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Shear stress-induced von Willebrand factor binding to platelet glycoprotein
Ib initiates calcium influx associated with aggregation
TW Chow, JD Hellums, JL Moake and MH Kroll
Biomedical Engineering Laboratory, Rice University, Houston, TX.
Platelets subjected to elevated levels of fluid shear stress in the absence
of exogenous agonists will aggregate. Shear stress-induced aggregation
requires von Willebrand factor (vWF) multimers, extracellular calcium
(Ca2+), adenosine diphosphate (ADP), and platelet membrane glycoprotein
(GP)Ib and GPIIb-IIIa. The sequence of interaction of vWF multimers with
platelet surface receptors and the effect of these interactions on platelet
activation have not been determined. To elucidate the mechanism of shear
stress-induced platelet aggregation, suspensions of washed platelets were
subjected to different levels of uniform shear stress (15 to 120 dyne/cm2)
in an optically modified cone and plate viscometer. Cytoplasmic ionized
calcium ([Ca2+]i) and aggregation of platelets were monitored
simultaneously during the application of shear stress; [Ca2+]i was measured
using indo-1 loaded platelets and aggregation was measured as changes in
light transmission. Basal [Ca2+]i was approximately 60 to 100 nmol/L. An
increase of [Ca2+]i (up to greater than 1,000 nmol/L) was accompanied by
synchronous aggregation, and both responses were dependent on the shear
force and the presence of vWF multimers. EGTA chelation of extracellular
Ca2+ completely inhibited vWF-mediated [Ca2+]i and aggregation responses to
shear stress. Aurin tricarboxylic acid, which blocks the GPIb recognition
site on the vWF monomer, and 6D1, a monoclonal antibody to GPIb, also
completely inhibited platelet responses to shear stress. The tetrapeptide
RGDS and the monoclonal antibody 10E5, which inhibit vWF binding to
GPIIb-IIIa, partially inhibited shear stress-induced [Ca2+]i and
aggregation responses. The combination of creatine phosphate/creatine
phosphokinase, which converts ADP to adenosine triphosphate and blocks the
effect of ADP released from stimulated platelets, inhibited shear
stress-induced platelet aggregation without affecting the increase of
[Ca2+]i. Neither the [Ca2+]i nor aggregation response to shear stress was
inhibited by blocking platelet cyclooxygenase metabolism with
acetylsalicylic acid. These results indicate that GPIb and extracellular
Ca2+ are absolutely required for vWF-mediated [Ca2+]i and aggregation
responses to imposed shear stress, and that the interaction of vWF
multimers with GPIIb-IIIa potentiates these responses. Shear stress-induced
elevation of platelet [Ca2+]i, but not aggregation, is independent of the
effects of release ADP, and both responses occur independently of platelet
cyclooxygenase metabolism. These results suggest that shear stress induces
the binding of vWF multimers to platelet GPIb and this vWF-GPIb interaction
causes an increase of [Ca2+]i and platelet aggregation, both of which are
potentiated by vWF binding to the platelet GPIIb-IIIa complex.
Volume 80,
Issue 1,
pp. 113-120,
07/01/1992
Copyright © 1992 by The American Society of Hematology
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