Modulation of erythrocyte acetylcholinesterase by cardiolipin: effect on subunit coupling revealed by irradiation inactivation.
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We demonstrate the ability of a peptide corresponding to the presequence of the cytochrome c oxidase subunit IV to induce lipid mixing between large unilamellar liposomes. This lipid mixing requires the presence of CL or PE, lipids able to form non-bilayer structures, and is not observed with other negatively charged lipids. However, the fact that this mixing occurs without mixing of the liposome aqueous phases and without destabilizing the lipid organisation is unusual and has not been observed for other amphiphilic peptides. This observation supports the idea that the presequence could play a role in the formation of translocation contact sites between the two mitochondrial membranes and facilitate the structural rearrangements of the outer and inner membrane proteins involved in the two import machineries in a way to permit the formation of a continuous import channel through the two mitochondrial membranes without mixing the cytoplasmic and mitochondrial aqueous contents.
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We describe a novel method for the purification of aPL, in which pure CL is immobilized on octyl-sepharose beads by hydrophobic interaction. No lipid contamination was present in eluates, and the system could be reutilized three times without loosing extracting capacity. Four patients with antiphospholipid syndrome were studied. A marked decrease in aCL and LA activities was found in all patient plasmas after the passage through a CL-octyl-sepharose column. Both activities were recovered in eluates which contained beta 2-GP-I and IgGs. beta 2-GP-I was also present in normal plasma eluates, which showed no aCL and slight LA activity. This method represents an improvement in the purification of aPL, and could be useful in explaining the mechanism of action of antibodies that are obtained using pure phospholipid as extracting matrix.
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Elevation of anticardiolipin antibodies has been observed in myocardial infarction and in many infections. To elucidate this topic, paired serum specimens from 40 patients with acute myocardial infarction were tested for anticardiolipin antibodies (solid-phase enzyme immunoassay) and enterobacterial common antigen antibodies (indirect hemagglutination test). Forty-one randomly selected individuals and 30 patients with chronic coronary heart disease served as controls. All individuals were males whose maximum age was 50 years. In patients with acute myocardial infarction the levels of anticardiolipin antibodies in paired sera rose significantly in all immunoglobulin classes (18% in the IgG class, 26% in the IgA class, and 43% in the IgM class), whereas no elevations occurred in the other groups. Fifteen of the acute myocardial infarction patients also showed at least a fourfold increase in enterobacterial common antigen antibodies, as compared with only one such increase in the two other groups combined. The increases were less marked than those seen in pronounced enterobacterial infections. These two reactions were closely associated.
HIV infection is associated with polyclonal increase in serum immunoglobulins and with elevated titers of serum antibodies to a variety of self antigens, including anti-phospholipid antibodies. In the present study, we found a high prevalence of 46.8% of serum IgG anticardiolipin antibodies (ACA) in a group of 111 unselected HIV-seropositive individuals. The presence of ACA was correlated with that of IgG antibodies to endothelial cells (AECA) but not with that of anti-beta 2 glycoprotein I antibodies, that were only found in 7.4% of the patients. The presence of IgG ACA was not associated with detectable lupus anticoagulant activity, nor with a history of thrombosis. Serum titers of ACA were not correlated with absolute numbers of circulating CD4+ cells. We found no relationship between the presence and titers of ACA, hypergammaglobulinemia, and serum titers of natural IgG autoantibodies to a panel of self antigens. Our results suggest that increased titers of ACA in HIV infection result from a biased expansion of B cell clones producing natural autoantibodies.
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