Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “LECITHINS”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 955 records · Page 53Linked to original sources

The activity of lecithin:cholesterol acyltransferase in the serum of cows at parturition or with fatty liver.

The activity of lecithin:cholesterol acyltransferase (LCAT), which is responsible for esterification of plasma cholesterol, was evaluated in bovine serum. It was associated with the high-density lipoprotein fraction that contains apolipoprotein A-I, an activator of LCAT. In lactating cows, the activity was around 1000 U (decrease in nmol of free cholesterol per h per ml of serum), slightly higher than in 1-month-old calves. LCAT activity decreased around parturition, at which the time the serum concentrations of cholesteryl esters and free cholesterol were concomitantly decreased. A reduced LCAT activity was also found in cows with fatty livers induced by the administration of ethionine. In the cows with fatty livers, the serum concentration of cholesteryl esters was markedly decreased, whereas that of free cholesterol was only slightly decreased, thereby increasing the free- to esterified-cholesterol ratio. These results suggest that the decrease in LCAT activity may be involved in the reduction in fertility associated with fatty liver because esterification of cholesterol by LCAT is essential for its transport from the liver to peripheral tissues, such as the corpus luteum, and because cholesterol serves as the source of progesterone synthesis in the latter organ.

Animals↗

Effects of starvation and plasma exchange on lecithin: cholesterol acyltransferase activity and cholesterol efflux in cholesterol-fed pigs.

The effects of starvation and of plasma exchange with a cholesterol-free substitute on efflux of tissue cholesterol and on lecithin: cholesterol acyltransferase (LCAT) activity in plasma and peripheral lymph were investigated in two pigs fed a cholesterol diet for 3-4 months. The pigs were labelled with i.v. [14C]cholesterol before plasma exchange or starvation. The cholesterol diet increased plasma total cholesterol concentration and LCAT activity in plasma and lymph, but had little effect on the rate of esterification of cholesterol in plasma or lymph. During cholesterol feeding, and when the animals were fed a normal diet, cholesterol esterification rates in plasma and lymph were much lower than the maximum rates achieved when LCAT was saturated with substrate, suggesting that LCAT in normal pig plasma and lymph is not saturated with substrate. Plasma exchange, carried out when the specific activity of tissue cholesterol exceeded that of plasma cholesterol, was followed by a brief rise in the specific activity of plasma cholesterol to a maximum value between the specific activities of muscle and adipose-tissue cholesterol, reflecting the transfer of radioactive cholesterol from tissue to plasma. During the rise in plasma total cholesterol specific activity there were no differences between the specific activities of low-density lipoprotein (LDL) cholesterol and high-density lipoprotein (HDL) cholesterol in plasma or lymph. Starvation had no effect on the plasma-cholesterol specific-activity curve. From about day 14 after labelling, cholesterol-specific activity decreased in the order: tissues greater than lymph greater than plasma. This suggests that the transfer of cholesterol from tissues to plasma was mediated by lipoproteins in the interstitial fluid.

Animals↗

Properties of the conductance induced in lecithin bilayer membranes by alamethicin.

Current-voltage relations have been measured across lecithin bilayers doped with alamethicin molecules. The results show that there are two aspects of the induced conductances, a voltage-dependent and a voltage-independent conductance. Both have been characterized as a function of alamethicin and KCl concentration. The two aspects of the conductances do not show the same changes with those two variables. The voltage-independent conductance is affected very little by changes in KCl concentration, and its dependance on alamethicin concentration reveals that it is produced by two or three alamethicin molecules. The voltage-dependent conductance is shifted by the changes in KCl concentration only when the concentrations are greater than or equal to 100 mM; below 100 mM KCl the slope of the log conductance-voltage curve is also reduced. The effect of changing alamethicin concentration reveals that nine or ten molecules are involved for KCl concentrations larger than 100 mM; if the KCl concentration is less than 100 mM, the effect of changing the alamethicin concentration is reduced. Time-dependent measurements have also been performed; only one time constant was found and it is strongly voltage-dependent. Also a very slow voltage-dependent absorption process is found. These results can be explained if it is assumed that pores are formed of a mixture of charged and uncharged alamethicin molecules when a voltage is applied and that uncharged alamethicin can also form pores without applying a voltage, once the absorption process has been started by previously applied voltages. The voltage dependence of the time constant seems to indicate that the voltage-dependent pore formation is produced by aggregates of charged alamethicin rather than independent molecules.

Alamethicin↗

Transmembrane electrophoresis of 8-anilino-1-naphthalenesulfonate through egg lecithin liposome membranes.

Valinomycin has been shown to increase the amount of 8-anilino-1-naphthalenesulfonate (ANS) bound to egg lecithin liposomes and also to increase the maximum fluorescence value, as derived from double reciprocal plots. The assay conditions were such that addition of valinomycin would not produce a transmembrane potential. The formation of a valinomycin potassium ANS complex in the micelle membrane is proposed. This could account for the increase in the maximum fluorescence value and, by acting as an ANS transporter, could also account for the increase in ANS bound. Tributylamine was also shown to increase the binding and maximum fluorescence of ANS. In assay conditions where the addition of valinomycin would produce a transmembrane potential negative inside, the tributylamine-induced fluorescence was reversed. The fluorescense decrease is interpreted as transmembrane electrophoresis of ANS in response to a transmembrane potential.

Anilino Naphthalenesulfonates↗

Ion and sugar permeabilities of lecithin bilayers: comparison of curved and planar bilayers.

Na+ and sugar permeabilities of egg lecithin bilayers were measured using curved bilayers and planar bilayers as represented by single-bilayer vesicles and black lipid films, respectively. The Na+ permeability coefficient measured with single-bilayer vesicles at 25 degrees C is (2.1 +/- 0.6) x 10(-13) cm sec-1. Because of technical difficulties it has been impossible to measure ionic permeabilities of values lower than about 10(-10) cm sec-1 in planar (black) lipid bilayers using tracer methods. The D-glucose and D-fructose permeabilities were measured with both curved and planar bilayers. The permeability coefficients measured with vesicles at 25 degrees C are (0.3 +/- 0.2) x 10(-10) cm sec-1 for glucose and (4 +/- 1) x 10(-10) cm sec-1 for D-fructose; these are in reasonable agreement with the corresponding values obtained for planar (black) lipid bilayers which are (1.1 +/- 0.3) x 10(-10) cm sec-1 for D-fructose, respectively.

Animals↗

Phospholipases. III. Effects of ionic surfactants on the phospholipase-catalyzed hydrolysis of unsonicated egg lecithin liposomes.

Apparent values of Km and Vmax have been measured for catalysis of hydrolysis of unsonicated egg lecithin liposomes, activated through addition of 0.4 M n-hexanol, by phospholipases A2 from bee and snake venoms and by phospholipase C from Clostridium welchii as a function of the concentration of three surfactants: hexadecylamine, hexadecyltrimethylammonium bromide, and dihexadecyl phosphate. For all three enzymes, values of Km and Vmax show little or no dependence on the concentration of these ionic surfactants, demonstrating that the liposomal surface charge is not a crucial factor in determining susceptibility to phospholipase-catalyzed hydrolysis.

Amines↗

Role of interfacial structured water in membrane: osmotic properties of L-alpha-egg lecithin liposomes.

The role of large amounts of membrane-bound water in regulating various functions of the membrane is not clear at present. We have investigated the effect of perturbing the interfacial water structure on the osmotic shrinkage properties, such as water permeability and extent of shrinkage of egg lecithin liposomes. Water structure was perturbed by a series of reagents which have been earlier reported to affect phase transition of dipalmitoyl phosphatidylcholine liposomes by perturbing interfacial water structure. Anomalous variations of osmotic shrinkage properties with concentration of structure maker and breaker reagents have been interpreted to arise from concentration-dependent structural transitions of the ordered water at the membrane-aqueous interface. Various modes of interaction of these reagents on interfacial structured water have been suggested. Influence of molecular size and functional groups on the molecule in actions of some structure makers and breakers were also observed.

Amines↗

Binding and incorporation of lecithin-cholesterol vesicles to lymphocytes: a spin-label study.

When lecithin-cholesterol vesicles, containing the membrane-bound spin probe 3-doxyl-cholestane, were set in contact with mouse lymphocytes, the vesicles adsorbed to the cell and vesicle-membrane components were transferred to it. The spin probe was enzymatically reduced at the inside of the cell membrane. The spin-label method provided a means to determine quantitatively the extent of vesicles adsorption and vesicle-cell fusion by measuring the transfer of vesicles membrane material to the cell. This method, together with the reduction of spin label by the cell, allowed also a quantitative estimate to the extent of endocytosis during cell-liposome interaction.

Animals↗

Lecithin-cholesterol acyltransferase activity in carbohydrate-induced hypertriglyceridemia in mice.

Feeding to mice of both basal as well as high sucrose diet led to increased levels of plasma triglycerides, which was associated with increased lecithin-cholesterol acyltransferase activity. Although males had significantly higher LCAT activity than females in all the dietary groups, sex difference in the plasma triglycerides was observed in high sucrose group only. Increase in plasma triglycerides in experimental groups was associated with an increase in LCAT activity.

Animals↗

Effect of intralipid infusion on serum high- and low-density lipoprotein cholesterol, lecithin:cholesterol acyltransferase, and lipoprotein lipase in tumor-bearing rats.

We compared the effects of 0.45% normal saline (NS), 5% Intralipid (IL), and 16.7% glucose (Glu) infusions on total serum triglycerides and cholesterol, serum high-(HDL-c) and low-density lipoprotein cholesterol (LDL-c), and activity of serum lecithin:cholesterol acyltransferase (LCAT), and serum lipoprotein lipase (LPL) in rats implanted with a fibrosarcoma. In tumor-bearing rats given NS, a two-fold increase in total serum cholesterol, a four-fold increase in LDL-c, and a five-fold decrease in the HDL-c/LDL-c ratio were observed compared to tumor-free rats. In tumor-bearing rats administered IL, a two-fold increase in total serum triglyceride and cholesterol, a three-fold increase in HDL-c and HDL-c/LDL-c ratio, and a two-fold increase in LPL activity were observed compared to tumor-bearing rats administered NS. In tumor-bearing rats administered Glu, a two-fold decrease in total serum cholesterol, a two-fold decrease in HDL-c, and a three-fold decrease in LDL-c were observed compared to tumor-bearing rats administered NS. Tumor weights and LCAT activity did not differ significantly between treatment groups. Previous results have demonstrated that lipophilic compounds that interact with plasma lipoproteins have altered pharmacological effects when administered with IL. Therefore, this study suggests that IL infusions alter the HDL-c/LDL-c ratio and could affect the pharmacological behavior of anticancer compounds that predominantly distribute into the LDL fraction upon entrance into the bloodstream.

Animals↗

Plasma lecithin: cholesterol acyltransferase activity in high- and low-responding rhesus monkeys.

The initial rate of esterification of plasma cholesterol by lecithin: cholesterol acyltransferase (LCAT) was measured in high- and low-responding rhesus monkeys fed a moderately high cholesterol (0.15 mg/kcal) diet. The results show that the rate of esterification of cholesterol in the plasma of the high-responders was significantly (p less than 0.025) higher than that of the low-responding animals. In view of known relationships between LCAT activity and plasma lipoprotein metabolism, it is suggested that the lipoprotein metabolism in the high-responders would differ from that in the low-responders.

Animals↗

[Investigations of the effect and mechanism of action of the beta-sympathomimetic ritodrine on the synthesis and release of dipalmitoyl-lecithin in the fetal rabbit lung (author's transl)].

For a period of 8 days, pregnant white New Zealand rabbits were treated either with the beta-sympathomimetic Ritodrine (1 mg/kg) body weight daily) or with 0.9% saline solution. The fetuses were delivered by caesarian section on the 25th and 30th day of gestation (term being 31 days). No significant difference was found between the Ritodrine and saline treated groups with respect to the levels of dipalmitoyl-lecithin (DPL) obtained from the homogenates as well as the alveolar lavages of the fetal lungs. These results indicate that with this experimental model, prepartum treatment with Ritodrine has no effect either on DPL synthesis or its release into the alveolar spaces. Furthermore, treatment with the beta-sympathomimetic produced no significant change in the concentrations of the specific glucocorticoid receptors in the cytosol and nuclei of the fetal lungs, and in addition, the lung cytosol glucose concentrations as well as the plasma corticosteroid levels were unaffected. These findings support the conclusion that the synthesis of DPL in the fetal lung is not stimulated by Ritodrine.

Animals↗

Utilization of various sterols by lecithin-cholesterol acyltransferase as acyl acceptors.

Highly purified lecithin-cholesterol acyltransferase of human plasma was used to study the utilization of various sterols as the acyl acceptor. The esterification of sterols was facilitated by the presence of a 3beta-hydroxyl group and the trans configuration of the A/B rings, as was evident from the lack of acceptor activity of all 3 alpha-hydroxy sterols tested and coprostanol. Cholesterol analogs in which the side chain is modified, such as campesterol, beta-sitosterol, desmosterol and stigmasterol, were less effective than cholesterol as acyl acceptors. However, androstan-3 beta-ol, which completely lacks the side chain, was found to be more active than cholesterol. The transfer of the acyl group to all effective sterols required the presence of the cofactor peptide apolipoprotein A-I.

Cholesterol↗

Lecithin-cholesterol acyltransferase: inhibition by local anesthetics in plasma from man and experimental animals in vitro.

Lecithin-cholesterol acyltransferase (LCAT, EC 2.3.1.43) was assayed in vitro in plasma from normal man, rat, rabbit and dog by following the formation of 14C-cholesteryl esters subsequent to labeling the plasma with 14C-cholesterol in vitro. In all species examined, various local anesthetics were found to inhibit LCAT when studied over the concentration range of 1 to 5 mM. The order of inhibition was dibucaine>benzocaine>tetracaine>lidocaine>procaine. Since LCAT activity represents the combined effect of a deacylation step and an esterification step, inhibition of LCAT by local anesthetics could theoretically involve either or both steps.

Adult↗

Reduced plasma lecithin cholesterol acyl transferase activity in rats fed iron-deficient diets.

An iron-deficient diet containing no fat (FF-Fe) or containing either 14% hydrogenated coconut oil (HCNO-Fe) or 14% corn oil (CO-Fe) was fed to separate groups of rats for 10 weeks. In the control group, the corresponding iron-supplemented diets were fed FF+Fe, HCNO+Fe, CO+Fe. When rats were fed iron-deficient diets, their plasma lecithin cholesterol acyl transferase (LCAT) activity was significantly reduced as compared to controls. Their plasma also contained releatively more cholesteryl esters (CE) than free cholesterol (CH). In rats fed FF+Fe and CO+Fe diets, plasma contained similar levels of CE and CH. In those fed HCNO+Fe diet, plasma had 40% less Ce than CH. Red cell CH content was significantly greater in the CO-Fe group. Iron deficiency, as indicated by low blood hemoglobin (Hb) and hematocrit (Hct) values, was also observed only in this group. The triglyceride and phospholipid contents of plasma in rats fed iron-deficient diets were significantly lower than of those in the control groups. Thus, changes in LCAT activity and CE/CH ratio in plasma showed the effect of iron-deficient diet consumption even before the blood Hb and Hct levels were reduced.

Animals↗

Oleic acid transfer from microsomes to egg lecithin liposomes: participation of fatty acid binding protein.

Oleic acid transfer from microsomes or mitochondria to egg lecithin liposomes was stimulated by fatty acid binding protein. By gel filtration, it could be demonstrated that this protein incorporates oleic acid into liposomes. Fatty acid binding protein transfer activity was higher using microsomes rather than mitochondria, which suggests a selective interaction with different kinds of membranes. Transfer of oleic acid by this soluble protein is greater than that of stearic acid. The results indicate that fatty acid binding protein may participate in the intracellular transport of fatty acids.

Animals↗

Inhibition of human lecithin cholesterol acyltransferase by monoterpenes.

The lecithin-cholesterol acyltransferase activity of human plasma was found to be inhibited by Rowachol, a proprietary mixture of pure monoterpenes. Menthol, the major ingredient in Rowachol (32%), and a number of other monoterpenes were found to inhibit the enzyme independently. Concentrations of monoterpenes required to achieve 50% inhibition were of the same order of magnitude as the cholesterol concentration present in the reaction mixture.

Camphor↗

Effect of polyestradiol on lecithin: cholesterol acyltransferase in male and female rats.

The effects of two doses of polyestradiol phosphate of lecithin: cholesterol acyltransferase activity and on liver and plasma cholesterol levels have been studied on female and male rats. Both treatments increased the hepatic content of esterified cholesterol, but the LCAT activity expressed as a percentage of cholesterol esterification was unaltered. The progress of esterification was not affected by the administration of the hormone. The LCAT activity in terms of the initial rate of esterification was decreased by the high dose of estradiol. This decrease was associated with a reduction of free plasma cholesterol level, as there is a significant positive correlation between these two parameters. The findings suggest that the increased esterified cholesterol in liver of estradiol-treated rats ins not mediated by an alteration in the LCAT activity.

Animals↗