Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P02749 (beta2-glycoprotein I)
836 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Washed human platelets were preincubated with 0-300 micrograms/ml human beta 2-glycoprotein I and the effect of this on the adenylate cyclase activity (EC.4.6.1.1.) was studied. Adenylate cyclase activity could be increased 2-3 fold. The same degree of activation was seen when low concentrations of prostaglandin E1 (1 microM) had been present concomitant with beta 2-glycoprotein I during preincubation. The dose-response curves of the adenylate cyclase activity measured as a function of the beta 2-glycoprotein I concentration were S-shaped in the absence of prostaglandin E1 and hyperbolic in its presence. The results suggest a biological function of beta 2-glycoprotein I as a compound conserving and activating the membrane-bound adenylate cyclase.
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PMID:Effect of beta 2-glycoprotein I on the activity of adenylate cyclase in platelet membranes. 668 48

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.
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PMID:Antiphospholipid antibodies bind ATP: a putative mechanism for the pathogenesis of neuronal dysfunction. 1629 22