File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Identification and comparsion of bile acid-binding polypeptides in ileal basolateral membrane

TitleIdentification and comparsion of bile acid-binding polypeptides in ileal basolateral membrane
Authors
Issue Date1988
PublisherSpringer New York LLC. The Journal's web site is located at http://link.springer.de/link/service/journals/00232/
Citation
The Journal Of Membrane Biology, 1988, v. 106 n. 1, p. 1-11 How to Cite?
AbstractBile acid-binding polypeptides were examined using basolateral membrane vesicles and enterocytes isolated from rat ileum. The uptake of a photolabile taurocholate derivative, (7,7,-azo-3α, 12α-dihydroxy-5β[3β-3H]cholan-24-oyl)-2-aminoethanesulfonate, 7,7-azo-TC, in ileal vesicles preloaded with paraaminohippurate (PAH) was stimulated with respect to uptake in unpreloaded vesicles. The PAH-transstimulated uptake of 7,7-azo-TC was inhibited by taurocholate and vice versa. Irradiation of membrane vesicles in the presence of 7,7-azo-TC irreversibly inhibited PAH-transtimulated taurocholate uptake. Photoaffinity labeling of basolateral membrane vesicles directly with [3H] 7,7-azo-TC and separation of proteins by SDS-PAGE revealed incorporation of radioactivity into several polypeptides. Photoaffinity labeling of vesicles in the presence of taurocholate inhibited the labeling of 54,000 and 59,000 mol. wt. polypeptides. The efflux of taurocholate from ileal enterocytes was cis-inhibited by 7,7-azo-TC and transstimulated by PAH. Irradiation of enterocytes in the presence of 7,7-azo-TC inhibited taurocholate efflux greater than the presence of 7.7-azo-TC in the dark. When enterocytes that were irradiated in the presence of [3H] 7,7-azo-TC were fractionated and the resultant basolateral membrane fraction was subjected to SDS-PAGE, incorporation of radioactivity into the 54,000 and 59,000 mol. wt. polypeptides was seen. In contrast, when the brush-border membrane fraction was subjected to SDS-PAGE, greatest incorporation of radioactivity was seen in the previously described 99,000 mol. wt. polypeptide. These studies suggest that 7,7-azo-TC shared transporters with natural bile acid and identified polypeptides that may be involved in bile acid and identified polypeptides that may be involved in bile acid transport across the basolateral membrane and differ from that seen in the brush-border membrane of the ileal epithelial cell. © 1988 Springer-Verlag New York Inc.
Persistent Identifierhttp://hdl.handle.net/10722/167479
ISSN
2015 Impact Factor: 1.991
2015 SCImago Journal Rankings: 0.738
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLin, MCen_US
dc.contributor.authorWeinberg, SLen_US
dc.contributor.authorKramer, Wen_US
dc.contributor.authorBurckhardt, Gen_US
dc.contributor.authorWilson, FAen_US
dc.date.accessioned2012-10-08T03:07:31Z-
dc.date.available2012-10-08T03:07:31Z-
dc.date.issued1988en_US
dc.identifier.citationThe Journal Of Membrane Biology, 1988, v. 106 n. 1, p. 1-11en_US
dc.identifier.issn0022-2631en_US
dc.identifier.urihttp://hdl.handle.net/10722/167479-
dc.description.abstractBile acid-binding polypeptides were examined using basolateral membrane vesicles and enterocytes isolated from rat ileum. The uptake of a photolabile taurocholate derivative, (7,7,-azo-3α, 12α-dihydroxy-5β[3β-3H]cholan-24-oyl)-2-aminoethanesulfonate, 7,7-azo-TC, in ileal vesicles preloaded with paraaminohippurate (PAH) was stimulated with respect to uptake in unpreloaded vesicles. The PAH-transstimulated uptake of 7,7-azo-TC was inhibited by taurocholate and vice versa. Irradiation of membrane vesicles in the presence of 7,7-azo-TC irreversibly inhibited PAH-transtimulated taurocholate uptake. Photoaffinity labeling of basolateral membrane vesicles directly with [3H] 7,7-azo-TC and separation of proteins by SDS-PAGE revealed incorporation of radioactivity into several polypeptides. Photoaffinity labeling of vesicles in the presence of taurocholate inhibited the labeling of 54,000 and 59,000 mol. wt. polypeptides. The efflux of taurocholate from ileal enterocytes was cis-inhibited by 7,7-azo-TC and transstimulated by PAH. Irradiation of enterocytes in the presence of 7,7-azo-TC inhibited taurocholate efflux greater than the presence of 7.7-azo-TC in the dark. When enterocytes that were irradiated in the presence of [3H] 7,7-azo-TC were fractionated and the resultant basolateral membrane fraction was subjected to SDS-PAGE, incorporation of radioactivity into the 54,000 and 59,000 mol. wt. polypeptides was seen. In contrast, when the brush-border membrane fraction was subjected to SDS-PAGE, greatest incorporation of radioactivity was seen in the previously described 99,000 mol. wt. polypeptide. These studies suggest that 7,7-azo-TC shared transporters with natural bile acid and identified polypeptides that may be involved in bile acid and identified polypeptides that may be involved in bile acid transport across the basolateral membrane and differ from that seen in the brush-border membrane of the ileal epithelial cell. © 1988 Springer-Verlag New York Inc.en_US
dc.languageengen_US
dc.publisherSpringer New York LLC. The Journal's web site is located at http://link.springer.de/link/service/journals/00232/en_US
dc.relation.ispartofThe Journal of Membrane Biologyen_US
dc.subject.meshAffinity Labelsen_US
dc.subject.meshAnimalsen_US
dc.subject.meshAzo Compounds - Diagnostic Use - Pharmacologyen_US
dc.subject.meshBile Acids And Salts - Pharmacokineticsen_US
dc.subject.meshBiological Markersen_US
dc.subject.meshBiological Transport, Activeen_US
dc.subject.meshCarrier Proteins - Isolation & Purification - Physiologyen_US
dc.subject.meshCell Membrane - Metabolismen_US
dc.subject.meshElectrophoresis, Polyacrylamide Gelen_US
dc.subject.meshEpithelium - Enzymology - Metabolismen_US
dc.subject.meshIleum - Cytology - Enzymology - Metabolismen_US
dc.subject.meshLightingen_US
dc.subject.meshMaleen_US
dc.subject.meshMembrane Proteins - Isolation & Purification - Physiologyen_US
dc.subject.meshRatsen_US
dc.subject.meshRats, Inbred Strainsen_US
dc.subject.meshTaurocholic Acid - Pharmacokineticsen_US
dc.subject.meshP-Aminohippuric Acid - Metabolismen_US
dc.titleIdentification and comparsion of bile acid-binding polypeptides in ileal basolateral membraneen_US
dc.typeArticleen_US
dc.identifier.emailLin, MC:mcllin@hkucc.hku.hken_US
dc.identifier.authorityLin, MC=rp00746en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1007/BF01871762en_US
dc.identifier.pmid3225838-
dc.identifier.scopuseid_2-s2.0-0024120055en_US
dc.identifier.volume106en_US
dc.identifier.issue1en_US
dc.identifier.spage1en_US
dc.identifier.epage11en_US
dc.identifier.isiWOS:A1988R169400001-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridLin, MC=7404816359en_US
dc.identifier.scopusauthoridWeinberg, SL=7101675958en_US
dc.identifier.scopusauthoridKramer, W=7202828799en_US
dc.identifier.scopusauthoridBurckhardt, G=26642911100en_US
dc.identifier.scopusauthoridWilson, FA=7202849433en_US

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats