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PubMed1982

Separation of phospholipids and individual molecular species of phospholipids by high-performance liquid chromatography.

Isocratic high-performance liquid chromatography methods are described for separating the major classes of phospholipids and for isolating the individual molecular species of phospholipids. Fractionation of a total lipid extract of rat liver on a silica column resulted in quantitative recoveries of all major phospholipids with preservation of their fatty acid composition. Rat liver phosphatidylcholine, phosphatidylethanolamine, phosphatidylinositol, and phosphatidylserine were then each chromatographed on a C18 reverse phase column to isolate individual molecular species. Component peaks were identified by their fatty acid composition and quantitated by phosphorus determination. Using this method we found that for each of these phospholipids from 30 to 35 different molecular species can be routinely identified and reproducibly quantitated. A characteristic elution sequence of molecular species permitted their identification based upon their retention times on a reverse phase column.

Animals↗
PubMed1981

Cooperative roles of various membrane phospholipids in the activation of calcium-activated, phospholipid-dependent protein kinase.

Although phosphatidylserine is the sole phospholipid effective for the activation of Ca2+-activated, phospholipid-dependent protein kinase in the presence of a small amount of unsaturated diacylglycerol and micromolar concentrations of Ca2+ (Takai, Y., Kishimoto, A., Kikkawa, U., Mori, T., and Nishizuka, Y. (1979) Biochem. Biophys. Res. Commun. 91, 1218-1224), other species of phospholipids modulate the activation of enzyme considerably. When phosphatidylserine is supplemented with phosphatidylethanolamine, further enhancement of the enzymatic activity is observed. Inversely, the addition of phosphatidylcholine or sphingomyelin markedly diminishes the enzyme activation by phosphatidylserine. Phosphatidylinositol, which serves as the source of unsaturated diacylglycerol, and phosphatidic acid do not show significant effects. Kinetic analysis has indicated that phosphatidylethanolamine enhances the enzyme activation by marked increase in the affinity of enzyme for Ca2+ and also by slight increase in the affinity for phosphatidylserine as well as for unsaturated diacylglycerol without affecting the maximum reaction velocity. Phosphatidylcholine and sphingomyelin diminish the enzyme activation in an uncompetitive manner with respect to Ca2+ and in a competitive manner with respect to both phosphatidylserine and unsaturated diacylglycerol. These results suggest that each species of the various membrane phospholipids plays a specific role with positive or negative cooperativity in the activation of this unique protein kinase.

Animals↗
PubMed1995

The complex of phosphatidylinositol 4,5-bisphosphate and calcium ions is not responsible for Ca2+-induced loss of phospholipid asymmetry in the human erythrocyte: a study in Scott syndrome, a disorder of calcium-induced phospholipid scrambling.

Elevation of cytoplasmic Ca2+ levels in human erythrocytes induces a progressive loss of membrane phospholipid asymmetry, a process that is impaired in erythrocytes from a patient with Scott syndrome. We show here that porcine erythrocytes are similarly incapable of Ca2+-induced redistribution of membrane phospholipids. Because a complex of phosphatidylinositol 4,5-bisphosphate (PIP2) and Ca2+ has been proposed as the mediator of enhanced transbilayer movement of lipids (J Biol Chem 269:6347,1994), these cell systems offer a unique opportunity for testing this mechanism. Analysis of both total PIP2 content and the metabolic-resistant pool of PIP2 that remains after incubation with Ca2+ ionophore showed no appreciable differences between normal and Scott erythrocytes. Moreover, porcine erythrocytes were found to have slightly higher levels of both total and metabolic-resistant PIP2 in comparison with normal human erythrocytes. Although loading of normal erythrocytes with exogenously added PIP2 gave rise to a Ca2+-induced increase in prothrombinase activity and apparent transbilayer movement of nitrobenzoxadiazolyl (NBD)-phospholipids, these PIP2-loaded cells were also found to undergo progressive Ca2+-dependent cell lysis, which seriously hampers interpretation of these data. Moreover, loading Scott cells with PIP2 did not abolish their impaired lipid scrambling, even in the presence of a Ca2+-ionophore. Finally, artificial lipid vesicles containing no PIP2 or 1 mole percent of PIP2 were indistinguishable with respect to transbilayer movement of NBD-phosphatidylcholine in the presence of Ca2+. Our findings suggest that Ca2+-induced redistribution of membrane phospholipids cannot simply be attributed to the steady-state concentration of PIP2, and imply that such lipid movement is regulated by other cellular processes.

4-Chloro-7-nitrobenzofurazan↗
PubMed1998

Antimalarial activity of 77 phospholipid polar head analogs: close correlation between inhibition of phospholipid metabolism and in vitro Plasmodium falciparum growth.

Seventy-seven potential analogs of phospholipid polar heads, choline and ethanolamine, were evaluated in vitro as inhibitors of Plasmodium falciparum growth. Their IC50 ranged from 10(-3) to 10(-7) mol/L. Ten compounds showed similar antimalarial activity when tested against three different parasite strains (2 chloroquine-sensitive strains and 1 chloroquine-resistant strain). Compounds showing marked antimalarial activity were assayed for their effects on phospholipid metabolism. The most active compounds (IC50 of 1 to 0.03 micromol/L) were inhibitors of de novo phosphatidylcholine (PC) biosynthesis from choline. For a series of 50 compounds, there was a close correlation between impairment of phospholipid biosynthesis and inhibition of in vitro malaria parasite growth. High choline concentrations caused a marked specific shift in the curves for PC biosynthesis inhibition. Concentrations inhibiting 50% PC metabolism from choline were in close agreement with the Ki of these compounds for the choline transporter in Plasmodium knowlesi-infected erythrocytes. By contrast, measurement of the effects of 12 of these compounds on rapidly dividing lymphoblastoid cells showed a total absence of correlation between parasite growth inhibition and human lymphoblastoid cell growth inhibition. Specific antimalarial effects of choline or ethanolamine analogs are thus likely mediated by their alteration of phospholipid metabolism. This indicates that de novo PC biosynthesis from choline is a very realistic target for new malaria chemotherapy, even against pharmacoresistant strains.

Animals↗
PubMed1998

Characterization of phospholipids in pre-alpha HDL: selective phospholipid efflux with apolipoprotein A-I.

Previously, we have shown that lipid-free apoA-I, when incubated with fibroblasts, will produce lipoproteins of pre-alpha mobility (Asztalos, B. F., et al. 1997. Arterioscler. Thromb. Vasc. Biol. 17: 1630-1636). In order to understand the nature of these pre-alpha particles, we further characterized their lipid content. The pre-alpha particles are high density lipoproteins, having a median density of 1.08 g/ml. They have a surface charge of -18.45 mV. The phospholipid composition of these particles showed that they have 4% each of phosphatidyl ethanolamine and inositol; 69% phosphatidyl choline and 18% sphingomyelin. This phospholipid composition is different from those of plasma HDL (81% phosphatidyl choline, 13% sphingomyelin), plasma membrane on the fibroblasts, and whole fibroblast phospholipid. To demonstrate that the pre-alpha mobility resides in the lipids, lipids from pre-alpha lipoproteins were reconstituted with lipid-free apoA-I. The resultant particles retained their pre-alpha mobility. We conclude that apoA-I may react with specific regions of plasma membrane to acquire this unusual lipid composition and that pre-alpha mobility is caused in part by the unusual phospholipid composition.

Apolipoprotein A-I↗
PubMed1998

[Changes in the contents of membrane phospholipid and membrane phospholipid asymmetry in glucose-6-phosphate dehydrogenase deficient erythrocyte].

OBJECTIVE: To study the effect of G6PD deficiency on membrane phospholipid structures. METHODS: Treatment of intact erythrocyte with phospholipase A2 was used for the membrane phospholipid asymmetry. Membrane phospholipid was determined by high performance liquid chromatography (HPLC). RESULTS: The contents of phosphatidylethanolamine (PE), phosphatidylcholine (PC), phosphatidylserine (PS) were 5.18 +/- 1.86, 1.51 +/- 0.58 and 5.70 +/- 1.91 mg/mg membrane protein, respectively, in G6PD deficient erythrocytes and were 5.59 +/- 1.16, 2.92 +/- 0.50 and 6.64 +/- 0.92 mg/mg membrane protein, respectively, in normal erythrocytes. In normal erythrocytes, 17.6% +/- 2.5% PE and 57.9% +/- 4.7% PC were present and no PS was found on the outer leaflet of the membrane. While in G6PD deficient ones, 30.2% +/- 5.7% PE, 53.8% +/- 7.4% PC and 27.2% +/- 5.8% PS were present on the outer leaflet. CONCLUSION: Membrane phospholipid changes in G6PD deficient erythrocytes might be one of the factors causing hemolysis.

Erythrocyte Membrane↗
PubMed1994

Reduction of HDL- and LDL-associated cholesterylester and phospholipid hydroperoxides by phospholipid hydroperoxide glutathione peroxidase and Ebselen (PZ 51).

The reaction of phospholipid hydroperoxide glutathione peroxidase (PHGPx) and Ebselen with phospholipid and cholesterylester hydroperoxides associated with HDLox and LDLox was investigated using specific HPLC assays for the hydroperoxides of phosphatidylcholine (PCOOH) and cholesteryllinolate (Ch18:2-OOH) and for cholesteryllinolate hydroxides (Ch18:2-OH). HDLox and LDLox were formed from the corresponding isolated native lipoproteins by controlled and limited oxidation initiated by aqueous peroxyl radicals. Incubation of HDLox or LDLox in the presence of PHGPx/GSH or Ebselen/GSH resulted in rapid degradation of both classes of lipid hydroperoxides, with equimolar amounts of Ch18:2-OH formed from Ch18:2-OOH. No pronounced differences were observed between PCOOH and Ch18:2-OOH in terms of substrate specificity, whereas HDLox-associated PCOOH and Ch18:2-OOH appeared to be slightly better substrates for PHGPx/GSH as compared to those in LDLox. Also, Ch18:2-OOH associated with HDLox but not LDLox were reduced by Ebselen or GSH alone. These in vitro findings indicate that the enzymatic PHGPx/GSH and the nonenzymatic Ebselen/GSH systems can efficiently reduce hydroperoxides of phospholipids and cholesterylesters associated with intact lipoproteins.

Azoles↗
PubMed1982

Phospholipid composition of subcellular fractions and phospholipid-exchange activity in chicken liver and MC-29 hepatoma.

The phospholipid composition of mitochondria, microsomes and plasma membranes from liver and MC-29 hepatoma from White Leghorn chickens has been investigated. It was established that all mitochondria and microsome phospholipid fractions obtained from MC-29 hepatoma are increased strongly compared to those from liver. The sphingomyelin augmentation was particularly great. In hepatoma plasma membranes only the sphingomyelin quantity was increased. Sphingomyelin- and phosphatidylcholine-exchange activities were observed in avian liver for the first time. These two activities were increased in MC-29 hepatoma cells. Three phospholipid-exchange proteins have been established in chicken liver 105000 X g supernatant. One of them specifically transports phosphatidylcholine, the second one is non-specific for phosphatidylcholine and sphingomyelin, and the third one is specific only for sphingomyelin. In hepatoma cells only a non-specific phosphatidylcholine- and sphingomyelin-exchange protein was found.

Animals↗
PubMed1989

Lateral diffusion of phospholipids in the lipid surface of human low-density lipoprotein measured with a pyrenyl phospholipid probe.

Human low-density lipoprotein (LDL) was labelled with the excimeric fluorescent phospholipid analogue 1-palmitoyl-2-(1'-pyreneoctanoyl)-sn-glycero-3-phosphocholine by using phosphatidylcholine-specific transfer protein for the probe insertion. The lateral diffusivity of the probe in the phospholipid/cholesterol surface monolayer of LDL was determined from the measured dependence of the pyrene monomer fluorescence yield on probe concentration. The data were analyzed by the milling-crowd model (J. Eisinger et al. (1986) Biophys. J. 49, 987-1001] to obtain the short-range lateral diffusivity of the probe. The lateral mobility of the probe in LDL was compared to that in model lipid systems, i.e. in protein-free LDL-like lipid particles and in small unilamellar vesicles, with a phospholipid/cholesterol composition characteristic of LDL. This analysis with the probability PE = 1 for excimer production between nearest-neighbour probes gives the lower limits for f, the frequency of translational lipid--lipid exchanges of the probe of 0.62 x 10(8), 0.19 x 10(8) and 0.19 x 10(8)s-1 in LDL, LDL-like lipid particles, and small unilamellar vesicles, respectively. The lower limits for the corresponding lateral diffusion constants are 16, 5 and 5 microns 2 s-1. The results suggest that the translational mobility of phospholipid molecules in the lipid--protein surface of LDL is not constrained by the apolipoprotein B-100 moiety or the neutral lipid core of the lipoprotein. Instead, the protein moiety may perturb the lipid order with the lipid--associating peptide domains and thus fluidize the amphiphilic surface monolayer of LDL relative to the protein-free model systems. In general, lateral diffusivity of the pyrenyl phospholipid probe in LDL and the model lipid systems is comparable to the lateral mobility of lipid analogue probes in a variety of model and biological membranes.

Androgen-Binding Protein↗
PubMed2002

Attachment of water-soluble proteins to the surface of (magnetizable) phospholipid colloids via NeutrAvidin-derivatized phospholipids.

The present work describes the incorporation of a functionalized phospholipid derivative into the phospholipid bilayer of both classical small unilamellar vesicles and recently developed magnetoliposomes, resulting in unique biocolloid structures onto which peripheral water-soluble enzymes can be immobilized on the surfaces. In the first part of this work, a synthesis protocol is outlined for a universal membrane anchor for water-soluble proteins. Dioleoylphosphatidylethanolamine-N-dodecanyl was used as the starting lipid molecule. After activation of the terminal -COOH group, alpha,omega-diamino-poly(ethylene glycol), used as a hydrophilic, flexible spacer arm, was coupled covalently. Subsequently, NeutrAvidin was bound, after blocking the free -NH(2) groups with citraconic anhydride. In the second part, the resulting lipid-NeutrAvidin derivative was incorporated into small unilamellar vesicles comprised of dimyristoylphosphatidylglycerol. FPLC with Superdex 200 as the column matrix clearly showed that biotinylated alkaline phosphatase, which served as a representative model of water-soluble proteins, was attached to the vesicles. Furthermore, magnetoliposomes, constructed of the same type of phospholipid molecules, were presented as interesting colloids to assess the degree of enzyme immobilization in a rapid and elegant manner. Potential applications that can emerge from this study are briefly discussed.

Avidin↗
PubMedDate not supplied

Axon-myelin transfer of phospholipids and phospholipid precursors. Labeling of myelin phosphoinositides through axonal transport.

Previous studies have provided evidence for axon-to-myelin transfer of intact lipids and lipid precursors for reutilization by myelin enzymes. Several of the lipid constituents of myelin showed significant contralateral/ipsilateral ratios of incorporated radioactivity, indicative of axonal origin, whereas proteins and certain other lipids did not participate in this transfer-reutilization process. The present study will examine the labeling of myelin phosphoinositides by this pathway. Both 32PO4 and [3H]inositol were injected monocularly into 7-9-wk-old rabbits and myelin was isolated 7 or 21 days later from pooled optic tracts and superior colliculi. In total lipids 32P counts of the isolated myelin samples showed significant contralateral/ipsilateral ratios as well as increasing magnitude of contralateral-ipsilateral differences during the time interval. Thin-layer chromatographic isolation of the myelin phosphoinositides revealed significant 32P-labeling of these species, with PIP and PIP2 showing time-related increases. This resembled the labeling pattern of the major phospholipids from rabbit optic system myelin in a previous study and suggested incorporation of axon-derived phosphate by myelin-associated enzymes. The 32P label in PI, on the other hand, remained constant between 7 and 21 days, suggesting transfer of intact lipid. This was supported by the labeling pattern with [3H]inositol, which also showed no increase over time for PI. These results suggest axon-myelin transfer of intact PI followed by myelin-localized incorporation of axon-derived phosphate groups into PIP and PIP2. The general topic of axon-myelin transfer of phospholipids and phospholipid precursors is reviewed.

Animals↗
PubMed2005

Simvastatin and preparation of polyunsaturated phospholipids produce similar changes in the phospholipid composition of high-density lipoproteins during hypercholesterolemia.

We studied the phospholipid composition of high-density lipoproteins in patients with coronary heart disease and hypercholesterolemia treated with simvastatin (Zocor, inhibitor of the key enzyme of cholesterol synthesis) and preparation of polyunsaturated phospholipids (lipostabil forte). Simvastatin produced a hypolipidemic effect and modulates the phospholipid composition of high-density lipoproteins (similarly to lipostabil forte). These changes contribute to functional activity of high-density lipoproteins in the reverse cholesterol transport.

Adult↗
PubMed1987

Interaction of spectrin with phospholipids. Quenching of spectrin intrinsic fluorescence by phospholipid suspensions.

Phospholipid suspensions prepared of phosphatidylethanolamine, phosphatidylserine and their mixtures are able to influence the intrinsic protein fluorescence of spectrin. In the case of phosphatidylethanolamine suspension up to 75% of protein fluorescence can be quenched. The interaction of phospholipid aggregates with spectrin is modulated by pH and ionic strength. Phospholipids, particularly phosphatidylethanolamine display a 'stabilizing' effect against the changes of protein fluorescence induced by increasing ionic strength and by thermal denaturation.

Erythrocyte Membrane↗
PubMed1993

Effects of differentiation on the phospholipid and phospholipid fatty acid composition of N1E-115 neuroblastoma cells.

The effects of differentiation on the phospholipid and phospholipid fatty acid composition of N1E-115 neuroblastoma cells were determined. The cellular lipids were extracted on days 0, 3 and 7, following the addition of 1.2% dimethylsulfoxide to induce cellular differentiation. Proportions of ethanolamine glycerophospholipids (EtnGpl), phosphatidylinositol (PtdIns) and sphingomyelin (CerPCho) were significantly elevated following differentiation. The mole percentage of choline glycerophospholipids (ChoGpl) decreased with differentiation. The plasmalogens, both choline and ethanolamine, increased by 1.3- and 2.3-fold, respectively, during differentiation. The fatty acid composition of the phospholipid classes was also altered. PtdIns and ChoGpl had decreased proportions of polyenoic fatty acids, while these proportions were increased in EtnGpl. Both ChoGpl and EtnGpl had increased n-3/n-6 series fatty acid ratios, but this ratio was decreased in PtdIns. The mole percentage of arachidonic acid was significantly decreased in both PtdIns and ChoGpl, but elevated in EtnGpl and may be a result of the increase in ethanolamine plasmalogen. Thus, differentiation did not increase the overall mole percentage of polyenoic FA in the cells nor increase the n-6 series fatty acid proportions. We speculate plasmalogens may have a role in the differentiation process or in maintaining the cell in the differentiated state.

Cell Differentiation↗
PubMed1980

Altered phospholipid composition and changed fatty acid pattern of the various phospholipid fractions of red cell membranes of cystic fibrosis children with pancreatic insufficiency.

After two-dimensional thin-layer chromatography, it appears that the phospholipid composition of the erythrocyte membranes of cystic fibrosis children, compared with healthy ones, is changed by an increase of the phosphatidyl inositol content. The plasmalogen concentration of the membrane phospholipids is the same for both groups. The fatty acid pattern of the various red cell membrane phospholipid fractions was determined by gas chromatography (Tables II, III and IV), and significant changes were observed in the cystic fibrosis patients (Table V). Phosphatidyl choline and ethanolamine (non-plasmalogen forms) especially show strikingly abnormal fatty acid patterns similar to those in the various plasma lipid fractions.

Child↗
PubMed1983

Non-uniform distribution of phospholipids in (Na+ + K+)-ATPase-rich membranes from Torpedo marmorata electric organ evidenced by spin-spin interactions between spin-labeled phospholipids.

(Na+ + K+)-ATPase membranes from Torpedo marmorata electric organ were labeled with high concentrations of paramagnetic phospholipid analogs (up to 5 mol of spin labels for 100 mol of endogeneous phospholipids). The mobile lipid bilayer component of the complex resonance spectra obtained showed low-field linewidth broadening due to spin-spin interactions; this was used as a measure of probe concentration in this compartment. Our results show that in the lipid shell surrounding the protein, there is a considerable enrichment in negatively charged phospholipids over neutral ones.

Animals↗
PubMed1984

Phospholipid composition and metabolism of crustacean gills as related to changes in environmental salinities: relationship between Na+-K+-ATPase activity and phospholipids.

The phospholipid composition and metabolism are studied in crustacean gills. It is reported that branchiae are rich in PC, PE and DPG and abundant in long chain polyunsaturated fatty acids (20:4 omega 6 and 20:5 omega 3 acids). The pathways of phospholipids synthesis appear similar to those described for vertebrates. It is demonstrated that there exist significant differences in the level of phosphatides between the anterior and posterior gills of Eriocheir sinensis. No matter what the salinity, the three more posterior located gills of Chinese crabs are shown to contain much more unsaturated phospholipids (PE and DPG). This is particularly true when animals are acclimated to dilute media. Moreover, lipids of posterior gills appear more fluid than the anterior ones as reported by the values of the degree of fluorescence polarization and the index of unsaturation of fatty acids. It is suggested that these lipid changes may indicate the existence of a functional difference between the various branchiae of euryhaline Eriocheir sinensis with respect to their ability to transport salt. It is shown that the renewal of DPG and PS is increased in posterior gills isolated from freshwater Chinese crabs. It is postulated that the enhanced formation of DPG in posterior gills is an indicator of an increased synthesis of mitochondria having as principal function to produce the necessary energy for the Na+ uptake. An attempt is made to correlate the PS metabolism and the Na+-K+-ATPase activity which is particularly located in the mitochondrial fractions of the three pairs of posterior gills.

Animals↗
PubMed1990

Interaction of phospholipids with Ca2+ ions. On the role of the phospholipid head groups.

Neutral phospholipids play an important role in Ca2+ binding to biomembranes, in particular if the membrane carries a net negative surface charge due to charged lipids or proteins. The concentration of Ca2+ ions in the plane of the phospholipid head groups can be enhanced by at least two orders of magnitude compared to bulk solution. Ca2+ binding furthermore changes the orientation of the phospholipid head groups which is accompanied by variations of the local membrane dipole potential of the order of 10(5) V/cm. Such high electric fields could entail conformational changes of membrane-bound proteins and the Ca2(+)-induced reorientation of the lipid dipoles could thus play a regulatory role in membrane function.

Calcium↗