Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Cholates”

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

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

At least 775 records · Page 43Linked to original sources
PubMed1979

Inhibition of Soybean Cell Growth by the Adsorption of Rhizobium japonicum.

Soybean cells in suspension culture were inhibited in their growth by mixed culture with Rhizobium japonicum 5033. Rhizobium cells had the ability to adsorb on the surface of soybean cells. Cell envelope prepared from Rhizobium by sonic oscillation inhibited the growth of soybean cells. The growth-inhibiting activity of the cell envelope was depressed by beta-glucosidase, KIO(4), urea, sodium cholate, and Triton X-100, but was stable on heating at 120 C for 15 minutes. Adsorption of the cell envelope on soybean cells was depressed by only beta-glucosidase. The sodium cholate-soluble fraction of the cell envelope had the growth-inhibiting activity. Results in this paper suggest that components of the Rhizobium cell surface cause the inhibition of soybean cell growth after the adsorption of the Rhizobium cell to the soybean cell.

Journal Article↗
PubMed1980

Activation of Glyceraldehyde-Phosphate Dehydrogenase (NADP) and Phosphoribulokinase in Phaseolus vulgaris Leaf Extracts Involves the Dissociation of Oligomers.

Phosphoribulokinase (EC 2.7.1.19, ATP: d-ribulose-5-phosphate-1-phosphotransferase) resembles the NADPH-dependent glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.13, d-glyceraldehyde-3-phosphate: NADPH(+) oxidoreductase [phosphorylating]) of chloroplasts in that the activation of both of these enzymes involves the dissociation of oligomers (apparently tetrameric forms) with low catalytic activity to give protomers which possess higher catalytic activity. Gel filtration on Sepharose 6B has shown that the molecular weights of the oligomer and active protomer of phosphoribulokinase are, respectively, about 6.8 x 10(5) and 1.7 x 10(5), whereas the corresponding values for glyceraldehyde-3-phosphate dehydrogenase are 8.2 x 10(5) and 2.2 x 10(5). Activation of both enzymes occurs in response to either ATP, dithiothreitol, or cholate while the glyceraldehyde-3-phosphate dehydrogenase is also activated by NADPH. Activation/dissociation of these enzymes may involve conformational changes resulting from nucleotide binding, the reduction of sulfur bridges, and the cholate induced loosening of hydrophobic interactions.

Journal Article↗
PubMed1984

Solubilization and partial purification of ATPase from a rose cell plasma membrane fraction.

The K(+)-stimulated ATPase was partially purified from a plasma membrane fraction of suspension cultured cells of rose (Rosa damascena) by two different solubilization procedures. Solubilization with 30 mm octyl-beta-d-glucopyranoside followed by precipitation with ammonium sulfate increased the specific activity of the enzyme about 6-fold. Solubilization with 1% cholate removed all but 1% of the phospholipids and resulted in an almost total loss of ATPase activity. The subsequent addition of polar lipids restored >90% of the ATPase activity with a doubling in specific activity. Fractionation of the cholate-solubilized ATPase activity on a Sephadex G-150 column resulted in 88% of the ATPase activity being recovered in two discrete, approximately equal peaks. Both ATPase activities were similar to plasma membrane ATPase activities in pH optimum, substrate specificity, ion stimulation, and inhibitor sensitivity. Assays of marker enzymes for Golgi apparatus, endoplasmic reticulum, and mitochondria revealed only a low contamination (<7%) from other membranes in the plasma membrane-enriched preparations. Lacking an unequivocal marker for the tonoplast, intact vacuoles were isolated, and their membrane density and ATPase activity were characterized and shown not to correspond to those of the putative plasma membrane preparation. These results suggest that there are two forms of ATPase separable by size in the plasma membrane of rose.

Journal Article↗
PubMed1987

Selective Solubilization of Membrane Proteins Differentially Labeled by p-Chloromercuribenzenesulfonic Acid in the Presence of Sucrose.

Broadbean (Vicia faba L.) leaf discs have been incubated with the slowly permeant thiol reagent [(203)Hg]-para-chloromercuribenzenesulfonic acid (PCMBS) in the presence or in the absence of sucrose, and the release of PCMBS-labeled proteins has been monitored in media containing various concentrations of urea, ethyleneglycol-bis-(beta-aminoethyl ether)-N, N, N', N'-tetraacetic acid (EGTA), sodium cholate, sodium dodecyl sulfate, Triton X-100, octylglucoside or (3-[3-cholamidopropyl)-dimethylammonio] 1-propane-sulfonate) (CHAPS). The proteins differentially labeled by PCMBS in the presence of sucrose which, on the basis of previous results, are assumed to include the sucrose carrier, were preferentially solubilized by 1% CHAPS, 1% octylglucoside, or 1% Triton X-100. Other PCMBS-labeled proteins (;background' proteins) could be partially removed by EGTA, urea, or 0.1% cholate. Sequential treatment by 10 mm EGTA and 1% CHAPS was found to give a fraction highly enriched in the differentially labeled proteins. Analysis of the specific activity of microsomal pellets suggests that the results obtained with leaf discs give a good account of what is occurring at the plasma membrane level. These data, which suggest that the proteins differentially labeled by PCMBS in the presence of sucrose are intrinsic membrane proteins, can be used to solubilize these proteins from microsomal fractions.

Journal Article↗
PubMed1991

Solubilization, partial purification, and reconstitution of the glycolate/glycerate transporter from chloroplast inner envelope membranes.

The glycolate/glycerate transporter of spinach (Spinacia oleracea L.) chloroplast inner envelope membranes was solubilized by treatment of the membranes with sodium cholate. Mixtures of the cholate extracts and soy asolectin were subjected to gel filtration to remove the detergent. The reconstituted vesicles were frozen, thawed, and sonicated in a buffer that contained 10 millimolar d-glycerate and, usually, [(3)H]sucrose as an internal space indicator. The dilution of the vesicles into a medium that contained 0.4 millimolar [(14)C]d-glycerate resulted in a rapid accumulation of labeled glycerate, followed by a much slower loss of [(14)C]d-glycerate from the vesicles. This behavior is characteristic of counterflow. The accumulation of [(14)C]d-glycerate was strongly inhibited by HgCl(2), which blocks glycolate/glycerate transport in intact chloroplasts. In the absence of proton ionophores, the extent of [(14)C]glycolate accumulation under similar conditions was much greater than that of [(14)C]d-glycerate. External glycolate inhibited d-glycerate counterflow and external d-glycerate inhibited glycolate counterflow. The external pH dependence of the efflux of [(14)C]d-glycerate accumulated in vesicles by counterflow and its inhibition by external l-mandelate are characteristics displayed by glycolate transport in intact chloroplasts. Partial purification of the transporter was achieved by glycerol gradient centrifugation. The solubilized glycolate and glycerate counterflow activities, assayed by reconstitution into vesicles, were found to sediment similarly.

Journal Article↗
PubMed1982

Metachromatic leukodystrophy caused by a partial cerebroside sulfatase.

A patient with neuropathy and myopathy since infancy but whose neuropathy had been stable for a number of years showed a profound deficiency of arylsulfatase A in leukocytes and urine. Urine contained material that stained metachromatically and cochromatographed with cerebroside sulfate. In contrast, cultured fibroblasts contained about 10-20% of normal arylsulfatase A with properties identical to properties of normal fibroblast enzyme, except that it showed no cerebroside sulfatase activity. Growing fibroblasts in the cerebroside sulfate loading test had an attenuated rate of sulfatide hydrolysis. A re-examination of the cerebroside sulfatase reaction revealed that while only limited hydrolysis occurred with low concentrations of taurodeoxycholate or cholate (type I activation), significant hydrolysis of the natural substrate did take place with high concentrations of cholate (type II activation). This suggests that there is a partial cerebroside sulfatase defect in this atypical form of metachromatic leukodystrophy.

Adult↗
PubMed1987

Tri(n-butyl) phosphate/detergent treatment of licensed therapeutic and experimental blood derivatives.

Incubation of an AHF concentrate with 0.3% tri(n-butyl)phosphate (TNBP) and 0.2% sodium cholate was shown to inactivate at least 10,000 infectious doses of lipid-enveloped viruses, including hepatitis B and non-A, non-B viruses and HTLV-III [Prince et al., Lancet i, pp. 706-710, 1986]. The use of TNBP/detergent combinations for virus sterilization was evaluated further to determine its effect on the structure and function of a wide variety of blood proteins. Vesicular stomatitis and Sindbis viruses were used as markers of virus inactivation. TNBP/detergent treatment did not significantly alter the function of AHF, factor VII, factor IX, factor X, fibrinogen, factor XIII, fibronectin, anti-HBsAg and anti-HA in normal serum globulin, haptoglobin, tumor necrosis factor, alpha-interferon, and both native and chemically polymerized stroma-free hemoglobin. As compared with partially purified derivatives, the extent of virus sterilization of plasma and component cryoprecipitate with 0.3% TNBP and 0.2% sodium cholate at ambient temperature could be improved by raising the TNBP concentration and temperature. Virus sterilization by TNBP/detergent mixtures appears to be generally applicable to blood protein derivatives.

Antiviral Agents↗
PubMed1975

Interconversion between different states of affinity for acetylcholine of the cholinergic receptor protein from Torpedo marmorata.

In receptor-rich membrane fragments from Torpedo, acetylcholine binds, in the presence of 70 muM Tetram, to a homogeneous population of high-affinity sites with Kd = (3.4 +/- 0.8) x 10(08) M. Dissolution of these membrane fragments by sodium cholate causes a decrease of affinity associated with the appearance of medium-affinity (Kd approximately 10(-7) M) and low-affinity (Kd greater than or equal to 10(-6) M) sites. Dissolution by neutral detergents Triton X-100 or Emulphogene preserves the high affinity of the acetylcholine binding sites. In all the soluble states of the receptor protein, Ca2+ ions and local anaesthetics no longer enhance the affinity for acetylcholine. Elimination of sodium cholate by dilution leads to the reassociation of the receptor protein, the recovery of high-affinity sites and the control by Ca2+ ions and local anaesthetics. Purification by affinity chromatography of the receptor protein in Triton X-100 is accompanied by a conversion of a majority of the acetylcholine sites into their state of low affinity. High-affinity sites can no longer be recovered by detergent dilution from these low-affinity ones.

Acetylcholine↗
PubMed1976

Multiple forms of cytochrome P-450 in rat-liver microsomes. Separation and some properties of different hydroxylases active on free and sulphoconjugated steroids.

Cytochrome P-450 from male and female rate liver microsomes has been solubilized with sodium deoxycholate, precipitated with ammonium sulphate and separated in the presence of deoxycholate into ten different fractions on a DEAE-cellulose column eluted with a stepwise gradient of KCL. Each fraction was characterized with respect to its ability to catalyze different hydroxylation reactions of free and disulphurylated 5alpha-androstane-3alpha,17 beta-diol, using a reconstituted system. All hydroxylases active on 5alpha-androstane-3alpha, 17 beta-diaol (i.e. the 2alpha-, 2beta-, 7alpha-, 7beta-, 12beta-, 15alpha-, 16alpha- and 18-hydroxylases) and 5alpha-androstane-3alpha, 17beta-diol 3,17-disulphate (i.e. the 15beta-hydroxylase) were solubilized with cholate. However, the 2beta- and 18-hydroxylases were partially inactivated when cholate was added to intact microsomes and these were also the only hydroxylase activities that could not be detected in reconstitution experiments with lipid, NADPH-cytochrome P-450 reductase and the cytochrome P-450 fractions recovered after DEAE-cellulose chromatography. Using microsomal preparations from male rat liver it was possible to obtain a partial separation of the 2alpha- and 7alpha-hydroxylases from the 12beta-, 15alpha- and 16 alpha-hydroxylases and also from the 7beta-hydroxylase. With preparations from female rat livers the l5beta was well separated from the 2alpha- and 7alpha-hydroxylases. The specific activities of the partially separated 2alpha-, 7alpha-, 7beta-, 12beta-, 15alpha- and 16alpha-hydroxylases calculated per nmol of cytochrome P-450 was 9--34% of the original activities in sonicated microsomes. There was an absolute requirement of the cytochrome P-450 fractions for all hydroxylase activities except for the 2alpha-hydroxylase activity. The requirement for NADPH-cytochrome P-450 reductase was not absolute for any of the hydroxylase activities and no lipid dependency was observed. Based on their behavior during solubilization and purification, elution pattern of the DEAE-cellulose column and different modes of regulation, the various hydroxylases studied can be divided into different groups. It is suggested that one form of cytochrome P-450 catalyzes the hydroxylation of 5alpha-androstane-3alpha,17beta-diol in the 2beta- and 18-positions, another form the 12beta-, 15alpha- and 16alpha-hydroxylations of the same substrate and a third form the 15beta-hydroxylation of 5alpha-androstane-3alpha,17beta-diol3,17-disulphate. It is concluded that rat liver microsomes contain multiple forms of cytochrome P-450 active on steroid hormones. It is suggested that the specificity of these forms is determined by the nature of the substrate binding site and by the distance between the binding and catalytic sites on the enzyme.

Animals↗
PubMed1978

Characteristics of the active transport of Ca2+ by submitochondrial vesicles.

Inner membrane vesicles have been prepared by cholate treatment of rat liver mitoplasts. The vesicles can actively accumulate Ca2+ in the absence or presence of inorganic phosphate. The uptake is inhibited by ruthenium red and uncouplers of oxidative phosphorylation. Like in intact mitochondria the driving force for the uptake reaction seems to be the negative inside membrane potential generated during the oxidation of substrates. The level of antimycin-A-sensitive reduction of ferricyanide by succinate indicates that the cholate inner membrane vesicles are about 70% right side out. Using cytochrome-c-extracted inner membrane vesicles it can be shown that only those which have the same right-side-out polarity as intact mitochondria can actively accumulate Ca2+.

Animals↗
PubMed1980

Reconstitution of a functional acetylcholine receptor. Conservation of the conformational and allosteric transitions and recovery of the permeability response; role of lipids.

The 'functional' state of the acetylcholine receptor protein has been followed during reconstitution with the fluorescent agonist [1-(5-dimethylaminonaphthalene)-sulfonamidol]-n-hexanoic acid-beta-N-trimetylammonium bromide ethyl ester (Dns-C6-Cho) and rapid-mixing techniques. Under appropriate conditions, a majority of the acetylcholine receptor sites can be recovered in a low-affinity state(s) for Dns-C6-Cho, similar to that found with the native membrane-bound receptor. This state can be slowly interconverted to a high-affinity state after rapid mixing with the agonist, and the non-competitive channel blockers, like the local anesthetics, still regulate this transition in an allosteric manner. Several experimental conditions commonly used for the solubilization of the receptor and for its purification in the presence of sodium cholate result in the failure of reconstitution: the soluble receptor protein is stabilized in a low-affinity state which can no longer be interconverted to a high-affinity state in the presence of agonists or local anesthetics. On the other hand, it is demonstrated that if the concentration of lipids remains elevated in the presence of sodium cholate, a soluble (9-S) low-affinity form of the receptor protein can be obtained which shows most of the characteristic properties of the membrane-bound receptor and in particular the slow interconversion to the high-affinity state and the effect of local anesthetics on this transition; furthermore, in these conditions the soluble protein can be manipulated ad libitum and submitted, for instance, to column filtrations and sucrose gradient centrifugations in the presence of detergent, without losing its characteristic conformational and allosteric transitions. After elimination of the detergent this form yields a reconstituted receptor which presents binding properties identical to those of the native membrane-bound receptor and leads to the formation of vesicles which exhibit carbamylcholine-sensitive ion fluxes. A necessary and sufficient condition for functional reconstitution is therefore the conservation, in the presence of lipids, of the allosteric properties of the receptor protein in its detergent-soluble form.

Acetylcholine↗
PubMed1984

Solubilization and reconstitution of alpha 2-adrenergic receptors from rat and calf brain.

Sodium cholate and digitonin were used to solubilize alpha2-adrenergic receptors from rat and calf brain. Sodium cholate extracted 40-50% of the membrane protein and 25-30% of the binding capacity. Digitonin extracted only 20-30% of the membrane protein and only 10-15% of the binding capacity of the native membranes. Both detergents were removed by dialysis in the presence of phospholipids, and the solubilized protein was precipitated upon addition of poly(ethyleneglycol) and magnesium. In the solubilization/reconstitution process no purification of the alpha2-adrenergic receptor was obtained, most probably due to its inactivation by the solubilization conditions. The reconstituted protein(s) tested for binding properties, using p-[3H]aminoclonidine and/or [3H]clonidine, maintained the pharmacological profile of the native alpha2-adrenergic receptor. The potency order of various alpha2-agonists and alpha2-antagonists as well as their stereoselectivity were identical to those of the native alpha2-receptor. Specific receptor binding decreases in the presence of the guanyl nucleotides GTP or guanosine 5'-[beta, gamma-imido]-triphosphate but not ATP, thus indicating a co-solubilization of GTP regulatory components (stimulatory protein Ns or inhibitory protein Ni or both). Adenylate cyclase activity of the reconstituted preparation is stimulated threefold by sodium fluoride, suggesting the presence of both Ns-protein and the catalytic unit (C) in the reconstituted protein(s).

Adenylyl Cyclases↗
PubMed1989

The identification of lysosomal ganglioside sialidase in human cells.

In this report we present evidence for the existence of a lysosomal ganglioside sialidase. The sialidase activity was solubilized by sonication and stimulated by cholate. The absence of ganglioside sialidase activity in sialidosis patients indicates that lysosomal sialidase is active towards gangliosides and glycoproteins. The plasma membranes were associated with two types of ganglioside sialidase activities, one was enhanced by cholate while the other was partially inhibited by this detergent.

Cell Fractionation↗
PubMed1992

The alpha subunit of the stimulatory guanine-nucleotide-binding regulatory protein forms high-molecular-mass aggregates, concomitant with iloprost-induced desensitization of human platelet adenylyl cyclase.

Prolonged treatment of human platelets with the prostacyclin analog iloprost led to desensitization of the response to various prostaglandin derivatives. However, basal adenylyl cyclase activity and stimulation by agents acting directly via Gs, the stimulatory guanine-nucleotide-binding regulatory protein of adenylyl cyclase, were likewise decreased. Reconstitution of desensitized membranes with purified Gs from turkey erythrocytes indicated no alteration in the catalyst itself. However, the function of Gs (in cholate extracts) appeared to be severely impaired when reconstituted with adenylyl cyclase catalyst. Modification of Gs was also indicated by its altered sedimentation in sucrose density gradients. From Western blots, the alpha subunit of Gs, alpha s, from control platelets sedimented as a 5.6S species, while that from desensitized cells appeared at higher S values (in a polydisperse distribution). Activation by guanosine 5'-[gamma-thio]triphosphate of Gs from control platelets shifted alpha s to 3.5-3.7S, while activation of Gs from desensitized platelets induced such shift only for a minor portion of alpha s. This small fraction alone appeared to be susceptible to ADP-ribosylation by cholera toxin/[32P]NAD. Furthermore, an antibody directed against the C-terminal hexadecapeptide of alpha s precipitated much less alpha s from cholate extracts derived from desensitized platelets. Modification of alpha s during desensitization was also suggested from cross-linking experiments using the homobifunctional agent bismaleimidohexane: alpha s from desensitized platelets formed a single product of 80 kDa, while that from untreated platelets yielded a doublet (100 kDa and 110 kDa).

Adenosine Diphosphate Ribose↗
PubMed1986

Optimisation of conditions for solubilisation of the bovine dopamine D2 receptor.

Solubilisation of the dopamine D2 receptor from a membrane preparation of bovine corpus striatum using cholate and NaCl was independently optimised with regard to cholate (0.2%, wt/vol), NaCl (1.5 M), and membrane protein (4 mg/ml) concentrations. A maximum solubilisation yield of 58% was obtained and receptors were measured using a [3H]spiperone binding assay incorporating a polyethylene glycol precipitation step. Solubilisation was confirmed by ultracentrifugation studies, passage of the receptor through fine-pore filters, increased thermolability, and by retention of the prelabelled receptor on gel filtration. The soluble receptor showed saturability and reversibility of binding. Displacement of [3H]spiperone from the soluble receptor by competing compounds correlated closely with displacement from the membrane-bound receptors. [3H]Spiperone binding was found to be pH-dependent, with maximum binding occurring at pH 7.8. A comparison of solubilisation was made with six other agents both with and without added NaCl and it was concluded that the cholate/NaCl solubilisation system provides an efficient, inexpensive, and reliable method for the preparation of functional bovine dopamine D2 receptors.

Animals↗
PubMed1986

Solubilization and partial purification of a presynaptic membrane protein ensuring calcium-dependent acetylcholine release from proteoliposomes.

In previous work, it was shown that cytoplasmic acetylcholine decreased on stimulation of Torpedo electric organ or synaptosomes in a strictly calcium-dependent manner. This led to the hypothesis that the presynaptic membrane contained an element translocating acetylcholine when activated by calcium. To test this hypothesis, the presynaptic membrane constituents were incorporated into the membranes of liposomes filled with acetylcholine. The proteoliposomes thus obtained released the transmitter in response to a calcium influx. The kinetics and calcium dependency of acetylcholine release were comparable for proteoliposomes and synaptosomes. The presynaptic membrane element ensuring calcium-dependent acetylcholine release is most probably a protein, since it was susceptible to Pronase, but only when the protease had access to the intracellular face of the presynaptic membrane. Postsynaptic membrane fractions contained very low amounts of this protein. It was extracted from the presynaptic membrane under alkaline conditions in the form of a protein-lipid complex of large size and low density which was partially purified. The specificity of the calcium-dependent release for acetylcholine was tested with proteoliposomes filled with equal amounts of acetylcholine and choline or acetylcholine and ATP. In both cases, acetylcholine was released preferentially. After cholate solubilization and gel filtration, the protein ensuring the calcium-dependent acetylcholine release was recovered at a high apparent molecular weight (between 600,000 and 200,000 daltons), its apparent sedimentation coefficient being 17S after cholate elimination. This protein is probably an essential coin of the transmitter release mechanism. We propose to name it mediatophore.

Acetylcholine↗
PubMed1989

Solubilization and characterization of sigma-receptors from guinea pig brain membranes.

The sigma-receptor, a distinct binding site in brain tissue that may mediate some of the psychotomimetic properties of benzomorphan opiates and phencyclidine, has been solubilized using the ionic detergent sodium cholate. Binding assays were performed with the solubilized receptor using vacuum filtration over polyethyleneimine-treated glass fiber filters. The pharmacological specificity of the solubilized binding site for sigma-receptor ligands is nearly identical to the membrane-bound form of the receptor, with the order of potencies for displacement of the selective sigma-ligand [3H]di-o-tolylguanidine ([3H]DTG) closely correlated. The stereoselectivity for (+)-benzomorphan opiate enantiomers was retained by the solubilized receptor. The soluble receptor retained high affinity for binding of [3H]DTG (KD = 28 +/- 0.5 nM) and (+)-[3H]3-(3-hydroxyphenyl)-N-(1-propyl)piperidine [(+)-[3H]3-PPP] (KD = 36 +/- 2 nM). Photoaffinity labeling of the solubilized receptor by [3H]p-azido-DTG, a sigma-selective photoaffinity label, resulted in labeling of a 29-kilodalton polypeptide identical in size to that labeled in intact membranes. Estimation of the Stokes radius of the [3H]DTG binding site was obtained by Sepharose CL-6B chromatography in the presence of 20 mM cholate and calculated to be 8.7 nm. This value was identical to the molecular size found for the binding sites of the sigma-selective ligands (+)-[3H]3-PPP and (+)-[3H]SKF-10,047, supporting the hypothesis that all three ligands bind to the same macromolecular complex.

Affinity Labels↗
PubMed1984

Cholestatic features in focal nodular hyperplasia of the liver.

Twenty specimens of focal nodular hyperplasia were studied with special attention to the histological features of chronic cholestasis (grouped under the headings of cholestasis, cholate-stasis and signs of ductular reabsorption). In all specimens, evidence was found for one or more features of cholestasis and cholate-stasis. Signs of ductular reabsorption were less constant, and apparently varied according to the developmental stage of the lesion. The cholestatic features emphasize the bile secretory capacity of the lesional parenchyma, and are apparently due to the lack of real bile ducts in the portal tract equivalents of the lesional tissue. Evidence is presented that the "ductular component" in FNH is not due to proliferation of pre-existing ductules, but rather derives from ductular metaplasia of liver cell plates in zone 1 equivalents. This metaplastic development of a ductular network may serve the function of reabsorbing the biliary constituents produced by the lesional parenchyma, leading to periductular inflammation and progressive fibrosis, thus producing an equivalent of biliary fibrosis and biliary cirrhosis.

Adult↗