Enhanced Diagnostic Tools
Anti-ß2glycoprotein I (anti-ß2GPI) antibodies constitute the main autoantibody specificity in the sera of patients with antiphospholipid syndrome (APS). There is evidence that anti- ß2GPI antibodies induce the precoagulant activity of the endothelium by cross-linking the ß2 glycoprotein I (ß2GPI) on the cell surface. Since ß2GPI lacks intracellular domains, homology with other molecules such as CD40 that could initiate signaling, was extensively searched. A 86% homology between the amino acid position 239-245 of the CD40 and 7-13 of the ß2glycoprotein was found. The CD40 peptide corresponding to amino acids 239-245 of the CD40 molecule was synthesized and coupled to a multiple antigenic peptide carrier. Antibodies to CD40 peptide were found in 61.5% APS patients (n=39), in 72.7% of systemic lupus erythematosus (SLE) positive for anti-ß2GPI antibodies (n=11) and 31.6% of SLE negative for anti- ß2GPI antibodies (n=19), but not in rheumatoid arthritis patients (n=28) or controls (n=36). Antibodies to CD40 peptide were associated with arterial thrombosis and/or brain microinfarcts. Affinity purified anti-CD40 peptide antibodies as well as affinity purified anti-ß2GPI antibodies recognized both, the ß2GPI and the CD40 peptide. The specificity of this recognition was confirmed with homologous and heterologous inhibition experiments. Confocal microscopy experiments demonstrated this cross-recognition of CD40 and ß2GPI molecules, by the purified anti-CD40 peptide antibodies, at the protein level. Thus, antibodies reacting with the ß2GPI can react and potentially activate different cells which express CD40 molecules at their surface.
If you need any literature regarding
any of our products or services, please do not hesitate to submit a request.