNIp, but not platelet-bound PNIp from complexing 125I-thrombin,
and (b) whereas PNIp extracted from platelets bound both thrombin and
urokinase, platelet- bound PNIp bound only thrombin. In experiments using
several different platelet isolation methods, PNIp accounted for a large
fraction of the rapid high affinity binding of 125I-thrombin to platelets.
However, platelets isolated and maintained in the presence of metabolic
inhibitors failed to take added thrombin into 125I-thrombin-PNIp complexes.
This finding suggests that PNIp is released from inside platelets during
activation, and thus does not function to transmit the primary activating
signal that is generated by thrombin binding to platelets.
Volume 73,
Issue 2,
pp. 472-478,
02/01/1989
Copyright © 1989 by The American Society of Hematology
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