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Beta 2-glycoprotein I is a requirement for anticardiolipin antibodies
binding to activated platelets: differences with lupus anticoagulants
W Shi, BH Chong and CN Chesterman
Department of Haematology, Prince of Wales Hospital, School of Pathology,
University of New South Wales, Sydney, Australia.
Antiphospholipid (aPL) antibodies are of major interest not only because
the lupus anticoagulant (LA) causes an inhibition of in vitro blood
coagulation, but also because the presence of aPL antibodies confers a risk
of thrombosis. The inhibition of in vitro phospholipid- dependent
coagulation (LA) is thought to be caused by the binding of LA to
procoagulant phospholipid surfaces, thus impeding the clotting process.
Another class of aPL antibodies are those originally described to be
directed against negatively charged phospholipids, in particular
cardiolipin (ACA). ACA are usually directed against a complex antigen
consisting of negatively charged phospholipid and a plasma protein, beta
2-glycoprotein I (beta 2-GPI). Further, there is antibody heterogeneity
even within individual patients so that ACA and LA are separable using
physicochemical techniques such as ion exchange chromatography and
chromatofocusing. Using such techniques we have enriched Ig fractions for
LA and ACA from two patient plasmas. The majority of Ig with LA activity
had a pI of 7.2 to 7.3 whereas ACA had a pI of 5.0 to 5.2. Using these
enriched fractions labeled with [125I]- iodine we have shown that LA binds
to platelets in a specific and saturable manner. Binding is dependent on
thrombin activation. [125I]- ACA behaves differently. Like LA, binding is
specific and dependent on thrombin activation but in this case requires the
presence of beta 2- GPI. ACA, in the presence of beta 2-GPI, competes for
binding with LA suggesting the same or contiguous site. There is no
cross-reactivity of these antibodies with GPIIb/IIIa and the most likely
binding site is phospholipid. In neither case does LA nor ACA have an
effect on thrombin-induced release of serotonin or beta-thromboglobulin nor
do they affect platelet aggregation induced by a number of agonists. This
antibody binding may play an etiological role in thrombocytopenia
associated with aPL, but does not explain thrombosis on the basis of
hyperaggregability or increased platelet release.
Volume 81,
Issue 5,
pp. 1255-1262,
03/01/1993
Copyright © 1993 by The American Society of Hematology
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