Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “CARDIOLIPIN”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 1,099 records · Page 61Linked to original sources
PubMed1995

Binding of autoimmune cardiolipin-reactive antibodies to heparin: a mechanism of thrombosis?

Autoimmune CL-rA need a plasma protein, beta 2GPI, to bind anionic PL. While beta 2GPI could be the true antigen, beta 2GPI binding to solid phase heparin did not determine its recognition by CL-rA when using patient plasmas. We tested plasmas from four patients with antiphospholipid syndrome in this study and no CL-rA binding to heparin sepharose was obtained. On the contrary, when CL-rA were first purified from the plasmas by means of a CL-octyl sepharose column, the purified material bound to the heparin sepharose column. Thus, after recognizing beta 2 GPI, CL-rA bind heparin. 'In vivo' CL-rA binding to heparin like-substances could inhibit the anti-thrombotic properties of endothelial cells.

Adult↗
PubMed2006

Patients with atherosclerotic syndrome, negative in anti-cardiolipin assays, make IgA autoantibodies that preferentially target domain 4 of beta2-GPI.

Autoantibodies targeting beta2-glycoprotein l (beta2-GPI), a component of the atherosclerotic plaque, are commonly found in patients with acute ischemic syndromes. Serum samples from APS (antiphospholipid syndrome) patients and from cardiovascular patients exhibiting acute atherosclerotic syndromes were analyzed for IgG and IgA antibodies in both anti-beta2-GPI and anticardiolipin (aCL) ELISA assays. All of the APS samples used here were positive in both assays. Serum samples from 382 atherosclerosis patients were also analyzed for IgG and IgA antibodies in the same assays. In sharp contrast to the APS samples, we found that only 1% of the samples from atherosclerosis patients were positive for IgA aCL, and 1.6% positive for IgG aCL, whereas 35.6% were positive for IgA anti-beta2-GPI and only 1.6% for IgG anti-beta2-GPI. The antigenic specificity of 29 serum samples from atherosclerosis patients was evaluated. Six different recombinant domain-deleted mutants (DM) of human beta2-GPI and full-length human beta2-GPI (wild-type) were used in competitive inhibition assays to inhibit the autoantibodies from binding in the anti-beta2-GPI ELISA assays. Domain-deleted mutants D--345 and D--45 inhibited the binding in the IgA anti-beta2-GPI assay, suggesting that these autoantibodies recognize domain 4 of the beta2-GPI molecule. These results clearly show that IgA anti-beta2-GPI autoantibodies from atherosclerotic patients are distinct from IgA autoantibodies found in APS samples.

Antibodies, Anticardiolipin↗
PubMed2005

Oxidation and biotinylation of beta 2 glycoprotein I glycan chains induce an increase in its affinity for anionic phospholipids similar to that obtained by the addition of anti-beta 2 glycoprotein I or anti-cardiolipin antibodies.

Binding of beta 2 glycoprotein I (beta2GPI) to apoptotic cells plays a key role in the opsonization of apoptotic bodies and the formation of antiphospholipids antibodies. Here, we describe the binding of beta2GPI to apoptotic cells using beta2GPI labelled with biotin-hydrazide (beta2GPI-bh) after oxidation of its glycan chains. Flow cytometry analyses and confocal microscopy showed that beta2GPI-bh, contrary to native beta(GPI, bound to apoptotic cells, either permeable or non-permeable to propidium iodide (PI), as did annexin-V-FITC. But, in the absence of divalent ions, beta2GPI-bh, contrary to annexin V, was still able to bind to apoptotic cells. Binding equilibrium studies, performed on solid-state anionic phospholipids (AnPL), revealed that beta2GPI-bh had a greater apparent affinity for AnPL than native beta2GPI. In presence of the anti-beta2GPI mAb 8C3, the ability of native beta2GPI to bind to AnPL was increased and binding to apoptotic PI+ and PI- CEM cells was observed whereas binding of beta2GPI-bh was barely affected by the addition of 8C3. However, the 8C3-enhanced ability of native beta2GPI to bind to AnPL was still weaker than that of beta2GPI-bh. It is not clear why the oxidation and biotinylation of glycan chains of beta2GPI increases its affinity for AnPL, but it seems that if such oxidative process occurs naturally, it could participate in enhancing antiphospholipid formation.

Animals↗
PubMed2004

Single nucleotide polymorphisms in the coding region of the apolipoprotein H (beta2-glycoprotein I) gene and their correlation with the protein polymorphism, anti-beta2glycoprotein I antibodies and cardiolipin binding: description of novel haplotypes and their evolution.

Apolipoprotein H (APOH), also known as beta2-glycoprotein I, is a major autoantigen for the production of antiphospholipid antibodies (APA) in autoimmune diseases. APA is also recognized by a cryptic epitope generated following the interaction of APOH with anionic phospholipids (PL). The prevalence of APA in the general U.S. white population is about 10%, but it ranges from 30-70% in patients with lupus and antiphospholipid syndrome. Since the structural characterization of APOH from different mammalian species is important to identify the evolutionary conserved regions that may be critical for its function, we have previously determined the chimpanzee APOH gene structure and the prevalence of APA. There are only two amino acid differences between the chimpanzee and human wild type APOH proteins. Chimpanzees have an unusually high prevalence (64%) of APA. There is a common protein polymorphism in the human APOH gene, with the occurrence of four alleles APOH*1, APOH*2, APOH*3 and APOH*4, the latter being present only in blacks. Based on its differential reactivity with an APOH monoclonal antibody, the APOH*3 allele is further divided into APOH*3(W) (present only in whites) and APOH*3(B) (present only in blacks). In this study we have screened a large African population (n = 755) to determine the prevalence of APA and the molecular basis of the protein polymorphism. Almost 50% of the Africans were found to be positive for APA. The APOH*3(B) allele was found to be identical to the chimpanzee's wild type APOH. Novel two-site or three-site haplotypes, encoded in the third domain of APOH, explained the molecular basis of the APOH*3(B), APOH*3(W) and APOH*4 alleles. Based on the comparison of the human and chimpanzee APOH DNA sequences, we suggest that the APOH*3(W) and APOH*4 alleles arose on the ancestral APOH*3(B) haplotype after the split of human races. We also found that these haplotypes are associated with the occurrence of APA. Recombinant APOH haplotypes, expressed in COS-1 cells, showed that these mutations also affect the binding of APOH to anionic PL.

Adult↗
PubMed2003

Association of the PRO12ALA polymorphism of the PPAR-gamma2 gene with oxidized low-density lipoprotein and cardiolipin autoantibodies in nondiabetic and type 2 diabetic subjects.

Peroxisome proliferator-activated receptor-gamma (PPAR-gamma) is a key component in adipocyte differentiation and fat-specific gene expression and may modulate macrophage functions, like proinflammatory activities, and stimulate oxidized low-density lipoprotein (ox-LDL) uptake. We hypothesized that the Pro12Ala polymorphism of the PPAR-gamma2 gene may affect the immune response to ox-LDL. Therefore, we investigated the association of the Pro12Ala polymorphism of the PPAR-gamma2 gene with ox-LDL autoantibodies, as well anticardiolipin antibodies, in a 10-year prospective study. The Pro12Ala polymorphism was genotyped in 119 nondiabetic subjects (age, 45 to 64 years; body mass index [BMI], 19 to 46 kg/m(2)) and 70 type 2 diabetic patients (age, 45 to 65 years; BMI, 19 to 46 kg/m(2)) by the polymerase chain reaction-single-strand conformation polymorphism (PCR-SSCP) method. Ox-LDL autoantibodies and anticardiolipin antibodies were determined at baseline and after 10 years of follow-up. At baseline, the Pro12Ala polymorphism was not associated with ox-LDL autoantibodies in nondiabetic subjects, whereas type 2 diabetic patients having the Pro12Ala or the Ala12Ala genotypes tended to have higher levels of ox-LDL autoantibodies than did type 2 diabetic patients with the Pro12Pro genotype. At the 10-year follow-up, diabetic subjects having the Ala12 allele had higher ox-LDL autoantibody levels than did diabetic subjects with the Pro12Pro genotype (P =.043 after adjustment for age, gender, BMI, and hemoglobin A(1c) [HbA(1c)] at 5 years). In nondiabetic subjects and regarding anticardiolipin antibodies, no such relationship was observed. We conclude that the Pro12Ala polymorphism of the PPAR-gamma2 gene was associated with increased ox-LDL autoantibodies in type 2 diabetic subjects. Genotype may therefore modulate the oxidative modification of LDL in hyperglycemic milieu.

Alanine↗
PubMed2000

Anti-cardiolipin antibodies in fetal blood and amniotic fluid derived from patients with the anti-phospholipid syndrome.

The aim of this study was to investigate whether, in patients with antiphospholipid syndrome, anticardiolipin antibodies pass from mother to offspring sera and amniotic fluid. Eleven patients with antiphospholipid syndrome (study group) and 11 healthy controls, matched by maternal and gestational age (control group) were prospectively examined for the presence of anticardiolipin antibodies in the cord blood during labour, and amniotic fluid during vaginal or Caesarean delivery. Three neonates (27.3%) in the study group had anticardiolipin antibodies in the cord blood, while none had them in the control group. Anticardiolipin antibodies were detected in the amniotic fluid in six (54.5%) of the study group pregnancies, compared with none in the control group. No adverse neonatal outcome was noted except for significantly lower (P < 0.0006) mean birth weight in the study group. Anticardiolipin antibodies can pass the placenta and be detected in fetal cord blood and amniotic fluid. This finding might be used in the future for the assessment of pregnancies with antiphospholipid syndrome.

Amniotic Fluid↗
PubMed1994

False-positive rapid plasma reagin tests in human immunodeficiency virus infection and relationship to anti-cardiolipin antibody and serum immunoglobulin levels.

The incidence of biologic false-positive rapid plasma reagin (RPR) tests may be increased in human immunodeficiency virus (HIV) infection; however, injecting drug use has not been excluded as the cause. Review of 3371 periodic syphilis serology results from 1077 HIV-seropositive patients in the United States Air Force HIV Natural History Study between January 1986 and June 1992 revealed a cumulative biologic false-positive RPR rate of 1%. Most (6/9) were transient low-titer results associated with a recent acute infectious process. False-positive RPR tests did not appear to correlate with anticardiolipin antibody levels or serum IgG or IgA levels, which are increased in HIV infection. Although not statistically significant, there was a trend toward higher IgM levels in patients with biologic false-positive tests. Thus, the incidence of false-positive RPR in an HIV-infected population with a low risk of injecting drug use is similar to that in the general population, and the mechanism may correlate with elevated serum IgM levels.

Analysis of Variance↗