| pubmed-article:17951301 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17951301 | lifeskim:mentions | umls-concept:C0205101 | lld:lifeskim |
| pubmed-article:17951301 | lifeskim:mentions | umls-concept:C1709059 | lld:lifeskim |
| pubmed-article:17951301 | lifeskim:mentions | umls-concept:C0439799 | lld:lifeskim |
| pubmed-article:17951301 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:17951301 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:17951301 | pubmed:dateCreated | 2008-1-24 | lld:pubmed |
| pubmed-article:17951301 | pubmed:abstractText | In response to a prolonged membrane depolarization, inactivation autoregulates the activity of voltage-gated ion channels. Slow inactivation involving a localized constriction of the selectivity filter (P/C-type mechanism) is prevalent in many voltage-gated K(+) channels of the Kv1 subfamily. However, the generalization of this mechanism to other Kv channel subfamilies has remained uncertain and controversial. In agreement with a "foot-in-the-door" mechanism and the presence of ion-ion interactions in the pore, elevated external K(+) slows the development of P/C-type inactivation and accelerates its recovery. In sharp contrast and resembling the regulation of the hippocampal A-type K(+) current, we found that Kv4.x channels associated with KChIP-1 (an auxiliary subunit) exhibit accelerated inactivation and unaffected recovery from inactivation when exposed to elevated external K(+). This regulation depends on the ability of a permeant ion to enter the selectivity filter (K(+) = Rb(+) = NH4(+) > Cs(+) > Na(+)); and the apparent equilibrium dissociation constant of a single regulatory site is 8 mM for K(+). By applying a robust quantitative global kinetic modeling approach to all macroscopic properties over a 210-mV range of membrane potentials, we determined that elevated external K(+) inhibits unstable closed states outside the main activation pathway and thereby promotes preferential closed-state inactivation. These results suggest the presence of a vestigial and unstable P/C-type mechanism of inactivation in Kv4 channels and strengthen the concept of novel mechanisms of closed-state inactivation. Regulation of Kv4 channel inactivation by hyperkalemia may help to explain the pathophysiology of electrolyte imbalances in excitable tissues. | lld:pubmed |
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| pubmed-article:17951301 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17951301 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17951301 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17951301 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17951301 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17951301 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17951301 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:17951301 | pubmed:issn | 1542-0086 | lld:pubmed |
| pubmed-article:17951301 | pubmed:author | pubmed-author:CovarrubiasMM | lld:pubmed |
| pubmed-article:17951301 | pubmed:author | pubmed-author:RochaC ACA | lld:pubmed |
| pubmed-article:17951301 | pubmed:author | pubmed-author:KaulinYu AYA | lld:pubmed |
| pubmed-article:17951301 | pubmed:author | pubmed-author:De... | lld:pubmed |
| pubmed-article:17951301 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:17951301 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:17951301 | pubmed:volume | 94 | lld:pubmed |
| pubmed-article:17951301 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17951301 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17951301 | pubmed:pagination | 1241-51 | lld:pubmed |
| pubmed-article:17951301 | pubmed:dateRevised | 2011-9-26 | lld:pubmed |
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