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Titolo:
Differential localization of human nongastric H+-K+-ATPase ATP1AL1 in polarized renal epithelial cells
Autore:
Reinhardt, J; Grishin, AV; Oberleithner, H; Caplan, MJ;
Indirizzi:
Yale Univ, Sch Med, Dept Cellular & Mol Physiol, New Haven, CT 06520 USA Yale Univ New Haven CT USA 06520 r & Mol Physiol, New Haven, CT 06520 USA Univ Munster, Dept Physiol, D-48149 Munster, Germany Univ Munster Munster Germany D-48149 t Physiol, D-48149 Munster, Germany
Titolo Testata:
AMERICAN JOURNAL OF PHYSIOLOGY-RENAL PHYSIOLOGY
fascicolo: 3, volume: 279, anno: 2000,
pagine: F417 - F425
SICI:
0363-6127(200009)279:3<F417:DLOHNH>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
GASTRIC-ACID SECRETION; ALPHA-SUBUNIT; BETA-SUBUNIT; FUNCTIONAL EXPRESSION; SORTING SIGNALS; RAT-KIDNEY; NA,K-ATPASE; H,K-ATPASE; H+,K+-ATPASE; TRANSPORT;
Keywords:
proton-potassium-adenosinetriphosphatase; sorting;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Caplan, MJ Yale Univ, Sch Med, Dept Cellular & Mol Physiol, 333 Cedar St, New Haven, CT 06520 USA Yale Univ 333 Cedar St New Haven CT USA 06520 ven, CT 06520 USA
Citazione:
J. Reinhardt et al., "Differential localization of human nongastric H+-K+-ATPase ATP1AL1 in polarized renal epithelial cells", AM J P-REN, 279(3), 2000, pp. F417-F425

Abstract

The human H+-K+-ATPase, ATP1AL1, belongs to the subgroup of nongastric, K+-transporting ATPases. In concert with the structurally related gastric H+-K+-ATPase, it plays a major role in K+ reabsorption in various tissues, including colon and kidney. Physiological and immunocytochemical data suggest that the functional heteromeric ion pumps are usually found in the apical plasma membranes of renal epithelial cells. However, the low expression levels of characteristic nongastric ion pumps makes it difficult to verify their spatial distribution in vivo. To investigate the sorting behavior of ATP1AL1, we expressed this pump by stable transfection in MDCK and LLC-PK1 renal epithelial cell lines. Stable interaction of ATP1AL1 with either the endogenous Na+-K+-ATPase beta-subunit or the gastric H+-K+-ATPase beta-subunit was tested by confocal immunofluorescence microscopy and surface biotinylation. In cells transfected with ATP1AL1 alone, the alpha-subunit accumulatedintracellularly, consistent with its inability to assemble and travel to the plasma membrane with the endogenous Na+-K+-ATPase beta-subunit. Cotransfection of ATP1AL1 with the gastric H+-K+-ATPase beta-subunit resulted in plasma membrane localization of both pump subunits. In cotransfected MDCK cells the heteromeric ion pump was predominantly polarized to the apical plasma membrane. Functional expression of ATP1AL1 was confirmed by Rb-86(+) uptake measurements. In contrast, cotransfected LLC-PK1 cells accumulate ATP1AL1 at the lateral membrane. The distinct polarization of ATP1AL1 indicates that the a-subunit encodes sorting information that is differently interpreted by cell type-specific sorting mechanisms.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 22:19:22