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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1996-10-17
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pubmed:abstractText |
We identified voltage-activated K+ channels in freshly dispersed smooth muscle cells from the circular layer of the canine colon in patch-clamp experiments using 200 nM charybdotoxin to suppress 270-pS Ca2+-activated K+ channels (BK channels). Three channel types were distinguished in symmetrical 140 mM KCl solutions: 19.5 +/- 1.7 pS channels (KDR1), 90.6 +/- 5.4 pS channels (KDR2) and 149 +/- 4 pS intermediate-conductance Ca2+-activated K+ channels (IK channels). All three types showed an increase in open probability with membrane depolarization. Ensemble average current from KDR1 channels inactivated with a time constant of 1.7 +/- 0.1 s at +60 mV test potential, while KDR2 and IK channels did not show inactivation. IK channels were activated by free cytoplasmic [Ca2+] (10(-6 )M) but were insensitive to 4-aminopyridine (4-AP, 10 mM) and intracellular tetraethylammonium (TEA, 1 mM). KDR1 channels were sensitive to 4-AP (10 mM) and intracellular TEA (1-10 mM) but not to Ca2+. KDR2 channels did not have a consistent pharmacological profile, suggesting that this class may be comprised of several subtypes. At +40 mV membrane potential, the catalytic subunit of protein kinase A (PKA) increased the open probability of KDR1 channels 3.4-fold and of KDR2 channels 3.9-fold, but had no effect on IK channels. In the absence of Mg-ATP, PKA did not affect channel open probabilities. At physiological membrane potentials (-60 mV) only openings of KDR1 channels could be induced by PKA, suggesting that these 4-AP-sensitive 20-pS K+ channels are primarily responsible for the cAMP-mediated hyperpolarization of colonic smooth muscle cells.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/4-Aminopyridine,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Charybdotoxin,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP-Dependent Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Tetraethylammonium Compounds
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0031-6768
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
432
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
401-12
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:8765999-4-Aminopyridine,
pubmed-meshheading:8765999-Adenosine Triphosphate,
pubmed-meshheading:8765999-Animals,
pubmed-meshheading:8765999-Calcium,
pubmed-meshheading:8765999-Charybdotoxin,
pubmed-meshheading:8765999-Colon,
pubmed-meshheading:8765999-Cyclic AMP-Dependent Protein Kinases,
pubmed-meshheading:8765999-Dogs,
pubmed-meshheading:8765999-Female,
pubmed-meshheading:8765999-Male,
pubmed-meshheading:8765999-Membrane Potentials,
pubmed-meshheading:8765999-Muscle, Smooth,
pubmed-meshheading:8765999-Patch-Clamp Techniques,
pubmed-meshheading:8765999-Potassium Channels,
pubmed-meshheading:8765999-Tetraethylammonium Compounds
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pubmed:year |
1996
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pubmed:articleTitle |
Regulation of smooth muscle delayed rectifier K+ channels by protein kinase A.
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pubmed:affiliation |
Dept. of Physiology, School of Medicine, Hanyang University, Seoul, Korea.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.
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