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Titolo:
IMMUNOLOGICAL DISTRIBUTION OF AN ORGANIC ANION TRANSPORT PROTEIN IN RAT-LIVER AND KIDNEY
Autore:
BERGWERK AJ; SHI XY; FORD AC; KANAI N; JACQUEMIN E; BURK RD; BAI S; NOVIKOFF PM; STIEGER B; MEIER PJ; SCHUSTER VL; WOLKOFF AW;
Indirizzi:
ALBERT EINSTEIN COLL MED,MARION BESSIN LIVER RES CTR,DIV NEPHROL,1300MORRIS PK AVE BRONX NY 10461 ALBERT EINSTEIN COLL MED,MARION BESSIN LIVER RES CTR,DIV NEPHROL BRONX NY 10461 UNITE RECH F-94276 LE KREMLIN BICETR FRANCE UNIV ZURICH HOSP,DIV CLIN PHARMACOL CH-8091 ZURICH SWITZERLAND
Titolo Testata:
American journal of physiology: Gastrointestinal and liver physiology
fascicolo: 2, volume: 34, anno: 1996,
pagine: 231 - 238
SICI:
0193-1857(1996)34:2<231:IDOAOA>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
GLUTAMYL-TRANSFERASE TRANSPEPTIDASE; BASOLATERAL PLASMA-MEMBRANE; EXPRESSION CLONING; BINDING PROTEIN; RNA-POLYMERASE; SYSTEM; SULFOBROMOPHTHALEIN; LOCALIZATION; BILIRUBIN; CHLORIDE;
Keywords:
SULFOBROMOPHTHALEIN; PROTEIN TRAFFICKING; PROTEIN PROCESSING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
38
Recensione:
Indirizzi per estratti:
Citazione:
A.J. Bergwerk et al., "IMMUNOLOGICAL DISTRIBUTION OF AN ORGANIC ANION TRANSPORT PROTEIN IN RAT-LIVER AND KIDNEY", American journal of physiology: Gastrointestinal and liver physiology, 34(2), 1996, pp. 231-238

Abstract

Na+-independent organic anion transport protein was recently cloned from rat liver using a Xenopus laevis oocyte expression system [E. Jacquemin, B. Hagenbuch, B. Stieger, A. W. Wolkoff, and P. J. Meier, Proc. Natl. Acad. Sci. USA 91: 133-137, 1994]. Although expression of this protein is sufficient for cells to transport the organic anion bromosulfophthalein, little is known about its cell biology or biochemical characteristics. Northern blot analysis performed under high-stringency conditions revealed hybridization with RNA only from liver and kidney;transcripts appeared the same in these two organs. Within kidney, hybridization was greatest when RNA extracted from the outer medulla was used. Immunoblot analysis revealed that in liver, the transporter was enriched in 0.1 M Na2CO3-extracted membranes and sinusoidal plasma membrane preparations, consistent with its being an integral membrane protein. This 80-kDa protein migrated as a 65-kDa protein after treatmentwith N-glycanase. Immunomorphological examination of liver revealed basolateral plasma membrane localization. In 0.1 M Na2CO3-extracted membranes of kidney, the transporter migrated as an 83-kDa protein on nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). On reduction, it resolved into peptides of 33 and 37 kDa. SDS-PAGE migration of the liver protein was unaffected by reduction. Immuno-morphological examination of kidney revealed apical plasma membranelocalization in the S3 segment of the proximal tubule of the outer medulla. Differential processing and trafficking of this transporter in liver and kidney may have important functional and regulatory consequences.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/01/21 alle ore 07:52:49