ASSOCIATION OF CANALICULAR MEMBRANE ENZYMES WITH BILE-ACID MICELLES AND LIPID AGGREGATES IN HUMAN AND RAT BILE

Simple item page
dc.contributor.authorACCATINO, L
dc.contributor.authorPIZARRO, M
dc.contributor.authorSOLIS, N
dc.contributor.authorKOENIG, CS
dc.date.accessioned2024-01-10T13:46:09Z
dc.date.available2024-01-10T13:46:09Z
dc.date.issued1995
dc.description.abstractThis study was undertaken to gain insights into the characteristics of the polymolecular association between canalicular membrane enzymes, bile acids, cholesterol and phospholipids in bile and into the cellular mechanisms whereby the enzymes are secreted into bile. With this purpose, we studied the distribution of bile acids, cholesterol, phospholipids, proteins and representative canalicular membrane enzymes (alkaline phosphatase, 5'-nucleotidase and gamma-glutamyl transpeptidase), which can be considered specific marker constituents, in bile fractions enriched in phospholipid-cholesterol lamellar structures (multilamellar and unilamellar vesicles) and bile acid-mixed micelles. These fractions were isolated by ultracentrifugation from human hepatic bile, normal rat bile and bile of rats treated with diosgenin, a steroid that induces a marked increase in biliary cholesterol secretion, and were characterized by density, lipid composition and transmission electron microscopy. These studies demonstrate that alkaline phosphatase, T-nucleotidase and gamma-glutamyl transpeptidase are secreted into both human and rat bile where they are preferentially associated with bile acid-mixed micelles, suggesting a role for bile acids in both release of these enzymes and lipids from the canalicular membrane and solubilization in bile. In addition, heterogeneous association of these enzymes with nonmicellar, lamellar structures in human and rat bile is consistent with the hypothesis that processes independent of the detergent effects of bile acids might also result in the release of specific intrinsic membrane proteins into bile.
dc.format.extent10 páginas
dc.fuente.origenWOS
dc.identifier.doi10.1016/0304-4165(94)00116-F
dc.identifier.eissn1872-8006
dc.identifier.issn0304-4165
dc.identifier.pubmedidMEDLINE:7827105
dc.identifier.urihttps://doi.org/10.1016/0304-4165(94)00116-F
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/79126
dc.identifier.wosidWOS:A1995QC58600005
dc.information.autorucMedicina;Accatino L;S/I;99016
dc.issue.numero1
dc.language.isoen
dc.nota.accesoSin adjunto
dc.pagina.final42
dc.pagina.inicio33
dc.publisherELSEVIER SCIENCE BV
dc.revistaBIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
dc.rightsregistro bibliográfico
dc.subjectCANALICULUS
dc.subjectMEMBRANE
dc.subjectENZYME
dc.subjectBILE
dc.subjectMICELLE
dc.subjectVESICLE
dc.subjectELASTIC LIGHT-SCATTERING
dc.subjectALKALINE-PHOSPHATASE
dc.subjectCHOLESTEROL CARRIERS
dc.subjectPHOSPHOLIPID-VESICLES
dc.subjectBILIARY CHOLESTEROL
dc.subjectPROTEINS
dc.subjectSERUM
dc.subjectSECRETION
dc.subjectOUTPUT
dc.subjectSALTS
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleASSOCIATION OF CANALICULAR MEMBRANE ENZYMES WITH BILE-ACID MICELLES AND LIPID AGGREGATES IN HUMAN AND RAT BILE
dc.typeartículo
dc.volumen1243
sipa.codpersvinculados99016
sipa.indexWOS
sipa.indexScopus
sipa.trazabilidadCarga SIPA;09-01-2024
Files
Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
ASSOCIATION OF CANALICULAR MEMBRANE ENZYMES WITH BILE-ACID MICELLES AND LIPID AGGREGATES IN HUMAN AND RAT BILE.pdf
Size:
3.32 KB
Format:
Adobe Portable Document Format
Description:
Download
Collections
Artículos de revistas