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PubMed2003

Dietary fats differentially modulate the expression of lecithin:cholesterol acyltransferase, apoprotein-A1 and scavenger receptor b1 in rats.

In the present study the effects of dietary fat with defined fatty acids on lecithin:cholesterol acyltransferase (LCAT) and apoA-1, the two components of HDL that play a major role in reverse cholesterol transport (RCT), were examined. In addition, the expression of scavenger receptor B1 (SR-B1), the receptor involved in the uptake of HDL core lipids, was also determined under the same conditions in rats fed semisynthetic diets supplemented with triolein (TO), tripalmitin (TP) or menhaden oil (MO). Serum LCAT activity [ micro mol CE/(L.h)] was significantly (P < 0.05) higher in rats fed TO (33 +/- 4) compared with those fed TP (23 +/- 3) or MO (21 +/- 1). The levels of hepatic LCAT mRNA and hepatic SR-B1 receptor protein did not differ between rats fed TP and MO. The triolein diet, on the other hand, increased the induction of hepatic LCAT mRNA and hepatic SR-B1 receptor protein 1.5- to 2-fold. Serum HDL cholesterol concentrations differed among all groups and were 1.30 +/- 0.08, 1.17 +/- 0.10 and 0.91 +/- 0.06 mmol/L for TO-, TP- and MO-fed rats, respectively. Serum apoA-1 levels were significantly higher in TO-fed rats than in the other two groups. The data indicate that TO increases the secretion of HDL and its components (apoA-1 and LCAT), and stimulates the production of hepatic SR-B1 receptor protein. Overall, these results suggest that triolein may promote RCT and thus retard the development of atherosclerosis.

Animals↗
PubMed1986

Human lecithin-cholesterol acyltransferase gene: complete gene sequence and sites of expression.

The human lecithin-cholesterol acyltransferase (LCAT) gene has been sequenced to completion. The gene is divided into six exons spanning approximately 4,200 bp. Exon five codes for amino acids homologous to the interfacial active site of several lipases, and also codes for an amphipathic alpha-helix resembling the carboxy terminus of apolipoprotein E. Blot hybridization data suggest that there is only one LCAT gene in humans. The 1550 base LCAT mRNA can be detected in liver and HepG2 (hepatocyte) cells, but not in small intestine, spleen, pancreas, placenta or adrenal tissue.

Base Sequence↗
PubMed2002

Lecithin: cholesterol acyltransferase is insufficient to prevent oxidative modification of low-density lipoprotein.

We tried to confirm the antioxidative capability of lecithin:cholesterol acyltransferase (LCAT) reported by Vohl et al. [Biochemistry (1999) 38, 5976-5981]. The enzyme solution protected LDL against oxidation. However, this protection was not due to LCAT enzyme, but to some unknown low-molecular-weight substance(s) in the solution; LCAT itself exerted little protective effect against LDL oxidation.

Antioxidants↗
PubMed1989

Isolation and properties of rat plasma lecithin-cholesterol acyltransferase.

Lecithin-cholesterol acyltransferase was purified from rat plasma and the properties of this enzyme during the purification procedures and those of the purified enzyme were investigated in comparison with the human enzyme. The rat enzyme was not adsorbed on hydroxyapatite, which was employed for the purification of the human enzyme. When purified human enzyme was incubated at 37 degrees C in 0.1 mM phosphate buffer (pH 7.4; ionic strength, 0.00025), no alteration of enzyme activity was observed for up to 6 h. In the case of the rat enzyme, however, approximately 40% of the enzyme activity was lost under the same conditions. The human enzyme and rat enzyme were both retained on a Sepharose 4B column to which HDL3 was covalently linked, in 39 mM phosphate buffer, pH 7.4. Although the human enzyme was eluted from the column in 1 mM phosphate buffer, the rat enzyme was dissociated from the column at a lower buffer concentration (0.1 mM phosphate buffer). These findings indicate that the rat enzyme effectively associated with HDL3 in 39 mM phosphate buffer, pH 7.4, but the association was more sensitive to increase of ionic strength compared with that of the human enzyme.

Animals↗
PubMed1977

Phosphatidylcholine substrate specificity of lecithin: cholestrol acyltransferase-in high density lipoproteins and in lipids dispersions.

Lecithin: cholesterol acyltransferase (LCAT) was more highly activated by apolipoprotein A-I (apoA-I) with dimyristoyl phosphatidylcholine (DMPC) than with dilinoleoyl phosphatidylcholine (DLPC) when lipid dispersion of cholesterol and each phosphatidylcholine was used as a substrate. When the enzyme reactions were activated by whole apolipoproteins of high density lipoproteins (HDL), DLPC was more available to the LCAT reaction than DMPC with high concentrations of apoHDL in an incubation mixture. However, no detectable enzyme reaction was observed with dipalmitoyl phosphatidylcholine (DPPC) under both conditions. On the other hand, all of these phosphatidylcholines acted as substrates of LCAT when they were incorporated into HDL coupled to Sepharose. The order of their relative reactivities to cholesterol was DMPC, DPPC, AND DLPC under the conditions used.

Apolipoproteins↗
PubMed1980

Liposomal membranes. VI. Polysaccharide-induced aggregation of multilamellar liposomes of egg lecithin.

Induced aggregation of multilamellar liposomes of egg lecithin with several polysaccharides, such as pullulan, dextran, hydroxyethylstarch, and amylopectin, has been investigated in conjunction with structural characteristics of polysaccharides, incubation temperature, ionic strength, and surface charge of liposomes. Aggregation of liposomes as a function of time was followed by monitoring turbidity of the liposome suspension at 600 nm. The inverse relationship between the minimal concentration and molecular weight of polysaccharides for the induced aggregation of liposomes was observed for all the polysaccharides employed. Polysaccharides having larger excluded volume more easily bind to liposomes, leading to the acceleration of the aggregation of liposomes. Hence, the order of efficiency of polysaccharides for the promotion of liposome aggregation was pullulan greater than dextran greater than hydroxyethylstarch congruent to amylopectin. Increasing the surface charge of liposomes brought about a decrease in aggregation irrespective of the sign. Even when negatively charged liposomes were incubated with the cationic DEAE-dextran, the liposome aggregation was depressed. These results including salt effect and temperature dependency of the induced aggregation of liposomes supported a plausible mechanism for the reaction, the polysaccharide-bridging mechanism, which has been provided for the polysaccharide-promoted agglutination of human erythrocytes.

Chemical Phenomena↗
PubMed1986

Selectivity and contribution of lecithin: cholesterol acyltransferase to plasma cholesterol ester formation.

Selectivity factors (Vm/Km) for human and rat lecithin: cholesterol acyltransferases (LCAT) for the transfer of various acyl groups from the 2-position of phosphatidylcholine were determined. By multiplying these values by the proportions of acyl groups at the 2-position of phosphatidylcholine, one can predict the proportions of molecular species of cholesterol ester which will be synthesized by LCAT. In human subjects fasted overnight, the molecular composition of plasma cholesterol ester was found to reflect the LCAT selectivity relatively accurately. This result supports the concepts that hepatic acyl-CoA:cholesterol acyltransferase (ACAT) does not contribute significantly to the synthesis of plasma cholesterol ester and that removal of cholesterol ester from plasma is not selective with respect to molecular species under these conditions. In contrast to the results with humans, the molecular composition of plasma cholesterol ester formed in spontaneously hypertensive rats fed a high-cholesterol diet and then fasted overnight differs from that which is predicted from LCAT selectivity and the proportion of various fatty acids at the 2-position of phosphatidylcholine: these results suggest that cholesterol ester is formed mainly via the ACAT reaction.

Adult↗
PubMed1999

Characterization of functional residues in the interfacial recognition domain of lecithin cholesterol acyltransferase (LCAT).

Lecithin cholesterol acyltransferase (LCAT) is an interfacial enzyme active on both high-density (HDL) and low-density lipoproteins (LDL). Threading alignments of LCAT with lipases suggest that residues 50-74 form an interfacial recognition site and this hypothesis was tested by site-directed mutagenesis. The (delta56-68) deletion mutant had no activity on any substrate. Substitution of W61 with F, Y, L or G suggested that an aromatic residue is required for full enzymatic activity. The activity of the W61F and W61Y mutants was retained on HDL but decreased on LDL, possibly owing to impaired accessibility to the LDL lipid substrate. The decreased activity of the single R52A and K53A mutants on HDL and LDL and the severer effect of the double mutation suggested that these conserved residues contribute to the folding of the LCAT lid. The membrane-destabilizing properties of the LCAT 56-68 helical segment were demonstrated using the corresponding synthetic peptide. An M65N-N66M substitution decreased both the fusogenic properties of the peptide and the activity of the mutant enzyme on all substrates. These results suggest that the putative interfacial recognition domain of LCAT plays an important role in regulating the interaction of the enzyme with its organized lipoprotein substrates.

Candida↗
PubMed1993

Expression of cellular retinol-binding protein and lecithin-retinol acyltransferase in developing rat testis.

Vitamin A deficiency in mammals results in the loss of germ cells on the adluminal side of the blood-testis barrier, suggesting a need for vitamin A that would be supplied by the surrounding Sertoli cells. Cellular retinol-binding protein (CRBP) and lecithin-retinol acyltransferase (LRAT) are two proteins found in Sertoli cells that are known to be involved in vitamin A trafficking. To clarify the role of these two proteins in the delivery of vitamin A to developing germ cells, we have examined changes in their cell-specific expression during the onset of puberty in the rat. In adult rats, Sertoli cell expression of CRBP varies with the cycle of the seminiferous epithelium. Here, we demonstrate that differences in the intensity of CRBP immunoreactivity are detectable in Sertoli cells of different tubules as early as postnatal Day 4, prior to the onset of meiosis. This indicates that variable expression of CRBP by Sertoli cells is established independently of late germ cells and may anticipate the cyclical variation seen in the adult. We further demonstrate that the specific activity of LRAT in rat testis increases tenfold between postnatal Days 20 and 35. This increase is attributable to the appearance of post-meiotic germ cells: the LRAT activity of microsomes prepared from a round spermatid-enriched cell fraction from post-pubertal rat testis could account for the majority of the LRAT activity observed in the whole testis. The presence of LRAT activity within adluminal germ cells suggests that they receive vitamin A as retinol and synthesize the retinyl esters that have been shown to be present in mature sperm.

Acyltransferases↗
PubMed1996

Intravenous lecithin-coated microcrystals of dantrolene are effective in the treatment of malignant hyperthermia: an investigation in rats, dogs, and swine.

Dantrolene effectively treats malignant hyperthermia (MH) hut the current form, Dantrium, must be dissolved to a 0.33 mg/mL, pH 9.5 solution. This study describes lecithin-coated microcrystal formulations of sodium dantrolene (MC-NaD) and neutral dantrolene (MC-D) which reconstitute to 200 mg/mL within 1 min. In rats, the pharmacokinetics and pharmacodynamics of MC-NaD and Dantrium were similar: half-lives of 3.1 h, volume distributions of 0.54 and 0.59 L/kg, and 95% effective dose (ED95) values for depression of skeletal muscle twitch height (ED95T) of 2.6 +/- 0.7 and 2.8 +/- 0.5 mg/kg. In swine, the ED95T values for MC-NaD and Dantrium were also similar (2.8 +/- 0.4 vs 2.7 +/- 0.6 mg/kg), but MC-D and Dantrium were only similar at doses more than 2.5 mg/kg (ED95T: 3.5 +/- 0.4 vs 2.7 +/- 0.5 mg/kg). In susceptible swine, MC-NaD successfully treated five of six MH episodes and prevented MH in three of four swine. However, MC-NaD caused marked pulmonary hypertension in swine, while MC-D caused only a mild response that was eliminated by filtration. Likewise, MC-D caused no pulmonary response in dogs. These observations suggest that MC-D has potential to improve the treatment of MH.

Animals↗
PubMed1985

Ultra-long-duration local anesthesia produced by injection of lecithin-coated methoxyflurane microdroplets.

This study was designed to evaluate a new drug delivery system. The authors undertook to determine if microdroplets prepared by encapsulating volatile anesthetics with a membrane of lecithin could be used for local anesthesia. Local anesthesia was determined by monitoring the response of the rat to tail clamping and electrical stimulation of the skin following the intradermal injection of the microdroplets. Microdroplets were prepared from isoflurane, enflurane, halothane, methoxyflurane, diethyl ether, chloroform, and heptane. Although all microdroplet preparations produced local anesthesia, only methoxyflurane microdroplets produced an ultra-long duration of local anesthesia (approximately 24 h). Further characterization of the methoxyflurane microdroplets revealed two important differences from conventional local anesthetics. First, the local anesthetic effect of methoxyflurane reached a plateau that did not change significantly for 20 h while the injection of lidocaine and bupivacaine resulted in a peak effect that returned to baseline within 1 and 3 h, respectively. Second, the anesthetic effect of methoxyflurane remained essentially localized to the site of injection, while the anesthetic effect of lidocaine and bupivacaine migrated 15 cm in less than 1 h. The toxicity and safety of methoxyflurane were evaluated. When administered over the dosage range 1-16% (v/v) intradermally, or by injections into muscle, or by repeat injections every 4 days for 16 days, all animals regained their pretreatment response to painful stimulations, and there was no evidence of gross injury to tissue. Deliberate intravenous injection of 0.8 ml of 6.7% (v/v) methoxyflurane microdroplets had no apparent anesthetic or toxic effect. The present study demonstrates that methoxyflurane microdroplets produce an anesthetic effect that is highly localized, stable in intensity, ultra-long in duration, and reversible.

Anesthesia, Local↗
PubMed1989

Hemodynamic effects of intravenous lecithin-based perfluorocarbon emulsions in dogs.

We evaluated and compared the acute hemodynamic effects of perfluorooctylbromide-100% (PFOB), a fluorocarbon emulsified in lecithin without pluronic-F68 (F68), to those of a standard iodinated contrast agent, renografin-76% (R76), and Fluosol-DA 20% (Fluosol), a fluorocarbon emulsified in part by F68. Five open chest dogs were instrumented to evaluate hemodynamic changes after iv injection of PFOB (1 ml.1 g/kg) and R76 (1 ml.0.37 g of iodine/kg). Fluosol (1 ml.0.2 g/kg) was given to two of the five dogs at the end of their study. Fluosol caused transient hemodynamic collapse in both dogs. R76 caused the known transient effect of hypotension (-15.4 +/- 3.3%) followed by hypertension (6.5 +/- 2.7%) and an increase in aortic flow (29.3 +/- 3.9% at 30 sec). PFOB caused minimal, clinically insignificant decrease in aortic flow (4 +/- 1% at 10 sec).

Animals↗
PubMed1998

Effects of vitamin E and HMG-CoA reductase inhibition on cholesteryl ester transfer protein and lecithin-cholesterol acyltransferase in hypercholesterolemia.

BACKGROUND: The enzyme lecithin-cholesterol acyl transferase (LCAT) esterifies free cholesterol on high-density lipoprotein (HDL) and the cholesteryl ester transfer protein (CETP) transfers cholesteryl ester to very-low-density lipoprotein (VLDL) and low-density lipoproteins (LDL). Using statins, contradictory findings have been made regarding CETP activity in normolipidemic individuals and in those with familial dysbetalipoproteinemia. In contrast, LCAT activity appears to be unaffected by simvastatin. Antioxidants have also been proposed for the use of anti-atherosclerotic treatment, because the oxidation of LDL may have a key role in the pathophysiology of atherogenesis. OBJECTIVE: To investigate, in hypercholesterolemic patients, whether a combination of pravastatin with the antioxidant, vitamin E, has greater effects on the activity of CETP and of LCAT than does pravastatin alone. METHODS: This placebo-diet-controlled multicenter trial included 220 hypercholesterolemic patients who were assigned randomly to groups to receive: diet and 20-40 mg pravastatin (n = 52), diet and alpha-tocopherol (n = 60), or diet associated with placebo (n = 52). Plasma LCAT activity was determined using excess exogenous substrate, containing [3H]cholesterol. Plasma CETP activity was measured in the supernatant fraction after precipitation of endogenous apo B-containing lipoproteins with phosphotungstate-Mg2+. The exchange of cholesteryl esters between [14C]cholesteryl ester-labeled LDL and unlabeled HDL was measured during a 16-h incubation, while LCAT was inhibited. RESULTS: The addition of pravastatin to the diet induced a significant decrease in plasma CETP activity (P < 0.05); this effect was less evident in the group cotreated with vitamin E. For the first time, it was shown that CETP concentrations increased significantly after vitamin E alone (P < 0.05). No significant differences in the plasma activity of LCAT were observed among the groups. CONCLUSIONS: Pravastatin reduced CETP activity, but not that of LCAT. Addition of vitamin E prevented the decrease in CETP activity and had no effect on LCAT activity. The mechanism responsible for these effects is unknown, but could involve the prevention of radical-induced damage to CETP by vitamin E.

Antioxidants↗
PubMed1995

Lipases and lecithin: cholesterol acyltransferase in the control of lipoprotein metabolism.

Lipoprotein lipase, hepatic lipase, and lecithin: cholesterol acyltransferase have coordinated enzymatic roles in lipoprotein metabolism. New evidence suggests that the lipases are multifunctional proteins that are able to mediate lipoprotein binding and uptake. The importance of all three enzymes in the control of lipoprotein metabolism can be explored in the future by using the newly generated transgenic animals.

Animals↗
PubMed2000

Lecithin-cholesterol acyltransferase: role in lipoprotein metabolism, reverse cholesterol transport and atherosclerosis.

In the past several years significant advances have been made in our understanding of lecithin-cholesterol acyltransferase (LCAT) function. LCAT beneficially alters the plasma concentrations of apolipoprotein B-containing lipoproteins, as well as HDL. In addition, its proposed role in facilitating reverse cholesterol transport and modulating atherosclerosis has been demonstrated in vivo. Analysis of LCAT transgenic animals has established the importance of evaluating HDL function, as well as HDL plasma levels, to predict atherogenic risk.

Animals↗
PubMed1991

Purification and characterization of a lecithin-dependent haemolysin from Escherichia coli transformed by a Vibrio parahaemolyticus gene.

Lecithin-dependent haemolysin (LDH) of Vibrio parahaemolyticus was purified from Escherichia coli C600 transformed with a plasmid (pHL591) ligated with a 1.5 kb DNA fragment of V. parahaemolyticus. The final preparation comprised two LDH proteins with different molecular masses which were immunologically cross-reactive and had the same enzymic activity. The LDH was a phospholipase hydrolysing both fatty acid esters of phospholipid, i.e. it hydrolysed phosphatidylcholine (PC) to lysophosphatidylcholine (LPC) and then LPC to glycerophosphorylcholine (GPC). From this point of view, LDH should be classified as a phospholipase B. Phospholipase B, however, does not usually show haemolytic activity, because the intermediate (LPC), which is the actual haemolytic agent, is immediately hydrolysed to the final product (GPC). On the other hand, LPC formed by LDH action was comparatively stable, because the rates of the two reactions catalysed by LDH, PC to LPC and LPC to GPC, are almost the same. This is the reason that LDH shows haemolytic activity. Therefore, LDH of V. parahaemolyticus is an atypical phospholipase to be designated as phospholipase A2/lysophospholipase.

Amino Acid Sequence↗
PubMed1999

Single-particle dynamics of water molecules confined in a lecithin-based gel.

We present experimental measurements, obtained by a quasielastic neutron scattering experiment, of the self-diffusion coefficient of water confined in the dense structure of lecithin-based gels. The inelastic neutron scattering (INS) technique was also used to monitor the dynamic state of water molecules involved in the gel structure. It is shown that, at least in highly concentrated systems, the diffusional properties of water can be related with the growth process of worm-like aggregates. However, an interpretation of our data consistent with a number of experimental results in the literature and with INS indications requires the adoption of a model in which the gel structure is better described in terms of percolating aggregates rather than the usually described polymer-like entangled (not interconnected) network. In such a way, we are pointing out the existence of an interpretative controversy calling for further investigation to be disentangled. The source of the inconsistencies is found in the commonly accepted basic assumption of the existence of a simple scaling law, relating the average micellar length to the concentration.

Journal Article↗
PubMed1970

Lecithin Biosynthetic Enzymes of Onion Stem and the Distribution of Phosphorylcholine-Cytidyl Transferase among Cell Fractions.

Enzymatic activities of the cytidine 5'-diphosphate choline pathway for lecithin biosynthesis were demonstrated in homogenates of onion stem (Allium cepa). Choline kinase activity was present in the postmicrosomal supernatant, with less than 3% sedimenting with the particulate fractions. Phosphorylcholine-cytidyl transferase was distributed among all fractions, and phosphorylcholine-glyceride transferase was predominantly found in the particulate fraction.The phosphorylcholine-cytidyl transferase activity of onion stem required a divalent ion (Mg(2+) or Mn(2+)) for activity, was inhibited by Ca(2+), and was specific for cytidine triphosphate, with optimal activity in the range pH 6 to 7. To evaluate the distribution among cell fractions, conditions of pH, cofactors, substrate, and assay were optimized for each fraction. One-third of the transferase activity sedimented with the mitochondria-proplastids fraction, and one-third was in the microsomal supernatant. The dictyosome fraction contained about 10% of the total activity but showed a greater specific activity than the other fractions. Similar results were obtained with homogenates from rat liver, in that purified Golgi apparatus fractions contained the highest phosphorylcholine-cytidyl transferase activity on a protein basis when compared with other cell fractions at pH 7.2.

Journal Article↗