Linked Life Data

10836990

Source:http://linkedlifedata.com/resource/pubmed/id/10836990

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2000-7-19
pubmed:abstractText
Our laboratory previously cloned a novel rabbit gene (Kcn1), expressed in kidney, heart, and aorta, and predicted to encode a protein with 58% amino acid identity with the K channel Shaker Kv1.3 (Yao X et al. Proc Natl Acad Sci USA 92: 11711-11715, 1995). Because Kcn1 did not express well (peak current in Xenopus laevis oocytes of 0.3 microA at +60 mV), the human homolog (KCNA10) was isolated, and its expression was optimized in oocytes. KCNA10 mediates voltage-gated K(+) currents that exhibit minimal steady-state inactivation. Ensemble currents of 5-10 microA at +40 mV were consistently recorded from injected oocytes. Channels are closed at the holding potential of -80 mV but are progressively activated by depolarizations more positive than -30 mV, with half-activation at +3.5 +/- 2.5 mV. The channel displays an unusual inhibitor profile because, in addition to being blocked by classical K channel blockers (barium tetraethylammonium and 4-aminopyridine), it is also sensitive to inhibitors of cyclic nucleotide-gated (CNG) cation channels (verapamil and pimozide). Tail-current analysis shows a reversal potential shift of 47 mV/decade change in K concentration, indicating a K-to-Na selectivity ratio of at least 15:1. The phorbol ester phorbol 12-myristate 13-acetate, an activator of protein kinase C, inhibited whole cell current by 42%. Analysis of single-channel currents reveals a conductance of approximately 11 pS. We conclude KCNA10 is a novel human voltage-gated K channel with features common to both K-selective and CNG cation channels. Given its distribution in renal blood vessels and heart, we speculate that KCNA10 may be involved in regulating the tone of renal vascular smooth muscle and may also participate in the cardiac action potential.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1931-857X
pubmed:author
pubmed:issnType
Print
pubmed:volume
278
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
F1013-21
pubmed:dateRevised
2011-4-28
pubmed:meshHeading
pubmed-meshheading:10836990-Animals, pubmed-meshheading:10836990-Base Sequence, pubmed-meshheading:10836990-Cyclic Nucleotide-Gated Cation Channels, pubmed-meshheading:10836990-DNA Primers, pubmed-meshheading:10836990-Female, pubmed-meshheading:10836990-Humans, pubmed-meshheading:10836990-Ion Channel Gating, pubmed-meshheading:10836990-Ion Channels, pubmed-meshheading:10836990-Membrane Potentials, pubmed-meshheading:10836990-Oocytes, pubmed-meshheading:10836990-Patch-Clamp Techniques, pubmed-meshheading:10836990-Potassium Channel Blockers, pubmed-meshheading:10836990-Potassium Channels, pubmed-meshheading:10836990-Potassium Channels, Voltage-Gated, pubmed-meshheading:10836990-Rabbits, pubmed-meshheading:10836990-Recombinant Proteins, pubmed-meshheading:10836990-Second Messenger Systems, pubmed-meshheading:10836990-Shaker Superfamily of Potassium Channels, pubmed-meshheading:10836990-Xenopus laevis
pubmed:year
2000
pubmed:articleTitle
KCNA10: a novel ion channel functionally related to both voltage-gated potassium and CNG cation channels.
pubmed:affiliation
University of Vermont, Burlington 05446, USA.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't