Antiphospholipid antibodies bind ATP: a putative mechanism for the pathogenesis of neuronal dysfunction

Antiphospholipid antibodies (aPL) generated in experimental animals cross-react with ATP. We therefore examined the possibility that aPL IgG from human subjects bind to ATP by affinity column and an enzyme linked immunosorbent assay (ELISA). Sera with high levels of aPL IgG were collected from 12 pa...

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Bibliographic Details
Published in:	Clinical & developmental immunology Vol. 12; no. 3; pp. 175 - 180
Main Authors:	Chapman, J, Soloveichick, L, Shavit, S, Shoenfeld, Y, Korczyn, A D
Format:	Journal Article
Language:	English
Published:	Egypt Hindawi Publishing Corporation 01-09-2005 Hindawi Limited
Subjects:	Adenosine Triphosphate - immunology Adenosine Triphosphate - metabolism Adult Aged Animals Antibodies, Antiphospholipid - metabolism Antibody Specificity Antiphospholipid Syndrome - complications Antiphospholipid Syndrome - immunology Antiphospholipid Syndrome - metabolism beta 2-Glycoprotein I Binding, Competitive Cardiolipins - immunology Cardiolipins - metabolism Central Nervous System Diseases - etiology Central Nervous System Diseases - immunology Central Nervous System Diseases - metabolism Cross Reactions Female Glycoproteins - immunology Glycoproteins - metabolism Humans Immunoglobulin G - metabolism In Vitro Techniques Middle Aged Neurotransmitter Agents - immunology Neurotransmitter Agents - metabolism Pregnancy
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Summary:	Antiphospholipid antibodies (aPL) generated in experimental animals cross-react with ATP. We therefore examined the possibility that aPL IgG from human subjects bind to ATP by affinity column and an enzyme linked immunosorbent assay (ELISA). Sera with high levels of aPL IgG were collected from 12 patients with the antiphospholipid syndrome (APS). IgG fractions from 10 of 12 APS patients contained aPL that could be affinity-bound to an ATP column and completely eluted with NaCl 0.5 M. A significant (> 50%) inhibition of aPL IgG binding by ATP 5 mM was found in the majority. Similar inhibition was obtained with ADP but not with AMP or cAMP. All the affinity purified anti-ATP antibodies also bound beta2-glycoprotein-I (beta2-GPI, also known as apolipoprotein H) suggesting that, similar to most pathogenic aPL, their binding depends on this serum cofactor. We further investigated this possibility and found that the binding of beta2-GPI to the ATP column was similar to that of aPL IgG in that most was reversed by NaCl 0.5 M. Furthermore, addition of beta2-GPI to aPL IgG significantly increased the amount of aPL binding to an ATP column. We conclude that aPL IgG bind ATP, probably through beta32-GPI. This binding could interfere with the normal extracellular function of ATP and similar neurotransmitters.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1740-2522 2314-8861 2314-7156 1365-2567 1740-2530
DOI:	10.1080/17402520500217844