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PubMed1987

Defect in cholesterol esterification associated with renal diseases.

Changes in lipidaemia and in cholesterol esterification rate were investigated in 65 patients with chronic mesangial glomerulonephritis (GN), and in 26 patients with polycystic kidneys (PL), as well as in age- and sex-matched control groups. As compared to the controls, a slightly significant increase in cholesterol and triglyceride concentrations was found only for the GN group, whereas the rate of cholesterol esterification showed a highly significant reduction in both groups of diseased subjects. The average values of molar esterification rate (MER) were, respectively, 75.4 and 61.6 mumol . l-1 . h-1 for the GN and PL groups, the respective control values being 96.9 and 91.1. Fractional esterification rate (FER) reflecting the rate of cholesterol exchange between blood and tissues fell in the same two groups of patients to 4.38 and 4.40% . h-1, respectively (controls 6.93 and 6.17). Both the changes in cholesterol esterification rates and a relative increase in the ratio of unesterified to esterified cholesterol were found in patients with low as well as normal glomerular filtration rates.

Adult↗
PubMed1977

Plasma cholesterol esterification in hypertriglyceridaemia.

Plasma cholesterol esterification was assessed in hypertriglyceridaemic patients and normal subjects by two in vitro methods, one using autologous substrate and one using exogenous substrate. There was a significant negative correlation between cholesterol esterification rate and the plasma triglyceride concentration when this was assessed with autologous substrate or with substrate from a hypertriglyceridaemic donor. The percentage of esterified cholesterol in plasma and the esterification rate were always reduced when the plasma triglyceride concentration exceeded 7 mmol/1 and the rate of esterification rose significantly with appropriate triglyceride-lowering therapy in such patients. Evidence is presented that the impaired cholesterol esterification observed in severe hypertriglyceridaemia is secondary to a reduced concentration of substrate high density lipoprotein cholesterol, as well as to an excess of large triglyceride-rich lipoproteins.

Adult↗
PubMed2005

Estradiol fatty acid esterification is increased in high density lipoprotein subclass 3 isolated from hypertriglyceridemic subjects.

Estrogen fatty acid esters are potent lipophilic estrogens transported exclusively in lipoproteins. They are formed in HDL in a reaction catalyzed by LCAT which is considered a prerequisite for their antioxidative action. Our previous studies in normotriglyceridemic (NTG) individuals demonstrated that estradiol (E2) esterification occurred mainly in HDL3 causing accumulation of esterified, but not of unesterified E2 in the lipoprotein particles. Using HDL obtained from hypertriglyceridemic (HTG) patients, we now investigated the effect of altered HDL composition on E2 esterification. Ultracentrifugally isolated HDL2 and HDL3 from NTG- and HTG-males were incubated in an in vitro model system with radioactive and with supraphysiological concentrations of non-radioactive E2 with and without exogenous LCAT. After purification, copper-induced oxidation of HDL was measured by monitoring conjugated diene formation. The results demonstrated that (i) E2 esterification occurring mainly in HDL3 was significantly more efficient in HTG-HDL3 compared to NTG-HDL3, (ii) triglyceride content in HDL3 correlated positively with E2 esterification rate, and (iii) addition of both exogenous LCAT and E2 into the incubation prolonged lag time of HDL3 oxidation. Thus, HDL composition regulates LCAT-facilitated E2 esterification but the in vivo role of this finding can be verified only in experiments using physiological hormone concentrations.

Esterification↗
PubMed1997

Sterol carrier protein-2 mediated cholesterol esterification in transfected L-cell fibroblasts.

The relative function of the 15 and 13.2 kDa forms of SCP-2 in cholesterol trafficking and metabolism was assessed using L-cell fibroblasts permanently transfected with the cDNA encoding for either the mouse 15 kDa or 13.2 kDa SCP-2. Expression of the 15 kDa, but not the 13.2 kDa SCP-2 increased [3H]cholesteryl ester formation from medium derived cholesterol by 30% compared to control cells. In both SCP-2 expressing cell lines, sphingomyelinase treatment increased the initial rate of [3 H]cholesteryl ester formation from plasma membrane derived cholesterol more than 11-fold and elevated [3H]cholesteryl ester levels 1.5-fold compared to control cells. Expression of both proteins resulted in nearly a 1.5-fold increase in [3H]oleic acid esterification into cholesteryl esters, although [3H]oleic acid esterification into triacylglycerols was also increased in the 13.2 kDa SCP-2 expressing cells relative to control. In both transfected cell lines, the cholesteryl ester mass was increased nearly 2-fold compared to control cells, consistent with increased cholesteryl ester synthesis. Similarly, triacylglycerol levels were increased 1.3-fold in the 13.2 kDa SCP-2 expressing cells which is consistent with the increased [3H]oleic acid esterification into triacylglycerol. In the 15 kDa SCP-2 expressing cells, triacylglycerol levels were decreased 60%, but free cholesterol levels were increased 1.2-fold relative to control cells. Thus, only the 15 kDa expression product, containing the putative targeting sequence, specifically enhanced cholesteryl ester formation from either plasma membrane or medium-derived cholesterol. In contrast, the 13.2 kDa expression product, lacking the putative targeting sequence, stimulated an increase in [3H]oleic acid esterification into both cholesterol and triacylglycerol pools, suggesting a non-specific stimulation of fatty acid esterification.

Animals↗
PubMed2002

Effect of clofibrate administration on the esterification and deesterification of steroid hormones by liver and extrahepatic tissues in rats.

Treatment of rats with clofibrate markedly stimulated the liver microsomal esterification of estradiol, testosterone, pregnenolone, dehydroepiandrosterone, and corticosterone by acyl-CoA:steroid acyltransferase. This enzyme catalyzes the esterification of estradiol with long-chain fatty acids in both liver and extrahepatic tissues. In untreated control rats, brain had the highest acyltransferase activity per milligram of microsomal protein for estradiol esterification (3- to 4-fold higher than in the liver). Although, treatment of rats with clofibrate stimulated the esterification of estradiol by 9- to 14-fold in the liver, estradiol esterification in kidney, lung, brain, uterus, fat, and mammary glands was not increased, indicating that liver may be uniquely sensitive to induction of acyl-CoA:estradiol acyltransferase by clofibrate. In additional studies, esterase activity for hydrolysis of the oleoyl ester of estradiol was determined in control and clofibrate-treated rats. Clofibrate administration increased esterase activity by an average of 107% in fat and 70% in liver. The results indicate that treatment of rats with clofibrate stimulates the hepatic formation of highly lipophilic fatty acid esters that can be hydrolyzed in the liver and in extrahepatic tissues to the parent steroid hormone by a clofibrate-inducible esterase.

Animals↗
PubMed1998

Inhibition of acyl coenzyme A:cholesterol acyltransferase blocks esterification but not uptake of cholesterol in Caco-2 cells.

The effects of cholesterol esterase (CEase) and acyl coenzyme A:cholesterol acyltransferase (ACAT) inhibitors on the uptake and esterification of cholesterol in Caco-2 cells were examined. CEase increased the uptake of [3H]cholesterol from bile salt mixed-micelles by 2.5- to 3.0-fold and its esterification by greater than 25-fold. Inhibition of cellular ACAT activity with CL277082 or CP113818 had little or no effect on cholesterol uptake measured in the presence or absence of CEase. The subsequent esterification of [3H]cholesterol was reduced greater than 90% by each ACAT inhibitor. Similar results were obtained in cells in which ACAT activity was induced by preincubation either with 25-hydroxycholesterol and mevalonic acid or with CEase and bile salt mixed-micelles containing 100 micromol/L cholesterol. Neither ACAT inhibitor had an effect on CEase-mediated synthesis or hydrolysis of cholesteryl oleate in vitro. Thus, the uptake of cholesterol from bile salt mixed-micelles in the presence or absence of CEase was not regulated by the level of cellular ACAT expression. The subsequent esterification of exogenous sterol was not due to CEase, but was completely dependent on ACAT activity. The dissociation of cholesterol uptake from ACAT activity suggests that the factors controlling the transfer of sterol from extracellular media to the cell are different from the factors regulating the cellular level of cholesterol esterification.

Bile Acids and Salts↗
PubMed2000

Xanthophyll esterification accompanying carotenoid overaccumulation in chromoplast of Capsicum annuum ripening fruits is a constitutive process and useful for ripeness index.

Changes in xanthophyll esterification degree during pepper fruit ripening have been studied in five cultivars (Numex, Mana, Belrubi, Delfin, and Negral). Esterification of xanthophylls with fatty acids is seen to be a process that is contemporary with and directly linked to the transformation of chloroplast (present in the green fruit) into chromoplast (present in the red fruit). Changes in the fractions of free and partially and totally esterified carotenoids are similar between varieties, reflecting the constitutive nature of esterification as part of the ripening process and being controlled by it. From the first stages of ripening, the fraction of totally esterified pigments (zeaxanthin diester, beta-cryptoxanthin diester, capsanthin diester, and capsorubin diester) makes up almost 50% of the total carotenoid content. The proportion of the partially esterified pigment fraction (zeaxanthin monoester, capsanthin monoester, and capsorubin monoester) in the total carotenoid content increases, with a gradual decrease in the fraction of free pigments (beta-cryptoxanthin, beta-carotene, zeaxanthin, capsanthin, and capsorubin). In the fully ripe stage, a balance is reached between the three esterification fractions (free, partially esterified, and totally esterified), with mean values of 24.17 +/- 4.06, 31.48 +/- 4. 61, and 44.36 +/- 5.05, respectively, which seems to be largely independent of variety. This suggests a marked control of the carotenoid composition of the totally developed chromoplast, indicating its use as an index of ripeness. The inclusion in the present study of a variety (Negral) that retains chlorophylls when ripening, and which shows the same esterification behavior, supports the idea that carotenogenesis is normal and independent of chlorophyll catabolism.

Capsicum↗
PubMed1999

Multidrug resistance (MDR1) P-glycoprotein enhances esterification of plasma membrane cholesterol.

Class I P-glycoproteins (Pgp) confer multidrug resistance in tumors, but the physiologic function of Pgp in normal tissues remains uncertain. In cells derived from tissues that normally express Pgp, recent data suggest a possible role for Pgp in cholesterol trafficking from the plasma membrane to the endoplasmic reticulum. We investigated the esterification of plasma membrane cholesterol under basal conditions and in response to sphingomyelinase treatment in transfected and drug-selected cell lines expressing differing amounts of functional class I Pgp. Compared with parental NIH 3T3 fibroblasts, cells transfected with human multidrug resistance (MDR1) Pgp esterified more cholesterol both without and with sphingomyelinase. Esterification also was greater in drug-selected Dox 6 myeloma cells than parental 8226 cells, which express low and non-immunodetectable amounts of Pgp, respectively. However, no differences in total plasma membrane cholesterol were detected. Transfection of fibroblasts with the multidrug resistance-associated protein (MRP) did not alter esterification, showing that cholesterol trafficking was not generally affected by ATP-binding cassette transporters. Steroidal (progesterone, dehydroepiandrosterone) and non-steroidal antagonists (verapamil, PSC 833, LY335979, and GF120918) were evaluated for effects on both cholesterol trafficking and the net content of 99mTc-Sestamibi, a reporter of drug transport activity mediated by Pgp. In Pgp-expressing cells treated with nonselective and selective inhibitors, both the kinetics and efficacy of inhibition of cholesterol esterification differed from the antagonism of drug transport mediated by Pgp. Thus, although the data show that greater expression of class I Pgp within a given cell type is associated with enhanced esterification of plasma membrane cholesterol in support of a physiologic function for Pgp in facilitating cholesterol trafficking, the molecular mechanism is dissociated from the conventional drug transport activity of Pgp.

3T3 Cells↗
PubMed1978

Effect of sugar and monoglyceride on fatty acid esterification.

The effect of hexose and monoolein on fatty acid esterification was studied in everted rings of rat jejunum. By use of [3H]oleic acid and [U-14C]glucose, esterification via both phosphatidic acid and monoglyceride pathways was quantified. Our results showed that 1) metabolizable sugars stimulate fatty acids esterification regardless of their mode of transport; 2) in the presence of glucose alone, in vitro fatty acid esterification is mediated entirely by the phosphatidic acid pathway; 3) glucose stimulates both esterification pathways in the presence of monoolein; 4) monoolein stimulates only the monoglyceride pathway and has no effect on the phosphatidic acid pathway; and 5) the rate-limiting factor in the presence of monoolein alone is the formation of acyl-CoA, whereas in the presence of glucose alone, the rate-limiting factor is the formation of alpha-glycerophosphate.

Acyl Coenzyme A↗
PubMed2001

Insulin increases FA uptake and esterification but reduces lipid utilization in isolated contracting muscle.

We examined the effect of insulin on the synthesis and degradation of muscle lipid pools [phospholipid (PL), diacylglycerol (DG), triacylglycerol (TG)] and palmitate oxidation in isolated resting and contracting (20 tetani/min) soleus muscles. Lipid metabolism was monitored using the previously defined pulse-chase procedure. At rest, insulin significantly increased total palmitate uptake into soleus muscle (+49%, P < 0.05), corresponding to enhanced DG (+60%, P < 0.05) and TG (+61%, P < 0.05) esterification, but blunted palmitate oxidation (-38%, P < 0.05) and TG hydrolysis (-34%, P < 0.05). During muscle contraction, when total palmitate uptake was increased, insulin further enhanced uptake (+21%, P < 0.05) and esterification of fatty acids (FA) to PL (+73%, P < 0.05), DG (+19%, P < 0.05), and TG (+161%, P < 0.01). Despite a profound shift in the relative partitioning of FA away from esterification and toward oxidation during contraction, the increase in palmitate oxidation and TG hydrolysis was significantly blunted by insulin [oxidation, -24% (P = 0.05); hydrolysis, -83% (P < 0.01)]. The effects of insulin on FA esterification (stimulation) and oxidation (inhibition) during contraction were reduced in the presence of the phosphatidylinositol 3-kinase inhibitor LY-294002. In summary, the effects of insulin and contraction on palmitate uptake and esterification are additive, while insulin opposes the stimulatory effect of contraction on FA oxidation and TG hydrolysis. Insulin's modulatory effects on muscle FA metabolism during contraction are mediated at least in part through phosphatidylinositol 3-kinase.

Animals↗
PubMed1993

Cell-derived unesterified cholesterol cycles between different HDLs and LDL for its effective esterification in plasma.

Pulse-chase incubations of human plasma with [3H]cholesterol-laden skin fibroblasts or low density lipoproteins (LDL) and nondenaturing two-dimensional electrophoresis were used to study the transfer and esterification of cell-derived unesterified cholesterol (UC) in human plasma lipoproteins. Specific radioactivities ([3H]UC per microgram of UC) were calculated, and net cholesterol mass transfer was quantified using a fluoro-enzymatic assay to validate productive transfers of UC between high density lipoprotein (HDL) and LDL. Cellular UC was initially taken up by pre-beta 1-HDL and subsequently transferred in the sequence pre-beta 2-HDL-->pre-beta 3-HDL-->alpha-HDL-->LDL. During the first 5 minutes of this process, only 5% of cellular cholesterol was esterified in pre-beta 3-HDL and alpha-HDL; the remainder reached LDL as UC. Cellular UC accumulating in LDL was then redistributed to various HDL particles via two pathways: 1) the partially LDL receptor-mediated uptake and re-secretion of UC by cells and 2) the direct transfer of UC to HDL, mostly to alpha-HDL and a small amount to pre-beta-HDL. UC was not transferred from LDL to HDL after inhibition of lecithin:cholesterol acyltransferase (LCAT). The esterification of cellular [3H]cholesterol in plasma was competitively inhibited by the addition of excess unlabeled LDL but not of excess HDL. However, both excess LDL and excess HDL prevented the esterification of cell-derived cholesterol in apolipoprotein B-free plasma. This demonstrated that LDL is the major source of UC to the LCAT reaction and that the transfer of UC from LDL to HDL is LCAT dependent. In conclusion, the effective esterification of cell-derived cholesterol in plasma involves a rapid transfer of UC via HDL particles to LDL, from which it is distributed to pre-beta-HDL and alpha-HDL. Furthermore, we hypothesize that the transfer per se of cellular UC to LDL forms a cholesterol concentration gradient between cell membranes and HDL and thus a second, reverse cholesterol transport mechanism in addition to the esterification of cholesterol by LCAT.

Cells↗
PubMed1981

Lipoproteins and cholesterol esterification rate in men and women with hypercholesterolaemia of type IIa.

The purpose of this study was to investigate sexual differences regarding lipoprotein concentrations and compositions, and the cholesterol esterification rate in subjects with type IIa hypercholesterolaemia. Twenty men and 33 women with type IIa hyperlipoproteinaemia, asymptomatic as regards ischaemic heart disease were investigated. Total cholesterol (TC), triglycerides (TG) and phospholipids (PL) were measured in plasma and in the very-low-density (VLDL), low-density (LDL) and high-density lipoprotein (HDL) fractions. The cholesterol esterification rate was determined in plasma in vitro. In comparison with the male group the females had higher concentrations of TC and PL in the HDL, leading to higher ratios of HDL-TC/LDL-TC and HDL-PL/LDL-Pl in the females group. The cholesterol esterification rates were equal in the sexes. However, relations between the cholesterol esterification rates and lipoprotein concentrations and between cholesterol esterification rates and overweight were not equal in the sexes. The higher HDL-TC concentration and HDL-TC/DL-TC ratio in women than in men with type IIa might partly explain the lower female morbidity in cardiovascular disease.

Adult↗
PubMed2000

Interleukin-4 augments acetylated LDL-induced cholesterol esterification in macrophages.

Activated subpopulations of lymphocytes and mast cells have been detected in atherosclerotic lesions. Interleukin-4 (IL-4) is a prominent cytokine released during activation of both cell types and its transcripts have been detected in both human and mouse atherosclerotic lesions. To define whether this local release of IL-4 influences macrophage lipid metabolism, we examined the effects of this cytokine on intracellular cholesterol esterification during incubation with modified low density lipoprotein (LDL). IL-4 greatly augmented cholesterol esterification induced by acetylated LDL (AcLDL) in both mouse peritoneal macrophages and the murine macrophage cell line, J774. This augmentation was maximal at a concentration of 1 ng/ml after incubation for 48 h. This was not a generalized effect on lipoprotein metabolism as IL-4 had no effect on cholesterol esterification in the presence of either LDL or beta-VLDL. Determination of binding isotherms demonstrated that IL-4 increased the number of cell surface binding sites for AcLDL. The IL-4-augmented AcLDL-induced cholesterol esterification was attenuated by the scavenger receptor class A (SR-A) antagonist, fucoidan, and the anti-mouse SR-A monoclonal antibody, 2F8. These data, combined with the known receptor specificity of AcLDL interactions, imply a role of SR-A in the IL-4 induced responses. Two cytokines that have been demonstrated previously to down-regulate SR-A, TNF-alpha and TGF-beta, antagonized the IL-4-induced augmentation of cholesterol esterification. Therefore, local release of IL-4 within atherosclerotic lesions could have a profound effect on macrophage lipid metabolism and the subsequent atherogenic process.

Animals↗
PubMed1975

Substrate specificity of lecithin:cholesterol acyltransferase. Esterification of desmosterol, b-sitosterol, and cholecalciferol in human plasma.

Desmosterol and beta-sitosterol were esterified when incubated with normal human plasma. The initial rate of demosterol esterification was 1.7 times faster, and that of beta-sitosterol 0.4 times slower, than the esterification rate of cholesterol. These ratios were found to be almost the same when plasma from different normal individuals was tested. Plasma from a patient with familial lecithin:cholesterol acyltransferase deficiency did not esterify any of the sterols. The esterification of desmosterol and beta-sitosterol was considerably slower in normal plasma in which in vitro cholesterol esterification previously had taken place. The different esterification rates could not be explained by a different affinity of the plasma lipoproteins for the sterols tested. Cholecalciferol added to normal plasma did not become esterified.

Acyltransferases↗
PubMed1991

Failure of the intracellular itinerary of beta very low density lipoproteins to augment cholesterol esterification in macrophages from Watanabe heritable hyperlipidemic rabbits.

beta very low density lipoproteins (beta-VLDL) interact with mouse peritoneal macrophages via specific receptors leading to pronounced stimulation of cholesterol esterification. The present study has defined an alternative pathway for the processing of beta-VLDL in alveolar macrophages from Watanabe heritable hyperlipidemic (WHHL) rabbits. Macrophages from either New Zealand (NZ) or WHHL rabbits degraded 125I-beta-VLDL to an equivalent extent. Degradation was competed to a similar extent in both cell types by either excess unlabeled beta-VLDL or low density lipoprotein, indicative of a specific receptor involvement. Accumulation of intracellular degradation products of beta-VLDL labeled with the residualizing label, dilactitol-125I-tyramine, was similar in both cell types demonstrating that degradation was not due to secreted proteolytic enzymes. beta-VLDL promoted the incorporation of [3H]oleate into cholesteryl-[3H]oleate and increased the cellular mass of cholesterol in NZ macrophages. In contrast, beta-VLDL did not augment cholesteryl-[3H]oleate deposition in WHHL macrophages. This lack of cholesterol esterification occurred despite equivalent acyl-CoA:cholesterol acyltransferase activity in microsomal fractions of both cell types, and similar augmentations in cholesteryl-[3H]oleate during incubation with phospholipase C-treated LDL. Incubation of WHHL macrophages with beta-VLDL increased cellular cholesterol mass, although the response was attenuated compared to NZ cells. To determine whether these disparities in cholesterol esterification were related to the catabolic fate of beta-VLDL-derived cholesterol esters, [3H]cholesteryl oleate was exchanged into the core of beta-VLDL and incubated with macrophages in medium containing [14C]oleate. NZ macrophages accumulated both [3H]cholesterol and [3H]cholesteryl-[14C]oleate after 5 h, indicating hydrolysis and re-esterification of cholesterol esters. In contrast, WHHL macrophages only accumulated [3H]cholesterol esters, suggesting uptake of cholesterol esters without subsequent hydrolysis. These data demonstrate that WHHL macrophages possess a pathway for the intracellular processing of beta-VLDL that permits internalization of the particle without stimulation of cholesterol esterification.

Animals↗
PubMed1990

Mechanism of free fatty acid re-esterification in human adipocytes in vitro.

Within adipose tissue, free fatty acids liberated by lipolysis may be re-esterified into newly synthesized triacylglycerol. We hypothesized that re-esterification may occur via an extracellular route, such that free fatty acids arising from lipolysis must leave the adipocyte and be taken up again before they can be re-esterified. We simultaneously measured rates of lipolysis, acylglycerol synthesis, and free fatty acid re-esterification in human adipose tissue and isolated adipocytes in vitro, utilizing a dual-isotopic technique. We manipulated incubations to increase mixing of released free fatty acids with the incubation medium. Such manipulations should decrease the probability that released free fatty acids would be taken up and re-esterified. We found that re-esterification was decreased in isolated adipocytes compared to fragments of tissue, in shaken compared to unshaken incubations, and in low adipocyte concentrations compared to high adipocyte concentrations. Rates of acylglycerol synthesis and lipolysis were unaltered by these manipulations, indicating that changes in free fatty acid re-esterification are not secondary to effects on these processes. The results are consistent with an extracellular route for free fatty acid re-esterification. Such a mechanism suggests that adipose tissue blood flow may play an important role in the regulation of free fatty acid release from adipose tissue.

Adipose Tissue↗
PubMed1986

Factors influencing the cholesterol esterification rate in lecithin cholesterol acyltransferase radioassay.

Factors affecting the esterification rate of cholesterol by lecithin cholesterol acyltransferase (LCAT E.C. 2.3.1.43) in native cold labelled substrates (human, rabbit, rat serum, plasma, VLDL, LDL depleted serum, rabbit intraocular fluids) repaired by use of ready-made 14C-cholesterol discs (Cholesterol kinetics LCAT-test, UVVVR, Czechoslovakia) were investigated. EDTA added to the serum during the cold incubation (18 h, 0 degrees C-4 degrees C) increased the rate of esterification due to elimination of Ca2+ ions. The similar stimulating effect was found in the presence of mercaptoethanol (ME) in the serum, while in the plasma already stimulated by EDTA no additional effect by ME could be noticed. Freezing and thawing did not affect the fractional esterification rate (FER-per cent of total serum unesterified cholesterol esterified per hour) in normolipidaemic sera, whereas in hyperlipidaemic sera, particularly those with high levels of VLDL, FER was stimulated. Esterification partially proceeded during the cold incubation of serum or plasma with 14C-cholesterol ready-to-use discs, attaining the values of about 0.3%/h and 2-6%/h, respectively, in human sera and in rabbit and rat sera. The starting level of esterification did not affect the linearity of LCAT reaction during warm incubation (30 min at 37 degrees C), neither was the absolute value of FER changed as compared with cold labelled sera with those inhibited by DTNB and reactivated by ME. Substantial LCAT activity was also detected in extremely diluted substrates--such as intraocular fluid collected from rabbits with induced uveitis or after preceding paracentesis.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMedDate not supplied

[Effect of ethinyl-estradiol on the biosynthesis and esterification of fatty acids in the rat liver].

Ethynyl-estradiol was shown to decrease the rate of biosynthesis of saturated, mono-, di-, tri- and tetraenic fatty acids in liver tissue and to increase the esterification of the newly synthesized fatty acids into triglycerides and phospholipids. The most distinct activation of esterification was found, if newly synthesized saturated fatty acids changed to triglycerides and tetraenic acids--into phospholipids. Ethynyl-estradiol stimulated also in liver tissue the esterification of exogenous saturated and unsaturated fatty acids into triglycerides and phospholipids, while relative esterification of unsaturated fatty acids into phospholipids tended to increase. The data obtained suggest that stimulation of endo- and exogenous fatty acids esterification into triglycerides and phospholipids of liver tissue may be important in pathogenesis of estrogen-induced hypertriglyceridemia.

Acetyl-CoA Carboxylase↗