Detalles del recurso
Pertenece a:
PubMed Central (PMC3 - NLM DTD)
Descripción: The Kv2.1 channel generates a delayed-rectifier current in neurons and is responsible for modulation of neuronal spike frequency and membrane repolarization in pancreatic β-cells and cardiomyocytes. As with other tetrameric voltage-activated K+-channels, it has been proposed that each of the four Kv2.1 voltage-sensing domains activates independently upon depolarization, leading to a final concerted transition that causes channel opening. The mechanism by which voltage-sensor activation is coupled to the gating of the pore is still not understood. Here we show that the carbon-monoxide releasing molecule 2 (CORM-2) is an allosteric inhibitor of the Kv2.1 channel and that its inhibitory properties derive from the CORM-2 ability to largely reduce the voltage dependence of the opening transition, uncoupling voltage-sensor activation from the concerted opening transition. We additionally demonstrate that CORM-2 modulates Shaker K+-channels in a similar manner. Our data suggest that the mechanism of inhibition by CORM-2 may be common to voltage-activated channels and that this compound should be a useful tool for understanding the mechanisms of electromechanical coupling.
Autor(es): Jara - Oseguera, Andrés - Ishida, Itzel G. - Rangel - Yescas, Gisela E. - Espinosa - Jalapa, Noel - Pérez - Guzmán, José A. - Elías - Viñas, David - Le Lagadec, Ronan - Rosenbaum, Tamara - Islas, León D. -
Id.: 55281516
Idioma:
inglés
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Versión: 1.0
Estado: Final
Palabras clave: Membrane Biology -
Tipo de recurso:
Text
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Tipo de Interactividad: Expositivo
Nivel de Interactividad: muy bajo
Audiencia:
Estudiante
- Profesor
- Autor
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Estructura: Atomic
Coste: no
Copyright: sí
Requerimientos técnicos: Browser: Any -
Fecha de contribución: 07-may-2012
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