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Titolo:
Cloning and functional expression of a liver isoform of the small conductance Ca2+-activated K+ channel SK3
Autore:
Barfod, ET; Moore, AL; Lidofsky, SD;
Indirizzi:
Univ Vermont, Dept Med, Burlington, VT 05405 USA Univ Vermont Burlington VT USA 05405 , Dept Med, Burlington, VT 05405 USA Univ Vermont, Dept Pharmacol, Burlington, VT 05405 USA Univ Vermont Burlington VT USA 05405 Pharmacol, Burlington, VT 05405 USA
Titolo Testata:
AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY
fascicolo: 4, volume: 280, anno: 2001,
pagine: C836 - C842
SICI:
0363-6143(200104)280:4<C836:CAFEOA>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACTIVATED POTASSIUM CHANNELS; PROTEIN-KINASE; CELL-LINE; SURFACE EXPRESSION; CALCIUM; MEMBRANE; DETERMINANTS; MECHANISM; PSD-95; REPEAT;
Keywords:
cloning; hepatocytes; immunofluorescence; ion channels; patch clamp; transfection;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
28
Recensione:
Indirizzi per estratti:
Indirizzo: Lidofsky, SD Univ Vermont, Burgess 414 MFU, Burlington, VT 05401 USA Univ Vermont Burgess 414 MFU Burlington VT USA 05401 5401 USA
Citazione:
E.T. Barfod et al., "Cloning and functional expression of a liver isoform of the small conductance Ca2+-activated K+ channel SK3", AM J P-CELL, 280(4), 2001, pp. C836-C842

Abstract

Small conductance Ca2+-activated K+ (SK) channels have been cloned from mammalian brain, but little is known about the molecular characteristics of SK channels in nonexcitable tissues. Here, we report the isolation from rat liver of an isoform of SK3. The sequence of the rat liver isoform differs from rat brain SK3 in five amino acid residues in the NH3 terminus, where itmore closely resembles human brain SK3. SK3 immunoreactivity was detectable in hepatocytes in rat liver and in HTC rat hepatoma cells. Human embryonic kidney (HEK-293) cells transfected with liver SK3 expressed 10 pS K+ channels that were Ca2+ dependent (EC50 630 nM) and were blocked by the SK channel inhibitor apamin (IC50 0.6 nM); whole cell SK3 currents inactivated at membrane potentials more positive than -40 mV. Notably, the Ca2+ dependence, apamin sensitivity, and voltage-dependent inactivation of SK3 are strikingly similar to the properties of hepatocellular and biliary epithelial SK channels evoked by metabolic stress. These observations raise the possibility that SK3 channels influence membrane K+ permeability in hepatobiliary cells during liver injury.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/04/20 alle ore 19:37:31