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At least 109 records · Page 6Linked to original sources
PubMed1979

Sodium cholate dissolution of retained biliary stones: mortality rate following intrahepatic infusion.

The reported complication rate from T-tube infusion of sodium cholate for dissolution of retained biliary stones is low. Among 84 patients reported in the English-language literature, and 10 additional cases of our own, there have been no deaths, an incidence of liver enzyme elevation in 7%, fever in 5%, cholangitis in 2%, and pancreatitis in 2%. Recently, we have infused 100mM sodium cholate at 30 cc/hr into patients through transhepatic biliary stents in an effort to rid the intrahepatic biliary tree of retained stones and biliary sludge. Appropriate precautions were taken to prevent increased biliary pressures by the insetion of a 30 cm manometer into the perfusion system. During four transhepatic infusions in three patients, all experienced nausea and vomiting, and two of the three patients developed diarrhea and abdominal pain. Liver enzymes became elevated during all four infusions, and two of the three patients became septic and died shortly after their infusions. Experimental work in animals suggests that intrahepatic sodium cholate infusion results in injury to the ductal epithelium and predisposes patients to bactermia and sepsis. Even though T-tube infusion of sodium cholate into the common bile duct is well tolerated, direct infusion into the intrahepatic biliary tree through a transhepatic tube is not and carries a high risk of sepsis and death.

Abdomen↗
PubMed1982

High resolution nuclear magnetic resonance spectroscopy of bile salts: individual proton assignments for sodium cholate in aqueous solution at 400 MHz.

The 400 MHz 1H-nuclear magnetic resonance spectrum of sodium cholate in dilute aqueous solution has been successfully resolved using a combination of decoupling, partial relaxation, and decoupled partial relaxation techniques. The individual carbon resonances in the 13C-NMR spectrum of sodium cholate have also have assigned. Assignments of individual methylene protons were made by consideration of the molecular structure of sodium cholate and the expected couplings and 1H-nuclear Overhauser enhancement experiments. Verification of the assignments of the methine protons was made by application of single frequency 1H-decoupled 13C-NMR. Variation of pH* from 6.0 to 11.0 did not alter the individual chemical shifts except for those between 2.12 delta and 2.30 delta, originating from the protons on the C23 position adjacent to the ionizable carboxyl group. The chemical shifts of the proton resonances were independent of concentration below 5 mM. Above 10 mM (micellar region), the proton chemical shifts were altered slightly and some band broadening occurred. These data are consistent with the formation of small micellar aggregates (up to N = 4) of cholate molecules.

Bile Acids and Salts↗
PubMed1984

Contribution of trypsin and cholate to the pathogenesis of experimental alkaline reflux esophagitis.

Previous studies suggest that trypsin and bile salts are the causative agents in alkaline reflux esophagitis. However, their individual effects on the esophageal mucosa is relatively weak when used alone. Since these agents seem to have different sites of action in the esophageal mucosa, we have investigated whether they might have a synergic action when used in combination. Rabbit esophagus was perfused in situ with a test solution containing trypsin and cholate, alone or in combination, at pH 7.0. The severity of mucosal damage was assessed, using as indicators of mucosal integrity transmucosal potential difference, net flux of Na+, and mucosal permeability to two neutral molecules of different sizes, 3H-H2O and 14C-erythritol. Cholate (in its conjugated and deconjugated form) was chosen as the bile salt test agent, because it is quantitatively important but almost inert on the esophageal mucosa when used alone. The results indicate that trypsin significantly decreased potential difference and increased mucosal permeability to Na+, 3H-H2O and 14C-erythritol. Cholate and taurocholate had no influence on the mucosa when used alone, but cholate, especially in its deconjugated form, increased significantly mucosal damage caused by trypsin. The findings suggest that trypsin and bile salts do have a synergic effect on esophageal mucosa, which may have pathogenetic significance in clinical alkaline reflux esophagitis.

Animals↗
PubMed1984

Apolipoprotein B: removal of lipids by sodium cholate and reassociation of a lipid-free apoprotein with dipalmitoyl phosphatidylcholine.

Apolipoprotein B (apoB) of human plasma low-density lipoprotein has been solubilized with sodium cholate added in an amount highly above its critical micellar concentration. During isolation by gel exclusion chromatography on Sepharose CL-4B, the apoB forms mixed micelles of protein and detergent that are free of endogenous lipids. The circular dichroic spectra of the sodium cholate-solubilized apoB indicate significant heterogeneity within the fractions obtained by gel chromatography. The peak position fraction of apoB taken from the column was used for reassociation with dipalmitoyl phosphatidylcholine (DPPC). A soluble apoB-DPPC complex has been prepared by incubation of apoB-sodium cholate and DPPC-sodium cholate solutions at 42 degrees C, followed with detergent removal by extensive dialysis in the presence of a XAD-2 ion-exchange resin. Data from negative-stain electron microscopy suggests the incorporation of solubilized apoB into single-bilayer phospholipid vesicles. Upon reassociation with phospholipid, a shift (to shorter wavelengths) occurs in the intrinsic fluorescence of the apoB, thus indicating a transfer of tryptophan residues to a more hydrophobic environment. Sodium dodecylsulfate-polyacrylamide electrophoresis gives a single band (apparent Mr 370,000) for apoB after solubilization, purification and interaction with the phospholipid.

Apolipoproteins B↗
PubMed1982

Micellar complexes of human apolipoprotein A-I with phosphatidylcholines and cholesterol prepared from cholate-lipid dispersions.

Micellar complexes of human apolipoprotein A-I and phosphatidylcholine, with or without cholesterol, were prepared by adding apolipoprotein A-I (apo A-I) to sodium cholate-lipid mixtures. Cholate was removed by dialysis and the apo A-I.lipid complexes were isolated by gel filtration chromatography or by density gradient ultracentrifugation. The lipid mixtures consisted of dipalmitoylphosphatidylcholine or egg yolk phosphatidylcholine in the presence of various molar ratios of cholesterol. The formation of complexes was examined at different phosphatidylcholine (PC)-to-apo A-I ratios, PC-to-cholate ratios, and cholate concentrations. Yields of complexes were maximal when incubation and dialysis were performed near the transition temperature of the PC. Upon lipid binding and complex formation, apo A-I experienced a significant increase in alpha-helix content, and a blue shift in the intrinsic tryptophan fluorescence. In all lipid-protein incubation mixtures, from 600:1 to 75:1, PC/apo A-I (molar ratios), relatively small, stable complexes were present which gave maximum yields at incubation ratios similar to their isolated stoichiometries of 75:1 to 140:1, PC/apo A-I (molar ratios). For the isolated complexes, molecular weights were determined by sedimentation equilibrium to be in the range from 220,000 to 260,000; fluorescence polarization using the hydrophobic probe 1,6-diphenyl-1,3,5-hexatriene showed a broadened and shifted gel to liquid-crystalline phase transition, characteristic of micellar complexes of apo A-I with PC. Complexes prepared using apo A-I, covalently labeled with 5-dimethylaminonaphthalene-1-sulfonyl chloride, had an overall particle rotational relaxation time of 530 ns. On electron micrographs, the complexes, negatively stained with phosphotungstate, appeared as lamellar, discoidal particles.

Apolipoprotein A-I↗
PubMed1981

Stabilization of acetylcholine receptor channels by lipids in cholate solution and during reconstitution in vesicles.

Acetylcholine receptors were solubilized from electric organ membranes of Torpedo californica in mixed micelles of sodium cholate and soybean lipids. Sodium cholate, when supplemented with relatively low amounts of soybean lipids (cholate:lipid, 20:1, molar ratio), was effective in solubilizing receptors without denaturing their agonist-regulated cation channels. Another dialyzable detergent, octylglucoside, denatured the ion channel even in the presence of excess lipids. Reassembly of receptors and lipids into vesicles was achieved by cholate dialysis. About 70% of the receptors were oriented with their toxin binding sites on the external surface of the vesicles. Evidence suggests that all of the receptors in a single vesicle were oriented either right side out or inside out. During the reassembly process about 10-fold greater lipid concentrations were required for the preservation of channel function. At lipid/protein ratios greater than 16:1 (w/w), receptors reassembled into vesicles at a constant protein/lipid ratio. These vesicles contained approximately 7% receptors by weight, 5-fold less than the native membrane. The remainder of the lipid assembled into small vesicles which did not contain receptors. At lipid/protein ratios less than 16:1 (w/w), receptors reassociated with lipids in higher weight ratios. Irreversible inactivation of a fraction of the acetylcholine receptor channels occurred in proportion to the greater packing density. This channel denaturation was accompanied by a lowered susceptibility of the disulfide bond between the delta subunits of the acetylcholine receptor dimer to reducing agents. Toxin binding and the orientation of the receptors in the reconstituted vesicles was not affected by reduced lipid/protein ratios. The unexpected constant acetylcholine receptor/lipid ratio in the reconstituted vesicles and the unexpected uniform orientation of the acetylcholine receptors within a vesicle are discussed in terms of the interactions occurring during the initial nucleation events of the reassembly process.

Acetylcholine↗
PubMed2004

Enhancement of apparent substrate selectivity of proteinase K encapsulated in liposomes through a cholate-induced alteration of the bilayer permeability.

Proteinase K-containing liposomes with highly selective membrane permeability properties were prepared. The selectivity obtained was with respect to the two substrate molecules added to the external aqueous phase of the liposomes: acetyl-L-Ala-Ala-Ala-p-nitroanilide (Ac-AAA-pNA) and succinyl-L-Ala-Ala-Ala-p-nitroanilide (Suc-AAA-pNA). The liposome-forming lipid used was POPC (1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine) and modulation of the membrane permeability was achieved using the detergent cholate. Proteinase K-containing mixed liposomes (PKCL) were prepared by adding cholate to preformed proteinase K-containing POPC liposomes (PKL) at a defined effective cholate/POPC molar ratio in the liposomal bilayer membrane R(e). Proteinase K was kept inside PKCL with a negligible amount of leakage into the bulk aqueous phase at R(e) < or = 0.30. At higher R(e), leakage of proteinase K was pronounced, even under conditions where POPC/cholate mixed liposomes seemed to be still intact (0.30 < R(e) < or = 0.39). At R(e) < or = 0.30, the reactivity of proteinase K in the PKCL measured with the externally added substrate Ac-AAA-pNA increased with increasing R(e), while the reactivity measured with Suc-AAA-pNA remained low, regardless of the R(e) value. This showed that externally added Ac-AAA-pNA molecules permeated the liposomal membrane more easily than Suc-AAA-pNA by modulating the membrane with cholate. Consequently, Ac-AAA-pNA was hydrolyzed in PKCL with considerably higher apparent substrate selectivity in comparison with the cases of proteinase K in PKL and free proteinase K (without liposomal encapsulation). The results obtained clearly demonstrate that the prepared PKCL can be utilized as a kind of nano-scaled bioreactor system which can take up a particular target substrate with high apparent substrate selectively from the external phase of the liposomes. Inside the liposomes, the target substrate is then converted into the corresponding products.

Cholates↗
PubMed2003

Simultaneous determination of 16 estrogens, dehydroepiandrosterone and their glucuronide and sulfate conjugates in serum using sodium cholate micelle capillary electrophoresis.

The simultaneous determination of 16 estrogens, dehydroepiandrosterone (DHEA) and their glucuronide and sulfate conjugates by micellar electrokinetic chromatography (MEKC) with sodium cholate micelle is reported. Sodium cholate, sodium dodecylsulfate (SDS) and alpha-, beta-, gamma-cyclodextrins were studied as micelle reagents in the pH range of 7.0-10.0. Estrogens, DHEA and their glucuronide and sulfate conjugates were separated using a 50 cm x 50 microm capillary with 10 mM borate-phosphate buffer (pH 8.0) containing 50 mM sodium cholate as carrier. The method could simultaneously determine 1.0-1000 microg/mL of steroids and metabolites in 100 microL of serum by photometric detection at 214 nm within 14 min and 80 ng/mL steroids could be determined by using 2.0 mL of serum. The relative standards deviations were 6.7-7.7% at 10 microg/mL in serum. The recoveries were 89.1-92.0% with 10 microg/mL serum samples.

Adult↗
PubMed2000

Stability of SUV liposomes in the presence of cholate salts and pancreatic lipases: effect of lipid composition.

The effect of bile salts (sodium cholate and sodium taurocholate), and pancreatic lipases on the structural integrity of SUV liposomes of different lipid compositions was studied. Liposomal membrane integrity was judged by bile salt or pancreatin-induced release of vesicle encapsulated 5,6-carboxyfluorescein, and vesicle size distribution before and after incubations. Bile salt concentration was 10 mM, while a saturated solution of pancreatin (mixed with equal volume of liposomes) was utilized. Results agree with earlier studies, demonstrating the instability of liposomes composed of lipids with low transition temperatures (PC and DMPC) in presence of cholates. Addition of cholesterol (1:1 lipid:chol molar ratio) does not substantially increase the encapsulated molecule retention. Nevertheless, liposomes composed of lipids with high transition temperatures (DPPC, DSPC and SM), retain significantly higher amounts of encapsulated material, under all conditions studied. Furthermore, the vesicles formed by mixing cholesterol with these lipids will possibly be sufficiently stable in the gastrointestinal tract for long periods of time. Sizing results reveal that in most cases release of encapsulated molecules is mainly caused by their leakage through holes formed on the lipid bilayer. However, in stearylamine containing DPPC and DSPC vesicles, the cholate-induced drastic decrease in vesicle size suggests total liposome disruption as the possible mechanism of encapsulated material immediate release.

Animals↗
PubMed2007

Preferential solvation within hydrophilic nanocavities and its effect on the folding of cholate foldamers.

The conformations of three cholate foldamers and one molecular basket were studied by fluorescence and NMR spectroscopy. In nonpolar solvents (e.g., hexane/ethyl acetate or ethyl acetate) mixed with a small amount of a polar solvent (e.g., alcohol or DMSO), the cholate oligomer folded into a helix with the hydrophilic faces of the cholates turned inward. Folding created a hydrophilic nanocavity preferentially solvated by the entrapped polar solvent concentrated from the bulk. This microphase separation of the polar solvent was critical to the folding process. Folding was favored by larger-sized polar solvent molecules, as fewer such molecules could occupy and solvate the nanocavity, thus requiring a smaller extent of phase separation during folding. Folding was also favored by smaller/acyclic nonpolar solvent molecules, probably because they could avoid contact with the OH/NH groups within the nanocavity better than larger/cyclic nonpolar solvent molecules.

Cholates↗
PubMed2002

Cholate feeding counteracts calcium-induced depression of apparent fat digestibility in rats.

This study tested the hypothesis that cholate feeding would counteract the earlier described calcium-induced inhibition of fat digestion. Rats were fed semipurified diets; either low (0.25%, w/w) or high (1.0%) in calcium, the latter diets being without or with 0.5% added sodium cholate. Apparent fat digestibility was 95.6% of intake in the rats fed the low-calcium diet. Calcium feeding significantly lowered apparent fat digestibility to 82.6%, but in the presence of cholate it was 91.2%. It is concluded that the inhibitory effect of calcium on fat digestion is mediated by diminishing the availability of bile acids.

Animals↗
PubMed2003

Involvement of cysteine proteinases in excystment of Paragonimus ohirai metacercariae induced by sodium cholate and A23187.

The involvement of intrinsic proteinases in the excystment of Paragonimus ohirai metacercariae was studied in in vitro excystment induced by sodium (Na) cholate, a bile salt and A23187, a Ca2+ ionophore. The effects of various proteinase inhibitors on the in vitro excystment were examined and similar inhibitory profiles were obtained. Benzyloxycarbonyl-L-leucyl-L-leucinal (Z-Leu-Leu-H), a cysteine proteinase inhibitor and 4-(2-aminoethyl)-benzenesulfonyl fluoride (Pefabloc SC), a serine proteinase inhibitor completely inhibited excystment, while L-3-carboxy-2,3-trans-epoxypropionyl-leucylamido (4-guanidino)-butane (E-64), a cysteine proteinase inhibitor and leupeptin, a cysteine/serine proteinase inhibitor permitted partial excystment at a lower rate, but inhibited it from proceeding from the partial excystment stage. In secretions released from metacercariae during excystment, proteinase activities detected towards various fluorogenic peptidyl substrates were almost completely inhibited by Z-Leu-Leu-H and E-64, but not by Pefabloc SC. Sodium cholate induced a higher secretion of cysteine proteinases and a higher rate of excystment than A23187. Profiles of cysteine proteinase activities towards five peptidyl substrates detected were markedly different among the two secretions and the lysate of newly excysted juveniles. Newly excysted juveniles released cysteine proteinases with similar activity profiles and levels to metacercariae induced by Na cholate-incubation, whereas the release of cysteine proteinases was reduced compared with metacercariae induced by A23187-incubation. These results provide valuable information about the involvement of intrinsic proteinases in metacercarial excystment.

Animals↗
PubMed1999

mrp, a multigene, multifunctional locus in Bacillus subtilis with roles in resistance to cholate and to Na+ and in pH homeostasis.

A 5.9-kb region of the Bacillus subtilis chromosome is transcribed as a single transcript that is predicted to encode seven membrane-spanning proteins. Homologues of the first gene of this operon, for which the designation mrp (multiple resistance and pH adaptation) is proposed here, have been suggested to encode an Na+/H+ antiporter or a K+/H+ antiporter. In the present studies of the B. subtilis mrp operon, both polar and nonpolar mutations in mrpA were generated. Growth of these mutants was completely inhibited by concentrations of added Na+ as low as 0.3 M at pH 7.0 and 0.03 M at pH 8.3; there was no comparable inhibition by added K+. A null mutant that was constructed by full replacement of the mrp operon was even more Na+ sensitive. A double mutant with mutations in both mrpA and the multifunctional antiporter-encoding tetA(L) gene was no more sensitive than the mrpA mutants to Na+, consistent with a major role for mrpA in Na+ resistance. Expression of mrpA from an inducible promoter, upon insertion into the amyE locus, restored significant Na+ resistance in both the polar and nonpolar mrpA mutants but did not restore resistance in the null mutant. The mrpA disruption also resulted in an impairment of cytoplasmic pH regulation upon a sudden shift in external pH from 7.5 to 8.5 in the presence of Na+ and, to some extent, K+ in the range from 10 to 25 mM. By contrast, the mrpA tetA(L) double mutant, like the tetA(L) single mutant, completely lost its capacity for both Na+- and K+-dependent cytoplasmic pH regulation upon this kind of shift at cation concentrations ranging from 10 to 100 mM; thus, tetA(L) has a more pronounced involvement than mrpA in pH regulation. Measurements of Na+ efflux from the wild-type strain, the nonpolar mrpA mutant, and the complemented mutant indicated that inducible expression of mrpA increased the rate of protonophore- and cyanide-sensitive Na+ efflux over that in the wild-type in cells preloaded with 5 mM Na+. The mrpA and null mutants showed no such efflux in that concentration range. This is consistent with MrpA encoding a secondary, proton motive force-energized Na+/H+ antiporter. Studies of a polar mutant that leads to loss of mrpFG and its complementation in trans by mrpF or mrpFG support a role for MrpF as an efflux system for Na+ and cholate. Part of the Na+ efflux capacity of the whole mrp operon products is attributable to mrpF. Neither mrpF nor mrpFG expression in trans enhanced the cholate or Na+ resistance of the null mutant. Thus, one or more other mrp gene products must be present, but not at stoichiometric levels, for stability, assembly, or function of both MrpF and MrpA expressed in trans. Also, phenotypic differences among the mrp mutants suggest that functions in addition to Na+ and cholate resistance and pH homeostasis will be found among the remaining mrp genes.

Antiporters↗
PubMed2001

[Study on calcium-cholate-phosphate ternary complexes by FTIR spectroscopy].

The aim of this paper was to examine the calcium-cholate-phosphate tenary complexes by FTIR spectroscopy. The results indicated that the mole ratio of cholate to phosphate were 1:3 and 1:4 in ternary complexes respectively when the initial mole ratio of cholate to phosphate were 3:1 and 1.5:1 in reaction. The FTIR spectroscopic results demonstrated that in the ternary complexes Ca2+ was coordinated with O in both COO- and PO(4)3- groups.

Calcium↗
PubMed1979

Cholate sodium infusion for retained common bile duct stones.

Eight patients with stones retained in the extrahepatic biliary tract underwent cholate sodium infusion for dissolution of the stones. In six patients, the stones disappeared. However, in two of the patients, the stones did not disappear, and they were removed with the ureteral basket. Infusion of cholate sodium was well tolerated by six patients, but was accompanied by nausea, vomiting, and abdominal pain in two patients. In one case, mucosal deformity of the common bile duct was noticed during the infusion, but it was not apparent on a subsequent cholangiogram. As a result of our experience, we conclude that cholate sodium infusion is a safe procedure for the attempted dissolution of retained common bile duct stones.

Adult↗
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↗
PubMed1976

Biliary reabsorption of cholate sodium, glycocholate sodium, and taurocholate sodium from the rat biliary tree after retrograde intrabiliary injection.

The results demonstrate the biliary reabsorption of 14C-cholate, 14C-glycocholate, and 14C-taurocholate from the rat biliary tree after retrograde intrabiliary injection. It could be shown that retrograde injection of these bile salts (20 nmol) in a total volume of 40 mul leads to significantly increased biliary reabsorption in contrast to the administration in a retrograde volume of only 20 mul. These differences in reabsorption may be explained by greater reabsorption at a more proximal site in the biliary tree. Furthermore 14C-glycocholate and 14C-taurocholate are reabsorbed to a lesser extent in contrast to 14C-cholate when bile flow was restarted at once after retrograde injection in a volume of 40 mul. It is speculated that conjugation of cholate to glycine and taurine has some effect on the extent of biliary reabsorption of this bile acid. Following the results presented in this paper one might hypothize that biliary reabsorption has an important influence on bile composition i.e. the biliary excretion of bile salts.

Animals↗
PubMed1977

Effects of different bile salts upon the composition and morphology of a liver plasma membrane preparation. Deoxycholate is more membrane damaging than cholate and its conjugates.

1. Rat liver plasma membrane preparations were incubated with various bile salts at 0 or 37 degrees C. the bile salts caused the removal of various amounts of proteins, membrane enzymes and phospholipids; the extent and nature of these losses, and the morphological changes which accompanied them, varied with the detergent used. 2. Cholate, taurocholate and glycocholate removed appreciable amounts of protein from the saline-washed membranes, and considerable amounts of both phospholipids and the membrane enzymes, 5-nucleotidase, alkaline phosphatase, alkaline phosphodiesterase 1 and L-leucyl-beta-naphtylamidase. These losses were greater at 37 that at 0 degrees C. The material remaining contained membrane-like profiles, many of vesicular form, even when the preparation was almost completely devoid of phospholipids. 3. Deoxycholate, both at 0 and 37 degrees C, removed more protein, membrane enzymes and phospholipids than did cholate and its conjugates. The material remaining was mainly granular and unorganised and the only remaining features were structures resembling the nexus, and occasional desmosomes. 4. Deoxycholate, a dihydroxy bile salt, therefore appears to cause greater perturbation of membrane structure than the trihydroxy bile salt, cholate, and its conjugates. The results may have implications for the effects of bile salts upon the membranes of liver cells during bile salt secretion and the production of bile.

Animals↗