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Mechanism and effects of the binding of lupus anticoagulant IgG and
prothrombin to surface phospholipid
LV Rao, AD Hoang and SI Rapaport
Department of Biochemistry, University of Texas Health Center at Tyler
75710, USA.
We report here experiments on how lupus anticoagulant antibodies (LA IgG)
that react with prothrombin bind to surface phospholipid and affect
prothrombin's affinity for surface phospholipid and activation to thrombin.
LA IgG was purified by protein A chromatography from the plasma of 16
patients of whom four had associated hypoprothrombinemia and 10 had
experienced thrombosis. Many LA IgG bound, in the absence of phospholipid
and calcium, not only to immobilized prothrombin but to both prothrombin 1
and fragment 1, which established at least an oligoclonal origin of LA IgG.
No LA IgG bound to thrombin. Although prothrombin and Ca2+ were required to
support binding of LA IgG to immobilized phosphatidylserine (PS),
prothrombin at higher concentrations inhibited binding, presumably by
competing with prothrombin/LA IgG complexes for PS binding sites.
Prothrombin 1, which cannot bind to PS, also inhibited binding of many LA
IgG to PS, presumably by forming competing soluble prothrombin 1/LA IgG
complexes. Despite their ability to react with prothrombin independent of
phospholipid, LA IgG enhanced binding of prothrombin to immobilized
phospholipid and to cultured human umbilical vein endothelial cells.
Prothrombin bound with LA IgG to the surface of endothelial cell monolayers
could be activated to thrombin after supernatant prothrombin and LA IgG
were washed away. The relation is discussed of these observations to a
hypothesis that LA IgG mediated concentration of prothrombin on cell
surface phospholipid represents a mechanism by which LA IgG could increase
thrombotic risk.
Volume 88,
Issue 11,
pp. 4173-4182,
12/01/1996
Copyright © 1996 by The American Society of Hematology
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