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Titolo:
Modulation of Na+/H+ exchange activity by Cl-
Autore:
Aharonovitz, O; Kapus, A; Szaszi, K; Coady-Osberg, N; Jancelewicz, T; Orlowski, J; Grinstein, S;
Indirizzi:
Hosp Sick Children, Cell Biol Program, Toronto, ON M5G 1X8, Canada Hosp Sick Children Toronto ON Canada M5G 1X8 Toronto, ON M5G 1X8, Canada Toronto Hosp, Dept Surg, Toronto, ON M5G 1L7, Canada Toronto Hosp TorontoON Canada M5G 1L7 Surg, Toronto, ON M5G 1L7, Canada Univ Toronto, Toronto, ON M5G 1L7, Canada Univ Toronto Toronto ON Canada M5G 1L7 ronto, Toronto, ON M5G 1L7, Canada McGill Univ, Dept Physiol, Montreal, PQ H3G 1Y6, Canada McGill Univ Montreal PQ Canada H3G 1Y6 siol, Montreal, PQ H3G 1Y6, Canada
Titolo Testata:
AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY
fascicolo: 1, volume: 281, anno: 2001,
pagine: C133 - C141
SICI:
0363-6143(200107)281:1<C133:MONEAB>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
RED-BLOOD-CELLS; NA-H EXCHANGE; BARNACLE MUSCLE-FIBERS; GLUTARALDEHYDE FIXATION; VOLUME REGULATION; SHRINKAGE; ANTIPORT; PH; ACTIVATION; PHYSIOLOGY;
Keywords:
antiport; type 1 Na+/H+ exchanger; anion dependence; osmotic activation; volume regulation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
40
Recensione:
Indirizzi per estratti:
Indirizzo: Grinstein, S Hosp Sick Children, Cell Biol Program, 555 Univ Ave, Toronto,ON M5G 1X8, Canada Hosp Sick Children 555 Univ Ave Toronto ON Canada M5G 1X8 ada
Citazione:
O. Aharonovitz et al., "Modulation of Na+/H+ exchange activity by Cl-", AM J P-CELL, 281(1), 2001, pp. C133-C141

Abstract

Na+/H+ exchanger (NHE) activity is exquisitely dependent on the intra- andextracellular concentrations of Na+ and H+. In addition, Cl- ions have been suggested to modulate NHE activity, but little is known about the underlying mechanism, and the Cl- sensitivity of the individual isoforms has not been established. To explore their Cl- sensitivity, types 1, 2, and 3 Na+/Hexchangers (NHE1, NHE2, and NHE3) were heterologously expressed in antiport-deficient cells. Bilateral replacement of Cl- with nitrate or thiocyanateinhibited the activity of all isoforms. Cl- depletion did not affect cell volume or the cellular ATP content, which could have indirectly altered NHEactivity. The number of plasmalemmal exchangers was unaffected by Cl- removal, implying that inhibition was due to a decrease in the intrinsic activity of individual exchangers. Analysis of truncated mutants of NHE1 revealedthat the anion sensitivity resides, at least in part, in the COOH-terminaldomain of the exchanger. Moreover, readdition of Cl- into the extracellular medium failed to restore normal transport, suggesting that intracellular Cl- is critical for activity. Thus interaction of intracellular Cl- with the COOH terminus of NHE1 or with an associated protein is essential for optimal activity.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/01/20 alle ore 15:11:12