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Autoantibodies to heparin from patients with antiphospholipid antibody
syndrome inhibit formation of antithrombin III-thrombin complexes [see
comments]
S Shibata, PC Harpel, A Gharavi, J Rand and H Fillit
Department of Geriatrics, Mount Sinai Medical Center, New York, NY 10029.
The antiphospholipid antibody syndrome (APS) is characteristically
associated with thrombosis. Heparan sulfate (HS) is a physiologic
endothelial cell surface modulator of normal anticoagulation, containing a
specific oligosaccharide sequence that binds antithrombin III with high
affinity and also is present in heparin, a related glycosaminoglycan. We
hypothesized that a subset of antiphospholipid antibodies with high
affinity for heparan sulfate/heparin epitopes may inhibit the function of
HS, promoting a procoagulant state. Purified IgG from all seven patients
with APS studied were reactive with heparin by enzyme-linked immunosorbent
assay, whereas none of five controls had antiheparin reactivity. IgG
antiheparin antibodies were purified from two APS patients by affinity
chromatography on heparin-Sepharose. Specificity studies showed that
low-affinity electrostatic interactions clearly did not account for the
observed reactivity with heparin, and that APS IgG antiheparin antibodies
were specifically reactive with a disaccharide present in the heparin
pentasaccharide that binds antithrombin III. Furthermore, APS IgG
antiheparin antibodies inhibited heparin-accelerated formation of
antithrombin III-thrombin complexes. We conclude that antiheparan
sulfate/heparin antibodies may be a cause of autoimmune vascular thrombosis
in the antiphospholipid antibody syndrome.
Volume 83,
Issue 9,
pp. 2532-2540,
05/01/1994
Copyright © 1994 by The American Society of Hematology
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