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Article: Identification of cytosolic and microsomal bile acid-binding proteins in rat ileal enterocytes

TitleIdentification of cytosolic and microsomal bile acid-binding proteins in rat ileal enterocytes
Authors
Issue Date1990
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 1990, v. 265 n. 25, p. 14986-14995 How to Cite?
AbstractStudies were performed to determine the subcellular fractions and proteins involved in the intracellular transport of bile acids in rat ileal cells. The photolabile derivative 7,7-azo-taurocholate inhibited the Na +-dependent uptake of taurocholate into rat ileal enterocytes reversibly in the dark and irreversibly following photolysis. When photolabeled cells were submitted to subcellular fractionation, greatest radioactivity was found in the soluble protein (SP) fraction with decreasing radioactivity in the brush-border- (BBM), basolateral- (BLM), mitochondria- (MT), microsome- (MC), and Golgi- (GO) enriched fractions. Following trichloroacetic acid precipitation, delipidation, and correction for loss of marker enzyme activity, protein bound radioactivity was in SP > BBM > MC > BLM > GO > MT. When photolabeled cells were first fractionated and then submitted to sodium dodecyl sulfate-polyacrylamide gel electrophoresis, a 99-kDa polypeptide was associated with BBM, 54- and 59-kDa polypeptides with BLM, 14-, 35-, 43-, 59-, and 68-kDa polypeptides with SP and a 20-kDa polypeptide with MC fractions. Immunoprecipitation with known antisera identified the 68-kDa polypeptide as albumin and the 43-kDa polypeptide as actin. No precipitation on the 14-kDa polypeptide was noted with anti-hepatic and anti-intestinal fatty acid-binding proteins. No precipitation of the 35-kDa polypeptide occurred with antibody to the hepatic cytosolic bile acid-binding protein. These studies reveal a previously unrecognized 20-kDa microsomal, and 14- and 35-kDa cytosolic bile acid-binding polypeptides which may be involved in the transcellular movement of bile acids.
Persistent Identifierhttp://hdl.handle.net/10722/167490
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLin, MCen_US
dc.contributor.authorKramer, Wen_US
dc.contributor.authorWilson, FAen_US
dc.date.accessioned2012-10-08T03:07:37Z-
dc.date.available2012-10-08T03:07:37Z-
dc.date.issued1990en_US
dc.identifier.citationJournal Of Biological Chemistry, 1990, v. 265 n. 25, p. 14986-14995en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://hdl.handle.net/10722/167490-
dc.description.abstractStudies were performed to determine the subcellular fractions and proteins involved in the intracellular transport of bile acids in rat ileal cells. The photolabile derivative 7,7-azo-taurocholate inhibited the Na +-dependent uptake of taurocholate into rat ileal enterocytes reversibly in the dark and irreversibly following photolysis. When photolabeled cells were submitted to subcellular fractionation, greatest radioactivity was found in the soluble protein (SP) fraction with decreasing radioactivity in the brush-border- (BBM), basolateral- (BLM), mitochondria- (MT), microsome- (MC), and Golgi- (GO) enriched fractions. Following trichloroacetic acid precipitation, delipidation, and correction for loss of marker enzyme activity, protein bound radioactivity was in SP > BBM > MC > BLM > GO > MT. When photolabeled cells were first fractionated and then submitted to sodium dodecyl sulfate-polyacrylamide gel electrophoresis, a 99-kDa polypeptide was associated with BBM, 54- and 59-kDa polypeptides with BLM, 14-, 35-, 43-, 59-, and 68-kDa polypeptides with SP and a 20-kDa polypeptide with MC fractions. Immunoprecipitation with known antisera identified the 68-kDa polypeptide as albumin and the 43-kDa polypeptide as actin. No precipitation on the 14-kDa polypeptide was noted with anti-hepatic and anti-intestinal fatty acid-binding proteins. No precipitation of the 35-kDa polypeptide occurred with antibody to the hepatic cytosolic bile acid-binding protein. These studies reveal a previously unrecognized 20-kDa microsomal, and 14- and 35-kDa cytosolic bile acid-binding polypeptides which may be involved in the transcellular movement of bile acids.en_US
dc.languageengen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_US
dc.relation.ispartofJournal of Biological Chemistryen_US
dc.subject.meshAnimalsen_US
dc.subject.meshBile Acids And Salts - Metabolismen_US
dc.subject.meshCarrier Proteins - Isolation & Purification - Metabolism - Radiation Effectsen_US
dc.subject.meshCell Fractionation - Methodsen_US
dc.subject.meshCentrifugation, Density Gradienten_US
dc.subject.meshCytosol - Metabolismen_US
dc.subject.meshEpithelial Cellsen_US
dc.subject.meshEpithelium - Metabolismen_US
dc.subject.meshHydroxysteroid Dehydrogenasesen_US
dc.subject.meshIleum - Cytology - Metabolismen_US
dc.subject.meshKineticsen_US
dc.subject.meshMembrane Glycoproteinsen_US
dc.subject.meshMicrosomes - Metabolismen_US
dc.subject.meshMolecular Weighten_US
dc.subject.meshMuscle, Smooth - Cytology - Metabolismen_US
dc.subject.meshRatsen_US
dc.subject.meshTaurocholic Acid - Metabolismen_US
dc.subject.meshUltraviolet Raysen_US
dc.titleIdentification of cytosolic and microsomal bile acid-binding proteins in rat ileal enterocytesen_US
dc.typeArticleen_US
dc.identifier.emailLin, MC:mcllin@hkucc.hku.hken_US
dc.identifier.authorityLin, MC=rp00746en_US
dc.description.naturelink_to_OA_fulltexten_US
dc.identifier.pmid2394709-
dc.identifier.scopuseid_2-s2.0-0025140903en_US
dc.identifier.volume265en_US
dc.identifier.issue25en_US
dc.identifier.spage14986en_US
dc.identifier.epage14995en_US
dc.identifier.isiWOS:A1990DX40000051-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridLin, MC=7404816359en_US
dc.identifier.scopusauthoridKramer, W=7202828799en_US
dc.identifier.scopusauthoridWilson, FA=7202849433en_US

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