title: TASK (TWIK-related acid-sensitive K+ channel) is expressed in glomerulosa cells of rat adrenal cortex and inhibited by angiotensin II.
abstract: The present study was conducted to explore the possible contribution of a recently described leak K+ channel, TASK (TWIK-related acid-sensitive K+ channel), to the high resting K+ conductance of adrenal glomerulosa cells. Northern blot analysis showed the strongest TASK message in adrenal glomerulosa (capsular) tissue among the examined tissues including heart and brain. Single-cell PCR demonstrated TASK expression in glomerulosa cells. In patch-clamp experiments performed on isolated glomerulosa cells the inward current at -100 mV in 30 mM [K+] (reflecting mainly potassium conductance) was pH sensitive (17+/-2% reduction when the pH changed from 7.4 to 6.7). In Xenopus oocytes injected with mRNA prepared from adrenal glomerulosa tissue the expressed K+ current at -100 mV was virtually insensitive to tetraethylammonium (3 mM) and 4-aminopyridine (3 mM). Ba2+ (300 microM) and Cs+ (3 mM) induced voltage-dependent block. Lidocaine (1 mM) and extracellular acidification from pH 7.5 to 6.7 inhibited the current (by 28% and 16%, respectively). This inhibitory profile is similar (although it is not identical) to that of TASK expressed by injecting its cRNA. In oocytes injected with adrenal glomerulosa mRNA, TASK antisense oligonucleotide reduced significantly the expression of K+ current at -100 mV, while the sense oligonucleotide failed to have inhibitory effect. Application of angiotensin II (10 nM) both in isolated glomerulosa cells and in oocytes injected with adrenal glomerulosa mRNA inhibited the K+ current at -100 mV. Similarly, in oocytes coexpressing TASK and ATla angiotensin II receptor, angiotensin II inhibited the TASK current. These data together indicate that TASK contributes to the generation of high resting potassium permeability of glomerulosa cells, and this background K+ channel may be a target of hormonal regulation.
authors.affiliation: Department of Physiology, Semmelweis University of Medicine, Budapest, Hungary.
authors.forename: G
authors.initials: G
authors.lastname: Czirják
authors.forename: T
authors.initials: T
authors.lastname: Fischer
authors.forename: A
authors.initials: A
authors.lastname: Spät
authors.forename: F
authors.initials: F
authors.lastname: Lesage
authors.forename: P
authors.initials: P
authors.lastname: Enyedi
mesh_terms: D015761:4-Aminopyridine / Q000494:pharmacology; D000804:Angiotensin II / Q000494:pharmacology*; D000818:Animals; D015152:Blotting, Northern; D001923:Brain Chemistry; D002463:Cell Membrane Permeability; D004553:Electric Conductivity; D005260:Female; D015870:Gene Expression / Q000187:drug effects*; D006863:Hydrogen-Ion Concentration; D008564:Membrane Potentials; D009206:Myocardium / Q000737:chemistry; D009419:Nerve Tissue Proteins; D016376:Oligonucleotides, Antisense / Q000494:pharmacology; D009865:Oocytes / Q000378:metabolism; D018408:Patch-Clamp Techniques; D011188:Potassium / Q000378:metabolism; D015221:Potassium Channels / Q000235:genetics*; D024683:Potassium Channels, Tandem Pore Domain; D012333:RNA, Messenger / Q000032:analysis; D051381:Rats; D017208:Rats, Wistar; D019789:Tetraethylammonium / Q000494:pharmacology; D014162:Transfection; D014982:Xenopus laevis; D015384:Zona Glomerulosa / Q000378:metabolism*
chemical_list: D009419:Nerve Tissue Proteins; D016376:Oligonucleotides, Antisense; D015221:Potassium Channels; D024683:Potassium Channels, Tandem Pore Domain; D012333:RNA, Messenger; D000804:Angiotensin II; C420132:potassium channel subfamily K member 3; D019789:Tetraethylammonium; D015761:4-Aminopyridine; D011188:Potassium