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Temperature-dependent effects of EDTA on the membrane glycoprotein IIb-
IIIa complex and platelet aggregability
D Pidard, D Didry, TJ Kunicki and AT Nurden
In agreement with previous studies, we observed that incubation of washed
human platelets with EDTA at 37 degrees C for short periods caused an
irreversible loss of their aggregation response to adenosine diphosphate
and markedly diminished their capacity to bind fibrinogen. AP-2 is a
monoclonal antibody that reacts with a determinant specific to the
glycoprotein (GP) IIb-IIIa complex. We now report that in a direct binding
assay, the number of sites for AP-2 on platelets incubated with EDTA at 37
degrees C fell to approximately 30% of those present on control platelets.
This effect of EDTA was not observed at room temperature. Analysis of the
treated platelets by sodium dodecyl sulfate-polyacrylamide gel
electrophoresis revealed normal amounts of GP IIb and GP IIIa. However,
studies using crossed immunoelectrophoresis with 125I-AP-2, 125I-Tab
(anti-GP IIb), or 125I- AP-3 (anti-GP IIIa) in intermediate gels showed
that at 37 degrees C, EDTA was inducing an irreversible change in GP
IIb-IIIa complexes. A reduction in size and probable dissociation of the GP
IIb-IIIa precipitate was accompanied by the appearance of precipitates
having the characteristics of those given by free GP IIb and free GP IIIa
and the location of a major new cathodal precipitate, which bound Tab and
AP-3 but not AP-2. Membrane modifications associated with the loss of
antigenic determinants on GP IIb-IIIa may explain EDTA-induced loss of
platelet aggregability at 37 degrees C.
Volume 67,
Issue 3,
pp. 604-611,
03/01/1986
Copyright © 1986 by The American Society of Hematology
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