scholarly journals Anticardiolipin and anti-beta 2 glycoprotein-I antibodies disappearance in patients with systemic lupus erythematosus and antiphospholipid syndrome while on belimumab

2018 ◽  
Vol 77 (11) ◽  
pp. 1694-1695 ◽  
Author(s):  
Savino Sciascia ◽  
Elena Rubini ◽  
Massimo Radin ◽  
Irene Cecchi ◽  
Daniela Rossi ◽  
...  
2012 ◽  
Vol 2012 ◽  
pp. 1-6 ◽  
Author(s):  
Zdenka Ulcova-Gallova ◽  
Alice Mockova ◽  
Miroslava Cedikova

Female patients in reproductive age with systemic lupus erythematosus and fertility complications together are observed by rheumatologists, gynecologists, and reproductive immunologists. The paper notes the presence of autoantibodies to zona pellucida, to phospholipids (phosphatidyl serine, phosphatidyl ethanolamine, phosphatidyl inositol, phosphatidyl glycerol, phosphatidic acid, annexin V, beta-2 glycoprotein I, and cardiolipin) and of isoantibodies to sperm cells. Isoantibodies to sperm cells are not significantly predominant, but autoimmunity is well expressed in IgG positivity against phosphatidyl inositol, phosphatidyl ethanolamine, phosphatidyl serine, cardiolipin, and beta-2 glycoprotein I, as well as antizona pellucida antibodies in IgG isotype. According to the levels of autoantibodies we have to choose preventive treatment to protect mother and her foetus.


1997 ◽  
Vol 56 ◽  
pp. 475-476
Author(s):  
M.E.A. Evangelopoulos ◽  
D.A. Sotos ◽  
A. Levedakos ◽  
M.E. Mavrikakis ◽  
C.D. Evangelopoulos

2004 ◽  
Vol 92 (12) ◽  
pp. 1303-1311 ◽  
Author(s):  
Anthi Balitsari ◽  
John Routsias ◽  
Panayiotis G.Vlachoyiannopoulos ◽  
Clio Mavragani ◽  
Efi Bourazopoulou

SummaryAnti-β2glycoprotein I (anti-β2GPI) antibodies constitute the main autoantibody specificity in the sera of patients with antiphospholipid syndrome (APS). There is evidence that antiβ2GPI antibodies induce the precoagulant activity of the endothelium by cross-linking the β2 glycoprotein I (β2GPI) on the cell surface. Since β2GPI 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 β2glycoprotein 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 β2GPI antibodies (n=11) and 31.6% of SLE negative for antiβ2GPI 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-β2GPI antibodies recognized both, the β2GPI 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 β2GPI molecules, by the purified anti-CD40 peptide antibodies, at the protein level. Thus, antibodies reacting with the β2GPI can react and potentially activate different cells which express CD40 molecules at their surface.


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