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PubMed1997

Influence of cardiolipin antibodies on the binding of treponemal specific antibodies in the fluorescence treponemal antibody absorption test and the Treponema pallidum immobilisation test.

The aim of the present study was to investigate the biological role of cardiolipin antibodies during Treponema pallidum infection. Inhibition of the binding of treponemal specific antibodies at the early and late stages of infection by cardiolipin antibodies was shown in the fluorescence treponemal antibody absorption (FTA-ABS) test and T. pallidum immobilisation (TPI) test. Incubation of treponemes with cardiolipin antibodies followed by a second incubation with treponemal specific antibodies resulted in a reduction of the titres of the FTA-ABS test and the TPI test. The findings suggest that cardiolipin antibody production should be considered as a virulence mechanism of pathogenic treponemes with the purpose of evading the host defence mechanisms.

Animals↗

PubMed1995

Binding of cardiolipin to polystyrene beads: evidence for a lamellar phase orientation.

The association of cardiolipin with polystyrene beads was studied using 31P-NMR and electron microscopy. In the presence and absence of fetal calf serum, cardiolipin appeared to bind to the polystyrene beads in lamellar phase as assessed by 31P-NMR imaging. Electron microscopic analysis revealed an even coating of phospholipid about the beads with extensive micelle binding. Cardiolipin-coated beads challenged with ACA-positive sera followed by immunogold indicated antibody bound to micelles associated with the bead. Studies conducted with ACA IgG purified from patient sera indicated that some ACA bound to CL beads in the absence of a source of ACA cofactor (i.e. gelatin-blocked beads), some ACA required beta 2-GPI for binding (i.e. no binding in the presence of beta 2-GPI-depleted plasma), whereas other ACA which showed negligible binding with gelatin-blocked beads, showed enhanced binding in the presence of beta 2-GPI-depleted plasma. The data indicate that: (1) cardiolipin binds to polystyrene beads in lamellar phase, (2) ACA bind to phospholipid micelles bound directly to the polystyrene beads, and (3) ACA differ between individuals displaying varying phospholipid and phospholipid/cofactor substrate specificities.

Antibodies, Anticardiolipin↗

PubMed1990

Anti-cardiolipin antibodies and HIV infection.

Anti-cardiolipin antibodies of IgG class were found in 48% of intravenous drug users, 38% of homosexuals and 14% of heterosexuals (with no other risk factor) infected with HIV. Anti-cardiolipin antibodies were not increased in HIV-negative heterosexual partners of HIV-infected patients, but mildly elevated levels were detected in HIV-negative drug users, relative to healthy controls unselected for HIV status. Among HIV infected drug users, anti-cardiolipin antibodies were not associated with thrombocytopenia, Pneumocystis carinii pneumonia, disease progression or clinical stage. Anti-cardiolipin antibodies appear to be another non-specific marker of HIV infection which may be particularly common in male intravenous drug users infected with the virus.

Autoantibodies↗

PubMed1988

Effective inhibition of cardiolipin-binding antibodies in gram-negative infections by bacterial lipopolysaccharide.

Anticardiolipin antibodies (ACA) were detected by solid-phase enzyme immunoassay in the majority of sera from patients with Gram-positive and Gram-negative bacterial infections. The response involved all the major immunoglobulin classes IgG, IgM, and IgA. The specificity of the ACA was studied in competitive inhibition experiments with three putative antigens: cardiolipin, lipopolysaccharide (LPS) isolated from Salmonella minnesota, strain Re 595, and synthetic Escherichia coli lipid A. The binding of IgG class ACA from the sera of five patients with Gram-negative infections was effectively inhibited by LPS, whereas 100-fold more cardiolipin was required for comparable inhibition. Pure lipid A was a less effective inhibitor of anticardiolipin activity than LPS. This pattern of reactivity was not seen in sera from patients with Gram-positive infections, syphilis, or systemic lupus erythematosus. Our findings suggest that cardiolipin may not be the inducing antigen for the cardiolipin-binding antibodies that develop in Gram-negative infections.

Antibody Specificity↗

PubMed1983

The effect of an integral membrane protein on lipid polymorphism in the cardiolipin-Ca2+ system.

The addition of Ca2+ to aqueous dispersions of cardiolipin triggers complete hexagonal (HII) phase formation at Ca2+/cardiolipin molar ratios greater than or equal to 1.0 as detected by 31PNMR and freeze-fracture electron microscopy. Incorporation of the integral membrane protein glycophorin prevents the bilayer leads to hexagonal (HII) phase transition at Ca2+/cardiolipin ratios as high as 15:1. Removal of the outwardly oriented, negatively charged sialic-acid-containing sugar groups of glycophorin with trypsin had little effect on the bilayer-stabilizing capacity of the protein. As the Ca2+ binding was found to be similar in both the cardiolipin and the cardiolipin-glycophorin systems, it can be concluded that the protein exerts a bilayer-stabilizing effect on the cardiolipin. In addition, the possibility that glycophorin may prevent vesicle fusion is also discussed.

Calcium↗

PubMed1986

An essential requirement of cardiolipin for mitochondrial carnitine acylcarnitine translocase activity. Lipid requirement of carnitine acylcarnitine translocase.

The phospholipid requirement for the optimal solubilization of carnitine acylcarnitine translocase from the inner membrane vesicles of rat liver mitochondria and for its reconstitution in liposomes was investigated. At the octylglucoside-solubilization step, the presence of cardiolipin proved superior to the other lipids tested. For reconstitution, a mixture having phosphatidylcholine, phosphatidylethanolamine and cardiolipin was found to be particularly effective. The requirement of cardiolipin at this step was met less effectively by other anionic phospholipids. Moreover, in intact mitochondria of rat liver and heart, the translocase activity was markedly inhibited by micromolar concentrations of doxorubicin, a specific cardiolipin-binding agent.

Acyltransferases↗

PubMed1994

Direct analysis and significance of cardiolipin transverse distribution in mitochondrial inner membranes.

The distribution of cardiolipin across the inner mitochondrial membrane was directly determined by using the ability of the fluorescent dye 10-N-nonyl-3,6-bis(dimethylamino)acridine (10-N-nonyl acridine orange) to form dimers when it interacts with the diacidic phospholipid. Two independent methods were employed: (a) a spectrophotometric measurement of 10-N-nonyl acridine orange binding to isolated rat liver mitochondria, mitoplasts and inside-out submitochondrial particles, and (b) a flow-cytometric analysis of specific red fluorescence, emitted when two dye molecules are bound to one membrane cardiolipin; the stoichiometry of 10-N-nonyl acridine orange binding to phosphatidylserine and phosphatidylinositol, 1 mol dye/mol phospholipid, prevented dye dimerisation and subsequent red-fluorescence appearance. 57% total cardiolipin was present in the outer leaflets of inner membranes of isolated organelles, a distribution confirmed by saturation measurements for mitoplasts and inside-out submitochondrial particles. The same asymmetry was directly observed in situ with mitochondrial membranes of quiescent L1210 cells, and with mitochondrial membranes of respiring yeasts. Nevertheless, alterations in ATP synthesis and inhibition of mitochondrial protein synthesis revealed that cardiolipin distribution was apparently tightly correlated with mitochondrial membrane assembly and activity.

Acridine Orange↗

PubMed1988

Binding affinity of serum immunoglobulin G to cardiolipin and other phospholipids in patients with systemic lupus erythematosus and syphilis.

Qualitative and quantitative assays for human antibodies to cardiolipin and other phospholipids were used in tests for these reactions in sera from patients with systemic lupus erythematosus (SLE) and syphilis. Of 22 SLE serum samples tested by the qualitative assay, 8 showed positive staining to cardiolipin, phosphatidic acid, and/or phosphatidylserine. All 47 syphilitic sera reacted with these three phospholipids. The apparent affinity of anticardiolipin binding was estimated by normalizing absolute binding levels as a function of serum concentration to the maximum percent bound. It was evident that antibody affinity was four- to fivefold lower in the SLE sera than in the syphilitic sera. Twelve serum samples from patients with one or more features of the anti-cardiolipin syndrome demonstrated mean binding values which were not distinguishable from binding in other SLE sera. In sera from patients with active SLE, binding affinity for cardiolipin was somewhat greater than that in samples from patients with inactive disease, but the differences were not statistically significant. The low anticardiolipin binding affinity which was observed in patients with SLE compared with that in patients with syphilis casts doubt on a pathogenic role for these reactions.

Adult↗

PubMed1974

Anti-cardiolipin and anti-phosphatidylglycerol antibodies prepared against bacterial phospholipids.

Anti-phosphatidylglycerol and anti-cardiolipin antisera were prepared in rabbits by using phospholipids purified from Micrococcus lysodeikticus. Anti-phosphatidylglycerol antibodies were found in antisera when either phosphatidylglycerol or cardiolipin were used as immunogens, but adsorption studies indicated they were not similar. Antibodies which reacted with phosphatidylinositol and phosphatidic acid were also found in the anti-cardiolipin antiserum. Structures of the antigenic groups in phosphatidylglycerol and cardiolipin are suggested from cross-reaction and adsorption studies. Adsorption studies with pure phospholipid antigens indicated the importance of the spacial orientation of phospholipid haptens for immunological reactivity.

Animals↗

PubMed1984

Correlation of 3,4-dihydroxybutyl 1-phosphonate resistance with a defect in cardiolipin synthesis in Escherichia coli.

Escherichia coli treated for 1 h with 100 microM rac-3,4-dihydroxybutyl 1-phosphonate (DBP), a glycerol-3-phosphate analog, die when sorted at 5 degrees C, whereas the viability of untreated cells is relatively unaffected. This observation formed the basis of a selection procedure that was used to isolate mutants that are partially resistant to DBP. One such mutant, strain 6204, is constitutive for DBP transport, exhibits a particularly high degree of cold resistance, has the same doubling time as the parent, and is similar to the parent strain in terms of incorporation of DBP into the lipid fraction. Glycerol-3-phosphate and phosphatidylglycerol phosphate synthetases obtained from strain 6204 and its parent were identical in terms of DBP recognition. The parent strain is killed when incubated in the presence of a combination of 70 microM rac-DBP and 0.25% deoxycholate, whereas strain 6204 continues to grow, albeit more slowly, in the presence of this combination. Strain 6204 can be distinguished from the parent strain on agar plates (low phosphate minimal medium with glucuronate as the sole carbon source) containing 15 microM rac-DBP. The insertion of Tn10 near the 6204 mutation has facilitated genetic manipulations. All phenotypic effects attributed to strain 6204 appear to be due to a single mutation. Genetic analysis indicates that Tn10, inserted near the gene responsible for DBP resistance, maps in the vicinity of 27 min. Three-factor crosses reveal a gene order of hemA-Dbpr-Tn10(zch)-trp. The only gene for phosphoglyceride metabolism known to map in this region is the gene associated with cardiolipin synthetase, cls. Genetic results suggest that the mutation responsible for DBP resistance maps in or very near cls. Analysis of the lipids isolated from untreated strain 6204 (and from each of the transductants prepared by P1 vir-mediated transfer of DBP resistance of wild-type strains) reveals that cardiolipin synthesis is defective. These results strongly suggest that the mutation responsible for DBP resistance has its primary effect on cardiolipin synthesis. To further test this hypothesis, strains with an authentic cls mutation were constructed and examined for resistance to DBP. These strains had growth properties that were identical with those of strain 6204. Wild-type strains and mutants defective in cardiolipin synthesis were treated with DBP and 20 mM magnesium or calcium chloride. Simultaneous treatment of either cell type with DBP and divalent cation not only failed to stimulate growth but, quite the contrary, had a marked synergistic growth inhibitory effect.

Butylene Glycols↗

PubMed2003

Membrane interaction of the glycosyltransferase MurG: a special role for cardiolipin.

MurG is a peripheral membrane protein that is one of the key enzymes in peptidoglycan biosynthesis. The crystal structure of Escherichia coli MurG (S. Ha, D. Walker, Y. Shi, and S. Walker, Protein Sci. 9:1045-1052, 2000) contains a hydrophobic patch surrounded by basic residues that may represent a membrane association site. To allow investigation of the membrane interaction of MurG on a molecular level, we expressed and purified MurG from E. coli in the absence of detergent. Surprisingly, we found that lipid vesicles copurify with MurG. Freeze fracture electron microscopy of whole cells and lysates suggested that these vesicles are derived from vesicular intracellular membranes that are formed during overexpression. This is the first study which shows that overexpression of a peripheral membrane protein results in formation of additional membranes within the cell. The cardiolipin content of cells overexpressing MurG was increased from 1 +/- 1 to 7 +/- 1 mol% compared to nonoverexpressing cells. The lipids that copurify with MurG were even further enriched in cardiolipin (13 +/- 4 mol%). MurG activity measurements of lipid I, its natural substrate, incorporated in pure lipid vesicles showed that the MurG activity is higher for vesicles containing cardiolipin than for vesicles with phosphatidylglycerol. These findings support the suggestion that MurG interacts with phospholipids of the bacterial membrane. In addition, the results show a special role for cardiolipin in the MurG-membrane interaction.

Bacterial Outer Membrane Proteins↗

PubMed2004

Cell membranes and apoptosis: role of cardiolipin, phosphatidylcholine, and anticancer lipid analogues.

The apoptotic program utilizes cellular membranes to transduce and generate operative signals. Lipids are major components of cellular membranes and have the potential to control the effectiveness of the signal by directing it to the proper location, being a source of new signals or as mediators in the response. These possible lipid functions are illustrated in the present review, focussing on the role that two different phospholipids, cardiolipin and phosphatidyl choline, play in apoptosis. Mitochondria have a central role in apoptosis, and many important aspects of the process mediated by this organelle converge through its distinctive lipid cardiolipin. Specifically, changes in cardiolipin metabolism have been detected in early steps of the death program and it is postulated (i) to mediate recruitment of pro apoptotic proteins like Bid to the mitochondria surface and (ii) to actively participate in the release of proteins relevant for the execution phase of apoptosis, like cytochrome c. Unlike the organelle specific distribution of cardiolipin, phosphatidylcholine is widely distributed among all organelles of the cell. The importance of phosphatidylcholine in apoptosis has been approached mainly through the study of the mode of action of (i) phosphatidylcholine anticancer analogues such as edelfosine and (ii) molecules that alter phosphatidylcholine metabolism, such as farnesol. The contribution of phosphatidylcholine metabolism to the apoptotic program is discussed, analyzing the experimental evidence available and pointing out some controversies in the proposed mechanisms of action.

Animals↗

PubMed1977

Further studies on the cardiolipin phosphodiesterase of Escherichia coli.

The cardiolipin phosphodiesterase of Escherichia coli was further characterized. This enzyme has a pH optimum of 7.0 and is Mg2+ dependent. Mn2+ and Co2+ could replace Mg2+ but other divalent cations were inhibitory or without effect. The enzyme is not periplasmic and does not appear to be associated with membrane fractions prepared by different methods. It is recovered as a soluble protein in the cytosol fraction but could not be readily purified because of its instability. With cell-free systems, a requirement for ATP or ADP could be shown under certain defined conditions. Other nucleotides were less effective or ineffective in stimulating the phosphodiesterase. The cells displayed the highest activity during the middle to late exponential stage but no marked requirement for ATP was apparent when the phosphodiesterase was obtained from such freshly grown cells. If, however, cells were starved for several hours in saline medium, the cardiolipin phosphodiesterase level fell and a requirement for added ATP could be shown. The cardiolipin phosphodiesterase is an enzyme distinct from cardiolipin synthase. The assay conditions are quite different from each of these enzymes as are their subcellular distributions.

Adenosine Diphosphate↗

PubMed2004

Ischemia, rather than reperfusion, inhibits respiration through cytochrome oxidase in the isolated, perfused rabbit heart: role of cardiolipin.

Ischemia and reperfusion result in mitochondrial dysfunction, with decreases in oxidative capacity, loss of cytochrome c, and generation of reactive oxygen species. During ischemia of the isolated perfused rabbit heart, subsarcolemmal mitochondria, located beneath the plasma membrane, sustain a loss of the phospholipid cardiolipin, with decreases in oxidative metabolism through cytochrome oxidase and the loss of cytochrome c. We asked whether additional injury to the distal electron chain involving cardiolipin with loss of cytochrome c and cytochrome oxidase occurs during reperfusion. Reperfusion did not lead to additional damage in the distal electron transport chain. Oxidation through cytochrome oxidase and the content of cytochrome c did not further decrease during reperfusion. Thus injury to cardiolipin, cytochrome c, and cytochrome oxidase occurs during ischemia rather than during reperfusion. The ischemic injury leads to persistent defects in oxidative function during the early reperfusion period. The decrease in cardiolipin content accompanied by persistent decrements in the content of cytochrome c and oxidation through cytochrome oxidase is a potential mechanism of additional myocyte injury during reperfusion.

Animals↗

PubMed1997

Antibodies against cardiolipin and oxidatively modified LDL in 50-year-old men predict myocardial infarction.

Autoantibodies against oxidatively modified low-density lipoproteins (oxLDL) and cardiolipin occur in patients with vascular diseases, including atherosclerosis. The ability of such antibodies to predict myocardial infarction (MI) was investigated in a prospective nested case-control study in which healthy 50-year-old men were followed up for 20 years. Raised levels of antibodies against oxLDL and cardiolipin at 50 years of age correlated positively with the incidence of MI and mortality related to MI 10 to 20 years later. IgG and IgA antibodies against cardiolipin were associated with MI between 50 to 60 years of age and IgG and IgA antibodies against oxLDL with MI at 60 to 70 years of age. Moreover, higher antibody levels were noted in those who died from acute MI in comparison to those who survived. The predictive power of IgA and IgG antibodies was strong and largely independent of that of other strong risk factors. In conclusion, raised levels of antibodies against oxLDL and cardiolipin may predict MI and MI-related death.

Aged↗

PubMed2002

Linoleic acid supplementation of Barth syndrome fibroblasts restores cardiolipin levels: implications for treatment.

The object of this study was to investigate whether the levels of cardiolipin in cultured skin fibroblasts of patients with Barth syndrome (BTHS) can be restored by addition of linoleic acid to growth media. To this end, fibroblasts from controls and BTHS patients were grown in the presence or absence of linoleic acid. High-performance liquid chromatography-electrospray ionization tandem mass spectrometry was used for quantitative and compositional analysis of cardiolipin. Incubation of cells from both BTHS and controls with different concentrations of linoleic acid led to a dose- and time-dependent increase of cardiolipin levels. The increased levels of cardiolipin in fibroblasts of BTHS patients after treatment with linoleic acid indicate that an increased amount of linoleic acid in the diet might be beneficial to BTHS patients.

Adolescent↗

PubMed2001

Chromatin-bound cardiolipin: the phospholipid of proliferation.

Chromatin-bound lipids, cardiolipin (CL), diglycerides, cholesterol, and cholesterol esters, together with nonhistone proteins, play a key role in structural and functional organization of the chromatin genome during various stages of evolution. There are two pools of chromatin lipids, namely loosely- and tightly-bound lipids. The entire chromatin cardiolipin is bound to DNA. The CL molecule has a common 'interphosphate' structural motive with DNA, i.e. DNA and CL phosphate moieties separated from each other with six chemical bonds and equidistant, which is important for CL functional role, the regulation of gene expression. The CL dominates in the DNA of the active genome but not in the DNA of the repressed genome. The amount of CL in the DNA from the repressed genome of pigeon erythrocytes (one CL molecule per 20 nucleosomes) is 20 times less than in the DNA from the active genome of rat thymus and liver and in the DNA of transformed cells. Cardiolipin provides A-form DNA in the complex with RNA-polymerase, which is necessary for transcription. The biological and structural function of cardiolipin can be realised only when unsaturated fatty acyl residues are present in its structure.

Animals↗

PubMed1992

Reversible, nonionic, and pH-dependent association of cytochrome c with cardiolipin-phosphatidylcholine liposomes.

Membrane association of cytochrome c (cyt c) was monitored by the efficiency of resonance energy transfer from a pyrene-fatty acid containing phospholipid derivative (1-palmitoyl-2[6-(pyren-1-yl)]hexanoyl-sn-glycero-3-phosphocholine (PPHPC)) to the heme of cyt c. Liposomes consisted of 85 mol% egg phosphatidylcholine (egg PC), 10 mol% cardiolipin, and 5 mol% PPHPC. Cardiolipin was necessary for the membrane binding of cyt c over the pH range studied, from 4 to 7. In accordance with the electrostatic nature of the membrane association of cyt c at neutral pH both 2 mM MgCl2 and 80 mM NaCl dissociated cyt c from the vesicles completely. At neutral pH also adenine nucleotides in millimolar concentrations were able to displace cyt c from liposomes, their efficiency decreasing in the sequence ATP > ADP > AMP. In addition, both CTP and GTP were equally effective as ATP. The detachment of cyt c from liposomes by nucleotides is likely to result from a competition between cardiolipin and the nucleotides for a common binding site in cyt c. When pH was decreased to 4 there was a small yet significant increase in the apparent affinity of cyt c to cardiolipin containing liposomes. Notably, at pH 4 the above nucleotides as well as NaCl and MgCl2 were no longer able to dissociate cyt c and, on the contrary, they slightly enhanced the quenching of pyrene fluorescence by cyt c. The above results do suggest that the membrane association of cyt c at acidic pH was non-ionic and presumably due to hydrogen bonding. The pH-dependent binding of cyt c to membranes was fully reversible. Accordingly, in the presence of sufficient concentrations of either nucleotides or salts rapid detachment and membrane association of cyt c could be induced by varying pH between neutral and acidic values, respectively.

Adenine Nucleotides↗