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Platelet-associated antibody to glycoprotein IIb/IIIa from chronic immune
thrombocytopenic purpura patients often binds to divalent cation- dependent
antigens
K Fujisawa, P Tani and R McMillan
Department of Molecular and Experimental Medicine, Scripps Research
Institute, La Jolla, CA 92037.
Chronic immune thrombocytopenic purpura (ITP) is a syndrome of destructive
thrombocytopenia due to autoantibodies against platelet- associated
antigens. These antigens are most commonly located on the platelet
glycoprotein (GP) IIb/IIIa complex. In the present studies, we show that
many platelet-associated anti-GPIIb/IIIa autoantibodies from chronic ITP
patients depend on conformationally intact GPIIb/IIIa for maximal binding.
We studied anti-GPIIb/IIIa autoantibodies from 19 ITP patients (15
platelet-associated, 8 plasma) and alloantibodies from three patients with
posttransfusion purpura (anti-PIA1). Antibodies were preincubated with
purified intact GPIIb/IIIa, EDTA-dissociated GPIIb/IIIa, GPIIIa, or GPIIb
for 2 hours and then residual antibody was measured in an antigen capture
assay. The binding results were compared with those obtained using antibody
preincubated in buffer. Of the 15 platelet-associated autoantibodies
studied, the intact GPIIb/IIIa complex resulted in greater inhibition of
antibody binding than the EDTA-dissociated complex, with a mean inhibition
ratio (intact/dissociated) of 7.9 (range, 1.4 to 30.3). Little inhibition
was noted using either GPIIb or GPIIIa. Conversely, plasma anti-PIA1
alloantibodies or plasma autoantibodies from ITP patients against the c-
terminal region of GPIIIa were more efficiently inhibited by the
dissociated complex or purified GPIIIa. We conclude that platelet-
associated anti-GPIIb/IIIa autoantibodies in chronic ITP are frequently
directed to cation-dependent conformational antigens.
Volume 81,
Issue 5,
pp. 1284-1289,
03/01/1993
Copyright © 1993 by The American Society of Hematology
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