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PubMed2005

Mild hepatic fibrosis in cholesterol and sodium cholate diet-fed rats.

To date, the majority of research on hypercholesterolemia has focused on the effects of a high cholesterol diet on atherosclerosis and coronary heart disease. The toxic effects of cholesterol on the liver and the relationship between the intake of a high cholesterol diet and hepatic fibrosis, however, have not been investigated clearly or histopathologically. Male Wistar rats were fed a diet supplemented with 1.0% cholesterol and 0.3% sodium cholate for 12 weeks. Rats were sacrificed and analyzed via blood biochemistry, traditional microscopy and immunohistochemistry. Following the feeding of this diet, the rates of aspartate aminotransferase, alanine aminotransferase, lactate dehydrogenase and total cholesterol in the rats were elevated consistently from week 3 and throughout the remainder of the experiment. From microscopic observation, hepatic necrosis, macrophage infiltration and steatosis increased markedly throughout the experiment. Hepatic fibrosis and myofibroblast proliferation were detected at weeks 9 and 12. Mast cell appearance was proportional to the degree of hepatic damage. These findings suggest that hepatic fibrosis is inducible by a high cholesterol diet and is likely the result of the interaction between several different cell types (i.e., macrophages, myofibroblasts, and mast cells) in an inflammatory milieu. Hypercholesterolemia should be considered as a risk factor for hepatic fibrosis as well as atherosclerosis and coronary artery disease.

Alanine Transaminase↗
PubMed1996

Optimization of selectivity and resolution in micellar electrokinetic capillary chromatography with a mixed micellar system of sodium dodecyl sulfate and sodium cholate.

Selectivity and resolution were studied for the separation of seven corticosteroids by micellar electrokinetic capillary chromatography (MEKC) using a mixed micellar solution of sodium dodecyl sulfate (SDS) and sodium cholate (SC), buffered with 3-(N-morpholino)propanesulfonic acid (MOPS) or 3-[(1,1-dimethyl-2-hydroxyethyl)amino]-2-hydroxypropane sulfonic acid (AMPSO). The changes in selectivity were compared for the AMPSO-SDS-SC system by varying the pH and the concentrations of AMPSO, SDS and SC. The experimental design started with the central composite design and continued in a sequential manner. The optimum selectivity for the separation of the corticosteroids was calculated from the analyte migration times and the analyte velocities, by using empirical quadratic regression models. Satisfactory regression fits and coefficients of determination for prediction were obtained with cross-validated models. To optimize the resolution, the physical parameters of capillary length and analysis time were varied under the conditions optimal for the selectivity. In both the selectivity and the resolution, optimization the overall optimum was determined by using the desirability function technique. Analysis times were controlled by using 1,3-diaminopropane to influence the electroosmotic flow velocity (veo). The voltage was kept constant, which resulted in higher electric field strength in shorter capillaries. No changes in the selectivity were observed when 1,3-diaminopropane was used to control the electroosmotic flow velocity. Such an optimization technique, where the chemical and physical factors affecting the separation are treated independently, seemed to be effective for finding the best possible resolution for the corticosteroids.

Adrenal Cortex Hormones↗
PubMed1988

Characterization of complexes of egg yolk phosphatidylcholine and apolipoprotein A-II prepared in the absence and presence of sodium cholate.

Complexes of apolipoprotein A-II and egg yolk phosphatidylcholine were prepared in mixtures of different composition in the absence and presence of sodium cholate. By gradient gel electrophoresis, complex preparations were polydisperse and particle size distributions were influenced by the composition of the reconstitution mixture. Complexes generally exhibited a discoidal morphology by electron microscopy, but showed increased formation of vesicular complexes at elevated levels of egg yolk PC in the mixtures. By chemical crosslinking, complexes formed in the absence of cholate were shown to consist primarily of discoidal species with three apolipoprotein A-II molecules per particle in the mixtures investigated; complexes formed in the presence of cholate included species ranging from three to five apolipoprotein A-II per particle. The number of apolipoprotein A-II per particle and the sizes of the complexes, prepared in cholate, increased with increase of egg yolk PC in the reconstitution mixture. Relative to the particle size distribution of discoidal complexes formed in the absence of cholate, those prepared in cholate showed a distribution shifted to larger particle sizes. Complexes of similar particle size distribution formed in the presence or absence of cholate showed similar physical-chemical properties. Discoidal complexes with the same number of apolipoprotein A-II per particle but of different size and composition were observed, suggesting the possibility of some conformational adaptation of apolipoprotein A-II leading to stabilization of egg yolk PC bilayers of different diameter. Properties of particle size distributions of discoidal complexes prepared in cholate of apolipoprotein A-II and egg yolk PC were compared with those of complexes of apolipoprotein A-I previously reported (Nichols, A.V., Gong, E.L., Blanche, P.J. and Forte, T.M. (1983) Biochim. Biophys. Acta 750, 353-364).

Apolipoprotein A-II↗
PubMed1974

The treatment of retained stones in the common bile duct with sodium cholate infusion.

Six patients with stones retained in the common bile duct after cholecystectomy and common duct exploration were treated by intraductal infusion of a sodium cholate solution. In the five patients whose stones were between the T-tube and the duodenum the treatment was successful within a few days. A stone became transiently impacted in the ampullary region soon after beginning therapy in three patients and produced mild pancreatitis in two. The only failure was in a patient whose stone was between the T-tube and the liver.

Adult↗
PubMed1974

Alteration of the kinetics of thrombin-catalyzed hydrolysis of amino acid ester substrates by sodium cholate and other steroids.

Thrombin-catalyzed hydrolysis of TAME proceeds by an initial zero-order phase which later falls off into an apparent first order reaction as substrate becomes limiting. Optimum amounts of sodium cholate not only accelerated TAME hydrolysis but also altered its kinetics to apparent zero-order to complete substrate hydrolysis. As this implies, the rate of hydrolysis in the presence of cholate was found to be independent of substrate concentration, provided concentrations TAME and cholate were low enough to prevent precipitation of some TAME-cholate as an insoluble complex. The formation of a soluble complex composed of polymeric molecules of TAME and cholate may explain both the acceleration and the change in reaction order. Although the pH and temperature optima for TAME hydrolysis by thrombin rising pH and temperature on the ascending protion of the curves. This is believed to be due to the greater solubility of the TAME-cholate complex. The effects of cholate on thrombin-catalyzed hydrolysis of other arginine esters as well as esters of lysine, histidine and phenylalanine were also studied. Solutions of sodium desoxycholate and androsterone-3-sulfate accelerated TAME hydrolysis as did supensions of testosterone, etiocholanolone, androsterone, androsterone-3-hemisuccinate and pregnandiol-3-glucuronidate. However, isoandrosterone, progesterone, pregnandiol, estradiol, estrone, estriol, estrone-3-sulfate, cholesterol, corticosterone, hydrocortisone and hydrocortisone-3-phosphate had no significant effect on TAME hydrolysis by thrombin. The ability of the andorogenic hormones to accelerate hydrolysis appeared to depend to some extent on the configuration of the substituent group at C3 and the hydrogen at C5. Androsterone-3-hemisuccinate was, like cholate, able to accelerate the hydrolysis of TAME at apparent zero-order kinetics to complete substrate hydrolysis.

Adrenal Cortex Hormones↗
PubMed1977

Treatment of retained bile duct calculi with T-tube infusion of sodium cholate and heparin.

A series of 26 patients with retained radiolucent bile duct calculi diagnosed at postoperative cholangiagrophy through the T-tube is presented. All patients were treated with infusion of 15-20 g sodium cholate in 1000 ml saline and 20,000 units of heparin in 1000 ml saline per 24 hours. In 19 of 26 patients (73 per cent) the calculi disappeared. No complications were encountered. This treatment is recommended prior to reoperation in all patients with retained radiolucent bile duct calculi diagnosed by postoperative cholangiography through the T-tube.

Adult↗
PubMed1997

Determination of serum corticosteroids by mixed micellar electrokinetic capillary chromatography with sodium dodecyl sulfate and sodium cholate.

The application of mixed micellar electrokinetic capillary electrochromatography to the determination of the corticosteroid hormones cortisone, cortisol (hydrocortisone), and dexamethasone in serum samples is demonstrated. The serum samples were enzymatically hydrolyzed, precipitated, solid-phase extracted, and analyzed by capillary electrophoresis. A micellar system of sodium dodecyl sulfate and sodium cholate buffered with an organic compound provided the electrolyte solution. Spiked blank serum samples were used for the linearity testing and limits of detection and quantitation were measured. Patient samples were analyzed and the concentrations of cortisol and cortisone were measured. The method, which was fast and easy to perform, was confirmed to be useful for the determination of corticosteroids in serum.

Adrenal Cortex Hormones↗
PubMed1983

Pancreatic porcine phospholipase A2 catalyzed hydrolysis of phosphatidylcholine in lecithin-bile salt mixed micelles: kinetic studies in a lecithin-sodium cholate system.

Pancreatic porcine phospholipase A2 catalyzed hydrolysis of phosphatidylcholine in bile salt lecithin mixed micelles has been studied, utilizing a series of assay mixtures for which the micellar size, weight, and composition had been experimentally determined. Under these conditions the enzymatic hydrolysis is dependent on the phosphatidylcholine-to-sodium cholate molar ratio within the mixed micelle rather than the bulk concentration of the phospholipid in the mixture: at 5 mM phosphatidylcholine, variation of the NPC/NNaCh ratio from 0.2 to 2.0 increases the enzymatic activity from 82 to 933 mumol/min/mg protein. The initial rates are linear throughout the entire series of assay mixtures, the activity vs micellar concentration curves exhibit saturation behavior, and treatment of the data according to the "surface-as-cofactor" theory provides linear double-reciprocal plots which intersect in one point. The assay system should be applicable for detailed kinetic studies of lipolytic enzymes, including mammalian phospholipases which exhibit rather low activities toward lecithin-Triton X-100 mixed micelles. The system should also provide a convenient basis for mechanistic studies involving the use of inhibitory phospholipid substrate analogs.

Animals↗
PubMed2003

Probing the binding dynamics to sodium cholate aggregates using naphthalene derivatives as guests.

The binding dynamics with bile salt aggregates for a series of naphthalene derivatives of different polarities was studied using fluorescence and laser flash photolysis. Fluorescence was employed to determine the nature of the binding site for each guest and the accessibility of the bound guest to quenchers. Laser flash photolysis was employed to study the mobility of the triplet states of the naphthalenes between the sodium cholate aggregates and the aqueous phase. Primary aggregates, which provide an environment protected from quenchers in the aqueous phase, bind 1- and 2-ethylnaphthalene as guests. The complexation dynamics with this type of aggregate is slow. 1- and 2-Naphthyl-1-ethanol, and 1- and 2-acetonaphthone bind to the secondary aggregates, which provide moderate protection from quenching and faster binding dynamics. The addition of salts lowered the cholate concentration at which primary aggregates were formed, but did not influence the formation of secondary aggregates.

Journal Article↗
PubMedDate not supplied

Effect of sodium cholate on the NADPH cytochrome P-450 reductase activity in the reconstituted rabbit pulmonary mixed-function oxidase system.

Solubilization, separation and purification procedures for rabbit pulmonary mixed-function oxidase (MFO) system have been shown to influence the NADPH cytochrome P-450 reductase component activity in the reconstituted system. The reductase activity as judged by cytochrome c reduction does not correlate with the reductase ability to interact with other MFO system components. Sodium cholate used in several solubilization and purification procedures may alter the reconstituted drug metabolizing activity.

Animals↗
PubMed1996

Effect of water-soluble polymers on the state of aggregation, vesicle size, and phase transformations in mixtures of phosphatidylcholine and sodium cholate.

The state of aggregation and the steady-state size of mixed aggregates made of phospholipids and surfactants are both determined by the surfactant/lipid ratio in the mixed aggregates (Re). Water-soluble polymers, such as dextrans and polyethylene glycols (PEGs) of different molecular weights, induce reversible aggregation of phospholipid vesicles, mostly due to dehydration of the vesicle surface and depletion forces, and only at much higher concentrations, PEGs (but not dextran) also induce irreversible size growth of the vesicles. Here we show that the water-soluble polymers dextrans and PEGs do not affect the vesicle-micelle phase boundaries in mixtures of phosphatidylcholine and the anionic surfactant sodium cholate. By contrast, these polymers affect markedly the steady-state size of cholate-containing vesicles. As compared with pure phosphatidylcholine vesicles, the cholate-containing vesicles have a lower tendency to undergo polymer-induced aggregation, probably due to the electrostatic repulsion between the negatively charged vesicles, but a higher tendency to undergo irreversible size growth at relatively low polymer concentrations. Such irreversible size growth was observed not only for PEG but also for dextran, which in the absence of cholate is incapable of inducing vesicle size growth. These findings are consistent with the prevailing concept that the polymer-induced size growth is due to the effect of large structural fluctuations in the bilayers of deformed aggregated vesicles, the surface of which is dehydrated by the polymer. The presence of cholate in the bilayers at sufficiently high concentrations induces such fluctuations, yielding irreversible size growth within the clusters of dehydrated vesicles formed upon mixing with polymers.

Cholic Acid↗
PubMed1985

Quantitative assays for evaluation of HTLV-III inactivation procedures: tri(N-butyl)phosphate:sodium cholate and beta-propiolactone.

Human T-lymphotropic retrovirus type III (HTLV-III) can be quantitatively assayed for infectivity by inoculation of serial dilutions into cultures of the H-9 cell line and testing for reverse transcriptase in the culture supernatants. Sequential harvests revealed that 14 days of incubation of cultures fed twice weekly was sufficient to reveal maximal titers. Stocks prepared from unconcentrated H9:HTLV-IIIb supernatants have contained from 10(4.5) to 10(6.0) (TCID50)/ml. Stocks prepared by 100-fold concentration of such fluids by pelleting or by polyethylene glycol precipitation followed by pelleting onto sucrose cushions contained 10(6.0)-10(6.5) TCID50/ml. Preliminary studies are under way to utilize this system for evaluation of sterilization processes which can be applied to blood derivatives. Exposure of HTLV-III suspended in Factor VIII preparations to 0.3% tri(n-butyl)phosphate-0.2% sodium cholate resulted in inactivation of greater than or equal to 10(4.5) TCID50 in 2.5 h at 27 degrees C. Exposure of HTLV-III suspended in 4 g of gamma-globulin per 100 ml to 0.14% beta-propiolactone for 4 h at room temperature at pH 8.0 inactivated greater than or equal to 10(4.5) TCID50. However, exposure to gamma-globulin alone inactivated about 99% of HTLV-III infectivity.

Cell Line↗
PubMed1999

Phase Behavior and Aggregate Structure in Aqueous Mixtures of Sodium Cholate and Glycerol Monooleate.

The phase behavior of the glycerol monooleate (GMO)-sodium cholate-water (or 0.9 wt% NaCl) system has been examined in the solvent-rich part, using small-angle X-ray scattering and conventional methods. Addition of cholate up to 7% of the total amphiphile swells the cubic phase of the binary GMO-water system so that it takes up almost 70% of water in the salt-free case and 55% in salt. With more bile salt the lamellar phase also appears highly swollen (up to 85% in water, 75% in brine). In the salt solution a small isotropic L3-phase region replaces the lamellar phase at a solvent content of about 79%. The lamellar phase can accept only about 0.2 cholate molecule per GMO, in both water and brine, and a phase with globular micelles (L1) follows and dominates the diagram. No threadlike micelles appear in this system. Investigation of the particle structures with cryo-transmission electron microscopy (TEM) in dilute systems (99% solvent) show globular micelles and coexisting vesicles and globular micelles. In the presence of salt, dilution of the L3 phase results in dispersed globular particles with an irregular internal morphology that suggests they are a dispersed L3 phase. These particles coexist with faceted particles having an inner structure giving a hexagonal pattern in projection, suggested to derive from the cubic phase. The cubic phase in the salt-free systems did not give dispersions stable enough for cryo-TEM examination. Copyright 1999 Academic Press.

Journal Article↗