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Heterogeneity of platelet secretion in response to thrombin demonstrated by
fluorescence flow cytometry
GI Johnston, EB Pickett, RP McEver and JN George
Platelet membrane changes that accompany in vivo activation may be
difficult to detect if only a small fraction of circulating platelets has
undergone secretion. This study describes an approach to that problem by
using a method to measure the number of molecules of fluorescein-labeled
antibody bound to individual platelets by flow cytometry. The platelet
response to different concentrations of thrombin was determined by
measuring the binding of a monoclonal antibody (S12) to GMP-140, an
alpha-granule membrane protein that becomes exposed on the platelet surface
during alpha-granule secretion. Unstimulated platelets bound a mean of
1,120 molecules of S12 per cell, and 93% of platelets bound less than 2,000
molecules. Platelet stimulation by 0.25 U/mL thrombin caused maximum S12
binding with a mean of 7,529 molecules per cell. Even at low concentrations
of thrombin (0.025 U/mL), 5% of platelets were maximally activated, binding
over 7,000 molecules of S12 per cell. Conversely, at 0.25 U/mL thrombin,
13% of platelets continued to bind less than 2,000 molecules of S12 per
cell. A mixture of as little as 5% thrombin-activated platelets with
unstimulated platelets could be detected by this method. Therefore flow
cytometry offers an important tool for investigating patients who may have
circulating activated platelets as part of a disorder predisposing to
thrombosis or hemorrhage.
Volume 69,
Issue 5,
pp. 1401-1403,
05/01/1987
Copyright © 1987 by The American Society of Hematology
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