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PubMed1978

The hydration of phospholipids and phospholipid-cholesterol complexes.

The hydration characteristics of phosphatidylcholines and the effect of cholesterol on these were studied with differential thermal analysis and water vapour adsorption experiments. Also the water adsorption of egg phosphatidylethanolamine and the effect of cholesterol on this was studied and compared with corresponding qualities of phosphatidylcholine. The differential thermal analysis study showed that the monohydrates of egg, dipalmitoyl, and dioleoyl phosphatidylcholine tightly bind approximately 9 molecules of water per phosphatidylcholine molecule. Cholesterol is proved to somewhat increase the water binding of the phospholipids. Cholesterol is also shown to decrease the heat change of the chain melting transition of dioleoyl phosphatidylcholine, but not to abolish it completely. The water adsorption experiments indicate that the hydration of phosphatidylcholines takes place in two steps; a strong initial water binding and a second phase of weak binding. The adsorption isotherm of egg phosphatidylethanolamine is strikingly different from that of egg phosphatidylcholine. Cholesterol is shown, also by this method, to increase the hydration of phospholipids especially that of dipalmitoylphosphatidylcholine. The results in this study are in good agreement with those presented by many other authors. Starting with the accumulated information of the hydration characteristics of phosphatidylcholines the organization of the bound water around the polar group is discussed and the most probable model is evaluated.

Adsorption↗
PubMed1989

Changes in the phospholipid composition and phospholipid asymmetry of ram sperm plasma membranes after cryopreservation.

The changes in the phospholipid composition of spermatozoa plasma membranes after freezing were determined by thin-layer chromatography. The results showed an augmentation of the diphosphatidylglycerol and a diminution of phosphatidylglycerol, phosphatidylserine, and phosphatidylethanolamine in sperm plasma membranes after freezing. In intact sperm cells we observed an elevation of the sphingomyelin and phosphatidylinositol levels and a diminution of the phosphatidylethanolamine and diphosphatidylglycerol levels. The effect of freezing on the phospholipid distribution between the inner and outer monolayers of the plasma membrane was also studied using exogenous phospholipases and trinitrobenzene sulfonate. The most important change we observed after freezing, was the translocation of diphosphatidylglycerol from the inner to the outer monolayer of the plasma membrane.

Animals↗
PubMed1991

Regulation of phosphatidylethanolamine methyltransferase and phospholipid methyltransferase by phospholipid precursors in Saccharomyces cerevisiae.

Phosphatidylethanolamine methyltransferase (PEMT) and phospholipid methyltransferase (PLMT), which are encoded by the CHO2 and OPI3 genes, respectively, catalyze the three-step methylation of phosphatidylethanolamine to phosphatidylcholine in Saccharomyces cerevisiae. Regulation of PEMT and PLMT as well as CHO2 mRNA and OPI3 mRNA abundance was examined in S. cerevisiae cells supplemented with phospholipid precursors. The addition of choline to inositol-containing growth medium repressed the levels of CHO2 mRNA and OPI3 mRNA abundance in wild-type cells. The major effect on the levels of the CHO2 mRNA and OPI3 mRNA occurred in response to inositol. Regulation was also examined in cho2 and opi3 mutants, which are defective in PEMT and PLMT activities, respectively. These mutants can synthesize phosphatidylcholine when they are supplemented with choline by the CDP-choline-based pathway but they are not auxotrophic for choline. CHO2 mRNA and OPI3 mRNA were regulated by inositol plus choline in opi3 and cho2 mutants, respectively. However, there was no regulation in response to inositol when the mutants were not supplemented with choline. This analysis showed that the regulation of CHO2 mRNA and OPI3 mRNA abundance by inositol required phosphatidylcholine synthesis by the CDP-choline-based pathway. The regulation of CHO2 mRNA and OPI3 mRNA abundance generally correlated with the activities of PEMT and PLMT, respectively. CDP-diacylglycerol synthase and phosphatidylserine synthase, which are regulated by inositol in wild-type cells, were examined in the cho2 and opi3 mutants. Phosphatidylcholine synthesis was not required for the regulation of CDP-diacylglycerol synthase and phosphatidylserine synthase by inositol.

Cloning, Molecular↗
PubMed1997

Phase behavior and permeability properties of phospholipid bilayers containing a short-chain phospholipid permeability enhancer.

The thermodynamic phase behavior and trans-bilayer permeability properties of multilamellar phospholipid vesicles containing a short-chain DC10PC phospholipid permeability enhancer have been studied by means of differential scanning calorimetry and fluorescence spectroscopy. The calorimetric scans of DC14PC lipid bilayer vesicles incorporated with high concentrations of DC10PC demonstrate a distinct influence on the lipid bilayer thermodynamics manifested as a pronounced freezing-point depression and a narrow phase coexistence region. Increasing amounts of DC10PC lead to a progressive lowering of the melting enthalpy, implying a mixing behavior of the DC10PC in the bilayer matrix similar to that of a substitutional impurity. The phase behavior of the DC10PC-DC14PC mixture is supported by fluorescence polarization measurements which, furthermore, in the low-temperature gel phase reveal a non-monotonic concentration-dependent influence on the structural bilayer properties; small concentrations of DC10PC induce a disordering of the acyl chains, whereas higher concentrations lead to an ordering. Irreversible fluorescence quench measurements demonstrate a substantial increase in the trans-bilayer permeability over broad temperature and composition ranges. At temperatures corresponding to the peak positions of the heat capacity, a maximum in the trans-bilayer permeability is observed. The influence of DC10PC on the lipid bilayer thermodynamics and the associated permeability properties is discussed in terms of microscopic effects on the lateral lipid organization and heterogeneity of the bilayer.

Calorimetry, Differential Scanning↗
PubMed1998

On the use of deuterated phospholipids for infrared spectroscopic studies of monomolecular films: a thermodynamic analysis of single and binary component phospholipid monolayers.

A thermodynamic study of monolayer mixing behavior was performed using binary lipid mixtures of DPPC + DOPG (7:1 mol:mol) as well as a mixture containing the phosphocholine acyl chain perdeuterated analog of DPPC, DPPC-d62 (i.e. 7:1 mol:mol DPPC-d62 + DOPG). An analysis was performed on these isotherms that calculated the Helmholtz excess free energy of mixing to determine potential thermodynamic differences in the fully protiated DPPC:DOPG monolayer versus the identical monolayer substituted with acyl chain perdeuterated DPPC (i.e. DPPC-d62). The main conclusions of this study are that: (1) the temperature-dependent thermodynamic phase behavior of DPPC-d62 differs substantially from that of DPPC, and these differences appear magnified when these molecules are studied as monomolecular films at the A/W interface as opposed to bulk phase systems; and (2) the calculated excess free energy of mixing values, deltaFxs(A), for the deuterium-containing 7:1 DPPC-d62:DOPG binary monolayer film show a type of near-ideal mixing behavior above 20 degrees C that is consistent with the 'squeezing-out' of the DOPG component in the binary mixture containing the DPPC-d62 component. This type of behavior does not occur in the graph of the excess free energy of mixing for the fully protiated 7:1 DPPC:DOPG binary monolayer film. The use of acyl chain perdeuterated DPPC (i.e. DPPC-d62) in binary monomolecular mixtures with other phospholipids produces a real and measurable difference on the thermodynamic properties of the monolayer when compared to the case of the fully protiated monomolecular film. In particular, the presence of DPPC-d62 in a 7:1 mol:mol DPPC-d62:DOPG binary monomolecular film may over-state the fluid nature of the monolayer at any given temperature, thereby leading to an over-estimate of the amount of material potentially 'squeezed out' of the monomolecular film. These results have implications for a commonly used IR spectroscopic method that relies on the incorporation of deuterium-labeled phospholipids into monolayers for vibrational spectroscopic analysis of individual components in a multicomponent monomolecular film.

1,2-Dipalmitoylphosphatidylcholine↗
PubMed1998

15-Lipoxygenation of phospholipids may precede the sn-2 cleavage by phospholipases A2: reaction specificities of secretory and cytosolic phospholipases A2 towards native and 15-lipoxygenated arachidonoyl phospholipids.

Reticulocyte-type 15-lipoxygenase is known to dioxygenate phospholipids without preceding action of phospholipases A2 (PLA2). Therefore we studied the reaction of the secretory PLA2s (sPLA2) from pancreas and snake venom, and of the human cytosolic PLA2 (cPLA2) with 1-palmitoyl-2-arachidonoyl phosphatidylcholine (PAPC) and their 15-lipoxygenated species (PAPC-OOH and PAPC-OH) either alone or as equimolar mixtures. These PLA2s cleaved PAPC-O(O)H with higher (sPLA2) or similar rates (cPLA2) as compared with native PAPC. In mixtures, however, PAPC proved to be the preferred, albeit not exclusive substrate for all three PLA2s. Thus, partial 15-lipoxygenation of phospholipids may also trigger liberation of arachidonic acid.

Arachidonate 15-Lipoxygenase↗
PubMed1983

Incorporation of danyslated phospholipids and dehydroergosterol into membranes using a phospholipid exchange protein.

A nonspecific phospholipid exchange protein (PLEP) preparation was used to transfer dansyl [3H]phosphatidylethanolamine (DNS-PE), dansyl[3H]phosphatidylserine (DNS-PS), and dehydroergosterol (DHE) from sonicated lipid vesicles to electroplax plasma membrane fragments enriched in Na+,K+-ATPase with retention of 80-90% of Na+,K+-ATPase activity. The transfer of individual fluorescent lipid molecules was distinguished from a nonspecific association of lipid vesicles and membranes by including [14C]triolein, a lipid that is not transferred by PLEPs, in the vesicles. Dansyl 3H-labeled phospholipids (DNS-[3H]PLs) or DHE was considered "incorporated" into the Na+,K+-ATPase membranes when fluorophores pelleted with the Na+,K+-ATPase preparation without the nonexchangeable [14C]triolein. The locations of incorporated DHE and DNS-PLs were also described by iodide quenching experiments. DHE was not accessible to iodide for quenching, while 75% of the DNS-PLs incorporated into Na+,K+-ATPase membrane fragments were accessible to iodide. After a technique was developed for using PLEP to incorporate fluorescent lipids into membranes with the Na+,K+-ATPase preparation, DNS-PE, DNS-PS, and DHE were then analogously incorporated into electroplax plasma membranes enriched in acetylcholinesterase (AChE) and into erythrocyte ghosts in order to evaluate the fluorophores as membrane probes. In the subsequent evaluation, the fluorescent properties of membrane-incorporated DNS-PE, DNS-PS, and DHE were systematically compared to the fluorescent properties of the molecules in lipid vesicles. The fluorescence polarizations of both DNS-PLs were increased by the presence of protein in a bilayer. The fluorescence polarization of DNS-PS was greater than the polarization of DNS-PE in both membranes and vesicles. In contrast, the polarization (and the lifetime) of DHE was the same whether the fluorescent sterol was in a membrane preparation or in vesicles. Fluorescence polarization and intensity of all three fluorophores were measured in the bilayer preparations as a function of temperature. The intensities of all three probes and the polarization of DNS-PE in both membranes and vesicles decreased biphasically with a change in slope occurring at 26.0-27.5 degrees C. DNS-PS in lipid vesicles was depolarized biphasically with increasing temperature, but when incorporated into membranes, DNS-PS was depolarized linearly without a change in slope. The polarization of DHE in either membranous or vesicle bilayers did not change with temperature.(ABSTRACT TRUNCATED AT 400 WORDS)

Animals↗
PubMed1986

Phospholipid lateral organization in synthetic membranes as monitored by pyrene-labeled phospholipids: effects of temperature and prothrombin fragment 1 binding.

Pyrene-labeled phospholipids have been used to test for the existence of lateral domains due to temperature-induced phase separations and binding of prothrombin fragment 1 to charged lipid vesicles. When in close proximity, pyrene-containing probes can exchange excited-state energy to form excimers; the ratio of the excimer to monomer fluorescence intensity (E/M) is proportional to the local concentration of probe in the membranes, as well as to the excimer lifetime and the probe's lateral diffusion coefficient. The ability of the pyrene-labeled phospholipids to quantitatively report the coexistence of multiple environments was demonstrated in dipalmitoylphosphatidylcholine/palmitoyloleoylphosphatidylcholine multilamellar vesicle preparations of varying compositions, each of which contained coexisting fluid and gel phases. In this system, pyrene-labeled phosphatidylcholine was found to favor the fluid relative to the gel phase with a partition coefficient of 7. At 37 degrees C, in dioleoylphosphatidylglycerol (DOPG)/palmitoyloleoylphosphatidylcholine (POPC) large, unilamellar vesicles containing either pyrene-labeled phosphatidylglycerol (py-PG) or pyrene-labeled phosphatidylcholine (py-PC), the excimer lifetime (37 ns) and the lateral diffusion constant of the probe (5.8 X 10(-8) cm2/s) were independent of the membrane composition and the presence of fragment 1 and Ca2+. Consequently, E/M was directly proportional to only the local concentration of the py-PG or py-PC probes. When saturating amounts of fragment 1 and 5 mM Ca2+ were added to DOPG/POPC vesicles that contained either probe, no change in E/M and hence the local probe concentration was observed.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1990

Characterization of phospholipid transfer between mixed phospholipid-bile salt micelles.

Concentration-dependent self-quenching of the fluorescent phospholipid N-(7-nitro-2,1,3-benzoxadiazol-4-yl)phosphatidylethanolamine (N-NBD-PE) was used to measure the rate of N-NBD-PE transfer between phosphatidylcholine-bile salt mixed micelles. In a previous study using the same technique, the rate of N-NBD-PE transfer between phosphatidylcholine-taurocholate mixed micelles was found to be several orders of magnitude faster than its transfer between phosphatidylcholine vesicles as a result of an increased rate of transfer through the water at low micelle concentrations and an increased rate of transfer during transient micelle collisions at higher micelle concentrations [Nichols, J. W. (1988) Biochemistry 27, 3925-3931]. In this study we have determined the influence of bile salt structure, incorporation of cholesterol, and temperature on the rate and mechanism of phospholipid transfer between mixed micelles. We found that both transfer pathways were a common property of mixed micelles prepared from a series of different bile salts and that the rates of transfer by both pathways increased as a function of the degree of bile salt hydrophobicity. Cholesterol incorporation into phosphatidylcholine-taurocholate mixed micelles displaced taurocholate from the micelles and resulted in an increased rate of transfer through the water and a decreased rate of transfer during micelle collisions. The temperature dependence of the transfer rates was used to calculate the activation free energy, enthalpy, and entropy for both mechanisms. The activation enthalpy was the major barrier to transfer by both mechanisms.(ABSTRACT TRUNCATED AT 250 WORDS)

Bile Acids and Salts↗
PubMedDate not supplied

Products and mechanism of the reaction of ozone with phospholipids in unilamellar phospholipid vesicles.

While considerable effort has been expended on determining the health effects of exposure to typical urban concentrations of O3, little is known about the chemical events responsible for toxicity. Phospholipids containing unsaturated fatty acids in the cell membranes of lung cells are likely reaction sites for inhaled ozone (O3). In this study, we examined the reaction of O3 with 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) in unilamellar phospholipid vesicles. Reaction of ozone with the carbon-carbon double bond of POPC yielded an aldehyde and a hydroxy hydroperoxide. The hydroxy hydroperoxide eliminated H2O2 to yield a second aldehyde. Upon further ozonolysis, the aldehydes were oxidized to the corresponding carboxylic acids. A material balance showed that no other reaction consumed POPC and O3 or produced these products. As a mechanistic probe, we measured incorporation of oxygen-18 from 18O3 into aldehyde, carboxylic acid, and H2O2. Approximately 50% of the aldehyde oxygen atoms were derived from O3. Oxygen in H2O2 was derived solely from O3, where both oxygen atoms in a molecule of H2O2 were from the same molecule of O3. One of the carboxylic acid oxygen atoms was derived from the precursor aldehyde, while the other was derived from O3. These results support the following mechanism. Cleavage of the carbon-carbon double bond of POPC by O3 yields a carbonyl oxide and an aldehyde. Reaction of H2O with the carbonyl oxide yields a hydroxy hydroperoxide, preventing formation ozonide by reaction of the carbonyl oxide and aldehyde. Elimination of H2O2 from the hydroxy hydroperoxide yields a second aldehyde. Oxidation of the aldehydes by O3 yields carboxylic acids.

Aldehydes↗
PubMed2001

Recognition by macrophages and liver cells of opsonized phospholipid vesicles and phospholipid headgroups.

The interaction of liposomes with blood proteins is believed to play a critical role in the clearance pharmacokinetics and tissue distribution of intravenously injected liposomes. In this article we have focused our discussion on the interaction of liposomes with key blood proteins, which include immunoglobulins, complement proteins, apolipoproteins, fetuin, von Willebrand factor, and thrombospondin, and their role in liposome recognition by professional phagocytes and nonmacrophage hepatic cells. Alternatively, macrophages as well as hepatocytes and liver endothelial cells may phagocytose/endocytose liposomes via direct recognition of phospholipid headgroups. A number of plasma membrane receptors such as lectin receptors, CD14, various classes of scavenger receptors (e.g., classes A, B, and D), Fc-gammaRI and FcgammaRII-B2 may participate in phospholipid recognition. These concepts are also discussed.

Animals↗
PubMed2001

Epoxyisoprostane and epoxycyclopentenone phospholipids regulate monocyte chemotactic protein-1 and interleukin-8 synthesis. Formation of these oxidized phospholipids in response to interleukin-1beta.

Monocyte recruitment to the vessel wall, mediated by monocyte chemotactic protein-1 (MCP-1) and interleukin-8 (IL-8), plays an important role in atherogenesis. We have shown previously that minimally oxidized low density lipoprotein, oxidized 1-palmitoyl-2-arachidonyl-sn-glycero-3-phosphorylcholine (Ox-PAPC), activates endothelial cells to produce MCP-1 and IL-8. By using liquid chromatography/mass spectrometry methods coupled with bioassay, we report a family of epoxyisoprostane (PEIPC) and epoxycyclopentenone (PECPC) phospholipids that are the components of Ox-PAPC responsible for the majority of this activity. Ox-PAPC contains five chromatographically distinguishable active PEIPC components (m/z 825.5) and four PECPC components (m/z 810.5). All nine components induced endothelial cell synthesis of IL-8 and MCP-1 in a dose-dependent fashion between 0.1 and 5 microm concentrations. The five PEIPC components had identical functional groups and all underwent dehydration to produce m/z 810.5. We present evidence that these phospholipids are regioisomers with epoxide groups at the 5,6-, 8,9-, 11,12-, or 14,15-positions of the sn-2 fatty acid and their epoxide groups is important for biological activity. We have shown previously that peroxisome proliferator-activated receptor alpha is involved in MCP-1 synthesis in response to Ox-PAPC. We now show that PEIPC and PECPC isomers are potent activators of peroxisome proliferator-activated receptor alpha. PEIPC and PECPC isomers are strongly recognized by specific circulating murine natural autoantibodies (EO6) and accumulate in cells treated with IL-1beta. These studies demonstrate that PEIPC and PECPC isomers are potent activators of endothelial cells increasing synthesis of IL-8 and MCP-1. Their accumulation in cells exposed to cytokines and in atherosclerotic lesions suggests that these lipids may play a role in a number of chronic disease processes.

Binding, Competitive↗
PubMed1980

Fusion of phospholipid vesicles with planar phospholipid bilayer membranes. I. Discharge of vesicular contents across the planar membrane.

Multilamellar phospholipid vesicles are introduced into the cis compartment on one side of a planar phospholipid bilayer membrane. The vesicles contain a water-soluble fluorescent dye trapped in the aqueous phases between the lamellae. If a vesicle containing n lamellae fuses with a planar membrane, an n-1 lamellar vesicle should be discharged into the opposite trans compartment, where it would appear as a discernible fluorescent particle. Thus, fusion events can be assayed by counting the number of fluorescent particles appearing in the trans compartment. In the absence of divalent cation, fusion does not occur, even after vesicles have been in the cis compartment for 40 min. When CaCl2 is introduced into the cis compartment to a concentration of greater than or equal to 20 mM, fusion occurs within the next 20 min; it generally ceases thereafter because of vesicle aggregation in the cis compartment. With approximately 3 x 10(8) vesicles/cm3 in the cis compartment, about 25-50 fusion events occur following CaCl2 addition. The discharge of vesicular contents across the planar membrane is the most convincing evidence of vesicle-membrane fusion and serves as a model for that ubiquitous biological phenomenon--exocytosis.

Exocytosis↗
PubMed1998

Docosahexaenoic acid concentrations in retinal phospholipids of piglets fed an infant formula enriched with long-chain polyunsaturated fatty acids: effects of egg phospholipids and fish oils with different ratios of eicosapentaenoic acid to docosahexaenoic acid.

Docosahexaenoic acid (DHA; 22:6n-3) is the major fatty acid in the phosphatidylethanolamine of photoreceptor cells. The supply of preformed DHA in milk may play an important role in early human visual development. We examined the effect of adding dietary DHA from yolk or fish oil on its accretion in the retina of newborn piglets fed artificially for 2 wk. DHA-enriched eggs from hens fed rapeseed oil and two fish oils with a high or low ratio of eicosapentaenoic acid (EPA; 20:5n-3) to DHA were used. The basic (conventional) formula contained (% by wt of total fatty acids) 17% linoleic acid (18:2n-6) and 1.3% alpha-linolenic acid (18:3n-3). The yolk-enriched formula also contained 0.5% arachidonic acid (AA; 20:4n-6) and 0.4% DHA. The fish-oil-enriched formulas contained either 0.3% EPA and 0.2% DHA (from salmon oil) or < 0.1% EPA and 0.3% DHA (low-EPA fish oil used at a low concentration), or 0.1% AA, 0.3% EPA, and 0.9% DHA (low-EPA fish oil used at a high concentration). The low-EPA fish oil used at a low concentration can supply the DHA required without increasing the EPA status but only the yolk-enriched formula allowed the artificially reared piglets to attain the same AA status in blood lipids as with sow milk feeding. The DHA concentration plateaued in the retina when it reached 7.5% by wt of total fatty acids in plasma phospholipids. Yolk phospholipids and fish oils are equally potent sources for supplying the highest retinal DHA concentration, which was found to be 41.7% by wt of total fatty acids in phosphatidylethanolamine (compared with 35% without supplementation). Inclusion of 0.2-0.3% DHA ensures maximal DHA accretion in the retina but cosupplementation with AA is necessary to achieve the status with maternal feeding in blood lipids and to prevent any possible imbalance between n-6 and n-3 fatty acids.

Animals↗
PubMedDate not supplied

Physical interaction between lipid A and phospholipids: a study with spin-labeled phospholipids.

When mixed bilayers containing spin-labeled phosphatidylethanolamine (or phosphatidylglycerol) and Escherichia coli B lipopolysaccharide were prepared, electron spin resonance signals indicated that the patches that were initially present and contained only phospholipids or only lipopolysaccharides were unusually stable and that little lateral diffusion of phospholipids into lipopolysaccharide domains, or vice versa, took place. These results explain how the outer layer of the outer membrane, which essentially contains only lipopolysaccharides in addition to proteins, can be generated and maintained stably in bacterial cells. Furthermore, the stability of pure lipopolysaccharide domains may have important implications in the mode of action of endotoxins in the body of the host. For example, lipopolysaccharide molecules may tend to form stable domains or patches spontaneously in the animal cell membrane, and special mechanisms (such as the binding to a special receptor) may be needed to disperse the lipopolysaccharide molecules within the host cell membranes.

Lipid A↗
PubMed2001

Membrane fusion between liposomes composed of acidic phospholipids and neutral phospholipids induced by melittin: a differential scanning calorimetric study.

Melittin-induced membrane fusion between neutral and acidic phospholipids was examined in liposome systems with a high-sensitivity differential scanning calorimeter. Membrane fusion could be detected by calorimetric measurement by observing thermograms of mixed liposomal lipids. The roles of hydrophobic and electrostatic interactions were investigated in membrane fusion induced by melittin. Melittin, a bee venom peptide, is composed of a hydrophobic region including hydrophobic amino acids and a positively charged region including basic amino acids. When phosphatidylcholine liposomes were prepared in the presence of melittin, reductions in the phase transition enthalpies were observed in the following order; dimyristoylphosphatidylcholine (DMPC) > dipalmitoylphosphatidylcholine (DPPC) > distearoylphosphatidylcholine (DSPC) > dielaidoylphosphatidylcholine (DEPC). The plase transition enthalpy of an acidic phospholipid, dipalmitoylphosphatidylserine (DPPS), was raised by melittin at low concentrations, then reduced at higher concentrations. DPPC liposomes prepared in melittin solution were fused with DPPS liposomes when the liposomal dispersions were mixed and incubated. Similar fusion was observed between dipalmitoylphosphatidylcholine and dimyristoylphosphatidic acid (DMPA) liposomes. These results indicate that a peptide including hydrophobic and basic regions can mediate membrane fusion between neutral and acidic liposomes by hydrophobic and electrostatic interactions.

Calorimetry, Differential Scanning↗
PubMed1984

Tetracycline diffusion through phospholipid bilayers and binding to phospholipids.

The ability of tetracycline to pass through phospholipid bilayers by diffusion was investigated. Liposomes did not retain enclosed tetracycline. Accumulation of tetracycline was observed with liposomes containing entrapped Tet repressor protein. These results indicate that the drug can pass through lipid bilayers. The antibiotic was also shown to bind to liposomes and isolated phospholipids.

Chemical Phenomena↗
PubMed2000

Distribution of phospholipid transfer protein in human plasma: presence of two forms of phospholipid transfer protein, one catalytically active and the other inactive.

Plasma phospholipid transfer protein (PLTP) plays an important role in the maintenance of plasma high-density lipoprotein (HDL) content and remodeling of HDL in the circulation. In the present study we have used different fractionation methods to investigate the distribution of PLTP in human plasma. A novel enzyme-linked immunosorbent assay developed during the study allowed for simultaneous assessment of both PLTP mass and activity in the fractions obtained. Size-exclusion chromatography and plasma fractionation by nondenaturing polyacrylamide gel electrophoresis (PAGE) yielded similar results demonstrating that PLTP associates in native plasma with two distinct particle populations, while ultracentrifugation with high salt leads to detachment of PLTP from lipoprotein particles and loss of a majority of its phospholipid transfer activity. Interestingly, analysis of the size-exclusion chromatography fractions demonstrated that PLTP exists in the circulation as an active population that elutes in the position of HDL corresponding to an average molecular mass of 160+/-40 kDa and an inactive form with an average mass of 520+/-120 kDa. The inactive fraction containing approximately 70% of the total PLTP protein eluted between HDL and low density lipoprotein (LDL). Thus, the two PLTP pools are associated with different types of lipoprotein particles, suggesting that the PLTP activity in circulation is modulated by the plasma lipoprotein profile and lipid composition.

Antibodies, Monoclonal↗