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PubMed1989

Distribution and functions of lecithin:cholesterol acyltransferase and cholesteryl ester transfer protein in plasma lipoproteins. Evidence for a functional unit containing these activities together with apolipoproteins A-I and D that catalyzes the esterification and transfer of cell-derived cholesterol.

The distribution of apolipoprotein A-I, apolipoprotein D, lecithin:cholesterol acyltransferase, and cholesteryl ester transfer protein in fasting normal human plasma was determined by two-dimensional electrophoresis followed by immunoblotting. The synthesis and transfer of labeled cholesteryl esters generated in plasma briefly incubated with [3H]cholesterol-labeled fibroblasts was followed in terms of the lipoprotein species containing these antigens. Following the early appearance of labeled free cholesterol in two pre beta-migrating apolipoprotein A-I species (Castro, G. R., and Fielding, C. J. (1988) Biochemistry 27, 25-29), labeled esters were first detected, after a 2-min delay, in a third pre beta-migrating species which also contained apolipoprotein D, lecithin:cholesterol acyltransferase, and cholesteryl ester transfer protein. Pulse-chase experiments determined that label generated in this fraction was the precursor of at least a major part of labeled cholesteryl esters in the bulk of alpha-migrating high density lipoprotein. Over the maximum time course of these experiments (15 min, 37 degrees C), less than 10% of labeled cholesteryl esters were recovered in low or very low density lipoproteins separated by electrophoresis, immunoaffinity, or heparin-agarose chromatography. These data suggest channeling of cell-derived cholesterol and cholesteryl esters derived from it through a preferred pathway involving several minor pre beta-migrating lipoproteins to alpha-migrating high density lipoprotein.

Antibodies, Monoclonal↗
PubMed1988

[Research on high-temperature transition in liposomes made from egg yolk lecithin].

The pyrene eximerization, polarity of pyrene microenvironment and relaxation times (T1 and T2) of water protons in the systems of monolamellar egg yolk lecithin liposomes were investigated depending on temperature and bilayer modification by cholesterol and alpha-tocopherol. The thermotropic transition of pyrene eximerization degree at 38 degrees C, abrupt polarity change of pyrene microenvironment at 22-25 degrees C in modified by tocopherol liposomes and abnormal behaviour of water proton relaxation times in the temperature range of 39-40 degrees C were found. This high-temperature transition is supposed to be due to the structural alteration in the region of egg yolk lecithin heads.

Biophysical Phenomena↗
PubMed1989

The reactivity of plasma phospholipids with lecithin:cholesterol acyltransferase is decreased in fish oil-fed monkeys.

The size of low density lipoproteins (LDL) is strongly correlated with LDL cholesteryl ester (CE) content and coronary artery atherosclerosis in monkeys fed cholesterol and saturated fat. African green monkeys fed 11% (weight) fish oil diets have smaller LDL and less CE per LDL particle than lard-fed animals. We hypothesized that this might be due to a lower plasma lecithin:cholesterol acyltransferase (LCAT) activity in fish oil-fed animals. Using recombinant particles made of egg yolk lecithin-[14C]cholesterol-apoA-I as exogenous substrate, we found no difference in plasma LCAT activity (27 versus 28 nmol CE formed per h/ml) of fish oil- versus lard-fed animals, respectively; furthermore, no diet-induced difference in immunodetectable LCAT was found. However, plasma phospholipids from fish oil-fed animals were over 4-fold enriched in n-3 fatty acids in the sn-2 position compared to those of lard-fed animals. Additionally, the proportion of n-3 fatty acid-containing CE products formed by LCAT, relative to the available n-3 fatty acid in the sn-2 position of phospholipids, was less than one-tenth of that for linoleic acid. The overall rate of LCAT-catalyzed CE formation with phospholipid substrates from fish oil-fed animals was lower (5-50%) than with phospholipid substrates from lard-fed animals. These data show that n-3 fatty acids in phospholipids are not readily utilized by LCAT for formation of CE; rather, LCAT preferentially utilizes linoleic acid for CE formation. The amount of linoleic acid in the sn-2 position of plasma phospholipids is reduced and replaced with n-3 fatty acids in fish oil-fed animals. As a result, LCAT-catalyzed plasma CE formation in vivo is likely reduced in fish oil-fed animals contributing to the decreased cholesteryl ester content and smaller size of LDL particles in the animals of this diet group.

Animals↗
PubMed1986

Nature of the enhancement of lecithin-cholesterol acyltransferase reaction by various apolipoproteins.

The effects of human apolipoproteins on the lecithin-cholesterol acyltransferase reaction were studied by using purified human lecithin-cholesterol acyltransferase and phosphatidylcholine-cholesterol vesicles. When the assay mixtures contained an optimal amount or excess of apo-A-I, the addition of apo-A-II, apo-C-II, apo-C-III1, or apo-C-III2 inhibited the enzymatic reaction. However, at suboptimal apo-A-I concentrations, the addition of low concentrations of these apolipoproteins exhibited activating effects. The relative activating effects were greater at lower apo-A-I levels. Under no circumstance did the combined activating effect of apo-A-I and other apolipoproteins exceed the maximum activating effect observed with the optimal level of apo-A-I alone. Since apo-A-II, apo-C-II, and apo-C-III did not show significant activating effects in the absence of apo-A-I, these apolipoproteins apparently did not act as true activator proteins for the enzymatic reaction. The activation of the enzymatic reaction by apo-A-I alone was shown to be due in part to the enhancement of the enzyme transfer between the substrate particles. The replacement of the transfer-enhancing effect of apo-A-I by apo-A-II, apo-C-II, or apo-C-III appears to be responsible for their apparent activating effects in the presence of suboptimal levels of apo-A-I. These apolipoproteins seemed to coexist with both the enzyme and apo-A-I on the substrate particles under the conditions when they showed the activating effect. However, at the concentrations inhibitory to the enzymatic reaction, these apolipoproteins displaced both the enzyme and apo-A-I from the phosphatidylcholine-cholesterol vesicles.

Apolipoprotein A-I↗
PubMed1986

Temperature-induced spectral properties of chlorophyll a incorporated into egg-yolk lecithin liposomes and lipo-protein complexes.

The temperature-induced fluorescence changes of Chl a in the systems consisting of albumin-egg-yolk lecithin and only lecithin were studied. As plotted against temperature in liposomes the fluorescence intensity of Chl a has a maximum at approximately 35 degrees C. In CLP complexes the curve profile for the fluorescence intensity versus temperature is sharper and the maximum occurred at a lower temperature (25 degrees C). No fluorescence maxima for ANS in liposomes and for Chl a in isotropic solutions were found. The second derivative absorption spectra of the investigated lipid systems exhibited bands which were characteristic of monomeric Chl a. We suggested that in the temperature zone studied Chl a in vitro is embedded within lipid bilayer rather than attached to the proteins. The occurrence of the fluorescence intensity maximum of Chl a in liposomes and lipo-protein complexes is related to the effects: temperature quenching of the fluorescence, Chl a-lipid interaction.

Chlorophyll↗
PubMed1979

Comparison of the association and orientation of gamma-glutamyltranspeptidase in lecithin vesicles and in native membranes.

gamma-Glutamyltranspeptidase purified following solubilization with Triton X-100 can associate with single-layered [14C]lecithin vesicles. Enzyme activity and radiolabeled vesicles were shown to co-migrate during Sepharose 4B chromatography and isopycnic sucrose gradient centrifugation. The enzyme-vesicle complex exhibits a density corresponding to that of a single enzyme molecule bound to a single vesicle, gamma-Glutamyltranspeptidase purified following a solubilization with papain does not bind to vesicles. In addition, papain treatment of vesicles containing the Triton-purified transpeptidase results in the release of 95% of the transpeptidase activity without release of internally trapped [3H]sucrose. The released transpeptidase is chromatographically identical to the papain-purified transpeptidase. gamma-Glutamyltranspeptidase activity associated with both native membranes and with lecithin vesicles exhibits a temperature-induced transition in its energy of activation. In contrast, the proteolytic- and detergent-solubilized forms of the enzyme exhibit a single energy of activation over the entire temperature range. These results suggest that gamma-glutamyltranspeptidase binding to vesicles is due to a papain sensitive sequence of amino acids and that the enzyme.vesicle complex closely approximates the interaction and orientation of gamma-glutamyltranspeptidase with brush border membranes.

Animals↗
PubMed1986

Synthetic substrates of lecithin: cholesterol acyltransferase.

Investigation of the substrate specificity of lecithin: cholesterol acyltransferase has been greatly aided by the use of synthetic particles containing the molecular lipid substrates and the apolipoprotein activators of the enzyme. These synthetic particles, in vesicle or disc-like micelle form, are described in some detail noting their preparation, properties, advantages, and limitations as substrates for lecithin:cholesterol acyltransferase. The reactions of the enzyme with the synthetic particles are reviewed in terms of acyl donor and acceptor specificity, activation by apolipoproteins, effects of various inhibitors, and the kinetics of the reaction.

Animals↗
PubMed1987

Studies of synthetic peptide analogs of the amphipathic helix. Effect of charge distribution, hydrophobicity, and secondary structure on lipid association and lecithin:cholesterol acyltransferase activation.

Four peptides capable of forming an amphipathic alpha-helix have been synthesized and their conformational and lipid-binding properties studied. These peptides have been designed to vary the alpha-helix-forming potential as well as the charge distribution of the model peptide. The resulting peptide analogs and their complexes with dimyristoyl phosphatidylcholine were studied by using right angle light scattering, negative stain electron microscopy, nondenaturing gradient gel electrophoresis, circular dichroism, intrinsic tryptophan fluorescence, and differential scanning calorimetry techniques. The four analogs, [Glu4,9, Leu11,17] (reverse-18A, [Glu4,9, Leu5,11,17] reverse-18A, [Glu1,8, Leu11,17] 18A, and [Glu1,8, Leu5,11,17] 18A were derived from a model amphipathic peptide Asp-Trp-Leu-Lys-Ala-Phe-Tyr-Asp-Lys-Val-Ala-Glu-Lys-Leu-Lys-Glu-Ala-Phe (18A) whose lipid-associating properties strongly mimic apolipoprotein A-I or derived from Lys-Trp-Leu-Asp-Ala-Phe-Tyr-Lys-Asp-Val-Ala-Lys-Glu-Leu-Glu-Lys-Ala-Phe (reverse-18A), a peptide with little affinity for lipid and having a reversed charge distribution compared to the 18A peptide. We have shown that by substituting glutamic acid and leucine for aspartic acid and alanine, respectively, in a weak lipid-associating amphipathic helix peptide, the lipid-associating ability can be increased. Thus, peptides with both kinds of charge distribution can associate with the lipid. The ability of the peptide to disrupt phospholipid bilayers, however, is higher for 18A analogs compared to the reverse-18A analogs even after increasing the helix-forming potential and hydrophobicity. In addition to forming smaller lipoprotein particles, the modified 18A analogs were much superior to the modified reverse-18A analogs in their ability to activate the enzyme lecithin:cholesterol acyltransferase. This demonstrates that the positions of charged residues in the amphipathic helix play an important role in lecithin:cholesterol acyltransferase activation.

Circular Dichroism↗
PubMed1987

A preparative high performance liquid chromatography method for separation of lecithin: comparison to thin-layer chromatography.

We have developed a high performance liquid chromatography (HPLC) method to separate lecithin from other phospholipid classes and to obtain lecithin from biologic materials. The separation was performed on a preparative 10-micron Spherisorb column with an optimized solvent system consisting of the following components: acetonitrile, isopropanol, methanol, water, and trifluoroacetic acid. The advantages of this method are the use of an isocratic solvent system limited to about 30 min and the very good separation of the phosphatidyl-choline fraction from the sphingomyelin fraction. Furthermore, the HPLC method has a better recovery rate than the thin-layer chromatography method, and it can be run under automatic control.

Animals↗
PubMedDate not supplied

[Transmembrane lipid transport between lecithin liposomes and neuroblastoma C1300 N18 cells].

The method of double isotopic labels was used to study dynamics of lipid metabolism between neuroblastoma C 1300 N 18 A 1 cells and lecithin liposomes which contained 4.5-5 mumol of lecithin in 1 ml of the suspension. The cell lipids were labelled by radioactive carbon and cultivated on the medium with [1-14C] sodium acetate, phosphatidylcholine of liposomes was labelled by tritium. It is shown that 15-30 min long incubation with liposomes causes a sharp decrease of the cholesterol esters amount with a simultaneous fall of the free cholesterol level. The total content of phospholipids in this case remains unchanged though there occurs the noticeable exchange of labelled phospholipids between cells and liposomes. The cholesterol content in the plasma membranes of cells lowers sharply. The neuroblastoma cells are able to compensate arising changes in the cholesterol level for 45-60 min after which they progressively die. 90 min later only an insignificant part of the population (about 10% of cells) is retained.

Biological Transport↗
PubMedDate not supplied

In vitro cultivation of mycobacteria in cholesterol lecithin media from lepromas of rats infected with Mycobacterium lepraemurium.

In vivo grown M. lepraemurium suspensions were inoculated into a basal medium containing cholesterol and lecithin. Slow growing strains of mycobacteria were cultured regularly in these media. The presence of free cholesterol or cholesterol in serum or cholesterol in trypsin-digested egg yolk was essential for growth. The primary cultures were difficult to obtain, but the strains were easily subcultured. A heavy inoculum was necessary to obtain primary cultures in the liquid media, no growth occurred on semisolid agar slants. Similarly slow-growing primary cultures were obtained on Ogawa egg yolk media. Growth developed in a considerably shorter time if Ogawa's medium was enriched with 0.4% yeast extract (Difco). The cultures obtained on Ogawa egg yolk media were successfully subcultered in liquid cholesterol-lecithin media. The relation of the cultured strains of mycobacteria to the pathology of murine leprosy is not yet clear. The dynamics of cholesterol metabolism in the macrophages related to murine leprosy is discussed.

Animals↗
PubMed1987

Automated enzymatic measurement of lecithin, sphingomyelin, and phosphatidylglycerol in amniotic fluid.

We describe methods for automated enzymatic measurement of lecithin, sphingomyelin, and phosphatidylglycerol in amniotic fluid. Phospholipase C (EC 3.1.4.3) and sphingomyelin phosphodiesterase (EC 3.1.4.12) are reacted with lecithin and sphingomyelin, respectively, to liberate phosphocholine. Phosphocholine is then reacted with alkaline phosphatase, choline oxidase, peroxidase, and 4-aminoantipyrine to form a colored complex, for which the absorbance at 500 nm is measured with a centrifugal analyzer. Phosphatidylglycerol is hydrolyzed by phospholipase D (EC 3.1.4.4) to form glycerol, which is subsequently reacted with ATP and NAD+ in the presence of glycerol kinase and glycerol-3-phosphate dehydrogenase to yield NADH. The absorbance of the NADH formed is measured at 340 nm. These methods provide a simple, rapid, and accurate alternative to thin-layer chromatography for determination of phospholipids in amniotic fluid for assessment of fetal lung maturity.

Amniotic Fluid↗
PubMed1985

Effect of propranolol on lecithin:cholesterol acyl transferase activity in vitro.

Recently propranolol was found to inhibit human lecithin: cholesterol acyl transferase (LCAT) activity both after oral treatment and after addition to plasma in vitro. Now the dose-response relationship of the propranolol effect on LCAT activity was evaluated in vitro. Concentrations required to produce half-maximal effects in 7 men ranged from 32.4 to 121.4 nmol/l which corresponds to the therapeutical concentration range of the drug. Complete inhibition could not be achieved. The maximal effect (propranolol-sensitive LCAT activity) varied between subjects depending on the preexiting lecithin: cholesterol acyl transfer rate in plasma. Propranolol mediated inhibition of LCAT activity could be abolished when heat-inactivated plasma instead of native plasma was used as LCAT substrate. It is concluded that the interindividual variability of propranolol-sensitive LCAT activity may reflect differences in the thermoinstable lipoprotein structure.

Humans↗
PubMed1985

Inhibition of lecithin: cholesterol acyl transfer by propranolol treatment in man.

The changes in some parameters of plasma lipoprotein metabolism in 25 hypertensive men, caused by a two months lasting oral treatment with 120 mg propranolol/day, were compared to the changes that occur during the same time in the subjects (n = 9) of an untreated control group. Propranolol led to an increase of triglycerides and a decrease of HDL cholesterol in plasma, the latter consisting in a small increase of unesterified cholesterol and a larger decrease of cholesteryl esters. In parallel a decrease in the lecithin:cholesterol acyl transfer, measured as initial rate of cholesterol esterification, was observed. The extent of the plasma lipid and enzyme alterations was shown to be dependent on the patient's pretreatment situation. Changes in lecithin:cholesterol acyl transfer rate after oral treatment correlated significantly with similar changes after propranolol addition in comparable amounts to plasma in vitro. A similarity between propranolol induced alterations in the metabolism of plasma lipoproteins and the situation in hereditary LCAT deficiency is obvious and may be interpreted as a harmful component of propranolol action.

Cholesterol Esters↗
PubMedDate not supplied

[Preparation of proteoliposomes--an artificial substrate for measuring the rate of the lecithin-cholesterol-acyltransferase reaction in whole plasma].

A procedure is described for production of artificial substrate, containing except of cholesterol and lecithin as well as the protein moiety, used in estimation of the rate of lecithin-cholesterol-acyltransferase reaction in whole blood plasma. The protein component of proteoliposomes involved total fraction of apoproteins of high density lipoproteins (HDL). The proteins containing in proteoliposomes were obtained by means of chloroform-methanol delipidation of the total HDL fraction, isolated from human blood plasma using preparative ultracentrifugation. Optimal concentration of the apoprotein in proteoliposomes was determined.

Cholesterol Esters↗
PubMed1979

Effect of taurine conjugated bile salts with and without lecithin on water and electrolyte transport in the canine gallbladder in vivo.

Because dihydroxy bile salts alter water and electrolyte transport in the intestine, we tested the effects of taurine conjugated bile salts on water and electrolyte transport in the canine gallbladder in vivo. 16.7 mM taurodeoxycholate or taurochenodeoxycholate completely abolished net absorption of water (P less than 0.01). 40 mM taurocholate significantly reduced net water absorption (P less than 0.05), whereas 16.7 mM taurocholate had no significant effect. Net movement of electrolytes was closely related to net water movement. Water and electrolyte absorption continued undisturbed when the gallbladders were exposed to 16.7 mM taurodeoxycholate together with 5.6 mM lecithin. Biliary lecithin, therefore, is important for the protection of the mucosa of the gallbladder from the potentially damaging effects of bile salts.

Animals↗
PubMed1979

Temperature and compositional dependence of the structure of hydrated dimyristoyl lecithin.

Differential scanning calorimetry and x-ray diffraction techniques have been used to investigate the structure and phase behavior of hydrated dimyristoyl lecithin (DML) in the hydration range 7.5 to 60 weight % water and the temperature range -10 to +60 degrees C. Four different calorimetric transitions have been observed: T1, a low enthalpy transition (deltaH approximately equal to 1 kcal/mol of DML) at 0 degrees C between lamellar phases (L leads to Lbeta); T2, the low enthalpy "pretransition" at water contents greater than 20 weight % corresponding to the transition Lbeta leads to Pbeta; T3, the hydrocarbon chain order-disorder transition (deltaH = 6 to 7 kcal/mol of DML) representing the transition of the more ordered low temperature phases (Lbeta, Pbeta, or crystal C, depending on the water content) to the lamellar Lalpha phase; T4, a transition occurring at 25--27 degrees C at low water contents representing the transition from the lamellar Lbeta phase to a hydrated crystalline phase C. The structures of the Lbeta, Pbeta, C, and Lalpha phases have been examined as a function of temperature and water content. The Lbeta structure has a lamellar bilayer organization with the hydrocarbon chains fully extended and tilted with respect to the normal to the bilayer plane, but packed in a distorted quasihexagonal lattice. The Pbeta structure consists of lipid bilayer lamellae distorted by a periodic "ripple" in the plane of the lamellae; the hydrocarbon chains are tilted but appear to be packed in a regular hexagonal lattice. The diffraction pattern from the crystalline phase C indexes according to an orthorhombic cell with a = 53.8 A, b = 9.33 A, c = 8.82 A. In the lamellae bilayer Lalpha strucure, the hydrocarbon chains adopt a liquid-like conformation. Analysis of the hydration characteristics and bilayer parameters (lipid thickness, surface area/molecule) of synthetic lecithins permits an evaluation of the generalized hydration and structural behavior of this class of lipids.

Calorimetry, Differential Scanning↗
PubMed1979

[Correlation between cholesterol and lecithin in the blood and muscles and physiologic indices in rats developing in various stress states].

Development female rats during the 1st year of life, under conditions of dynamic exercises caused starting from the 4th month, a decrease in the blood cholesterin and the raise of lecithin and lecithin--cholesterin index (L/Ch). No hypercholesterinemia common for the control animals develops by the 13th month in these animals. The cholesterin content increases in their muscles. Static loads launch less beneficent shifts of the above parameters. These rats reveal larger amount of the blood cholesterin along with its decrease in the muscles by the end of the 1st year. Under nociceptive effects the rats develop hypercholesterinemia and hypolecithinemia yet by the 7th month which accounts for a sharply reduced L/Ch index. At 13 months cholesterin is obviously decreased in the muscles of these rats. Resting energy expenditure is increased in these rats due to activated thyroid function and to a decrease in the cholinergic maintenance of regulation.

Acetylcholinesterase↗