Am J Physiol Cell Physiol Fuel your research with LabChart
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Am J Physiol Cell Physiol 270: C964-C968, 1996;
0363-6143/96 $5.00
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Suzuki, M.
Right arrow Articles by Imai, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Suzuki, M.
Right arrow Articles by Imai, M.

AJP - Cell Physiology, Vol 270, Issue 3 C964-C968, Copyright © 1996 by American Physiological Society

ARTICLES

Electrophysiological characterization of RACTK1 K+ channel in stable cell line

M. Suzuki, M. Murata, M. Ikeda, T. Miyoshi and M. Imai
Department of Pharmacology, Jichi Medical School, Minamikawachi, Japan.

RACTK1 is a pH-sensitive K+ channel cloned from rabbit renal collecting tubule cells. To characterize the function of this K+ channel in more detail, RACTK1 was transfected to an established cell line and the patch-clamp study was performed. cDNA of RACTK1 was inserted in the pMAM vector and transfected to Chinese hamster ovary cells. In one of 36 cell lines, the channel protein as expressed by the dexamethasone-induced mRNA and was detected by the specific antibody. The RACTK1 K+ channel with 80 pS was consistently observed. In inside-out patch, Ca2+ at concentrations higher than 500 nM activated the channel. Open probability was decreased by protein kinase A (from 45 to 4.2%, n+6) but not by protein kinase C. Whole cell currents of the transformed cells represented K+ conductance that was not blocked by an addition of charybdotoxin but by apamin. RACTK1 K+ channel has similar, though not identical, characteristics to the Ca2+ -activated K+ channel. RACTK1 might therefore encode a subunit of the intermediate conductance Ca2+ -activated K+ channel observed in the apical membrane of the rabbit renal collecting duct.


This article has been cited by other articles:


Home page
 Am. J. Physiol. Cell Physiol.Home page
Corrigenda
Am J Physiol Cell Physiol, July 1, 2006; 291(1): C194 - C194.
[Full Text] [PDF]

Home page
 Am. J. Physiol. Renal Physiol.Home page
L. G. Palmer
Potassium secretion and the regulation of distal nephron K channels
Am J Physiol Renal Physiol, December 1, 1999; 277(6): F821 - F825.
[Abstract] [Full Text] [PDF]

Home page
 J. Neurosci.Home page
T. C. Holmes, K. Berman, J. E. Swartz, D. Dagan, and I. B. Levitan
Expression of Voltage-Gated Potassium Channels Decreases Cellular Protein Tyrosine Phosphorylation
J. Neurosci., December 1, 1997; 17(23): 8964 - 8974.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online