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- Publisher Website: 10.1007/BF01871762
- Scopus: eid_2-s2.0-0024120055
- PMID: 3225838
- WOS: WOS:A1988R169400001
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Article: Identification and comparsion of bile acid-binding polypeptides in ileal basolateral membrane
Title | Identification and comparsion of bile acid-binding polypeptides in ileal basolateral membrane |
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Authors | |
Keywords | basolateral membrane bile acid-binding polypeptides photoaffinity labeling |
Issue Date | 1988 |
Publisher | Springer 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? |
Abstract | Bile 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 Identifier | http://hdl.handle.net/10722/167479 |
ISSN | 2023 Impact Factor: 2.3 2023 SCImago Journal Rankings: 0.667 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Lin, MC | en_US |
dc.contributor.author | Weinberg, SL | en_US |
dc.contributor.author | Kramer, W | en_US |
dc.contributor.author | Burckhardt, G | en_US |
dc.contributor.author | Wilson, FA | en_US |
dc.date.accessioned | 2012-10-08T03:07:31Z | - |
dc.date.available | 2012-10-08T03:07:31Z | - |
dc.date.issued | 1988 | en_US |
dc.identifier.citation | The Journal Of Membrane Biology, 1988, v. 106 n. 1, p. 1-11 | en_US |
dc.identifier.issn | 0022-2631 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/167479 | - |
dc.description.abstract | Bile 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.language | eng | en_US |
dc.publisher | Springer New York LLC. The Journal's web site is located at http://link.springer.de/link/service/journals/00232/ | en_US |
dc.relation.ispartof | The Journal of Membrane Biology | en_US |
dc.subject | basolateral membrane | - |
dc.subject | bile acid-binding polypeptides | - |
dc.subject | photoaffinity labeling | - |
dc.subject.mesh | Affinity Labels | en_US |
dc.subject.mesh | Animals | en_US |
dc.subject.mesh | Azo Compounds - Diagnostic Use - Pharmacology | en_US |
dc.subject.mesh | Bile Acids And Salts - Pharmacokinetics | en_US |
dc.subject.mesh | Biological Markers | en_US |
dc.subject.mesh | Biological Transport, Active | en_US |
dc.subject.mesh | Carrier Proteins - Isolation & Purification - Physiology | en_US |
dc.subject.mesh | Cell Membrane - Metabolism | en_US |
dc.subject.mesh | Electrophoresis, Polyacrylamide Gel | en_US |
dc.subject.mesh | Epithelium - Enzymology - Metabolism | en_US |
dc.subject.mesh | Ileum - Cytology - Enzymology - Metabolism | en_US |
dc.subject.mesh | Lighting | en_US |
dc.subject.mesh | Male | en_US |
dc.subject.mesh | Membrane Proteins - Isolation & Purification - Physiology | en_US |
dc.subject.mesh | Rats | en_US |
dc.subject.mesh | Rats, Inbred Strains | en_US |
dc.subject.mesh | Taurocholic Acid - Pharmacokinetics | en_US |
dc.subject.mesh | P-Aminohippuric Acid - Metabolism | en_US |
dc.title | Identification and comparsion of bile acid-binding polypeptides in ileal basolateral membrane | en_US |
dc.type | Article | en_US |
dc.identifier.email | Lin, MC:mcllin@hkucc.hku.hk | en_US |
dc.identifier.authority | Lin, MC=rp00746 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1007/BF01871762 | en_US |
dc.identifier.pmid | 3225838 | - |
dc.identifier.scopus | eid_2-s2.0-0024120055 | en_US |
dc.identifier.volume | 106 | en_US |
dc.identifier.issue | 1 | en_US |
dc.identifier.spage | 1 | en_US |
dc.identifier.epage | 11 | en_US |
dc.identifier.isi | WOS:A1988R169400001 | - |
dc.publisher.place | United States | en_US |
dc.identifier.scopusauthorid | Lin, MC=7404816359 | en_US |
dc.identifier.scopusauthorid | Weinberg, SL=7101675958 | en_US |
dc.identifier.scopusauthorid | Kramer, W=7202828799 | en_US |
dc.identifier.scopusauthorid | Burckhardt, G=26642911100 | en_US |
dc.identifier.scopusauthorid | Wilson, FA=7202849433 | en_US |
dc.identifier.issnl | 0022-2631 | - |