Developmental Expression of Kv Potassium Channels at the Axon Initial Segment of Cultured Hippocampal Neurons

Sánchez-Ponce, Diana; Felipe Oroquieta, Javier de; Garrido, Juan José y Muñoz Céspedes, Alberto (2012). Developmental Expression of Kv Potassium Channels at the Axon Initial Segment of Cultured Hippocampal Neurons. "Plos One", v. 7 (n. 10); pp.. ISSN 1932-6203. https://doi.org/10.1371/journal.pone.0048557.

Descripción

Título: Developmental Expression of Kv Potassium Channels at the Axon Initial Segment of Cultured Hippocampal Neurons
Autor/es:
  • Sánchez-Ponce, Diana
  • Felipe Oroquieta, Javier de
  • Garrido, Juan José
  • Muñoz Céspedes, Alberto
Tipo de Documento: Artículo
Título de Revista/Publicación: Plos One
Fecha: 2012
Volumen: 7
Materias:
Escuela: Centro de Tecnología Biomédica (CTB) (UPM)
Departamento: Otro
Licencias Creative Commons: Reconocimiento - Sin obra derivada - No comercial

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Resumen

Axonal outgrowth and the formation of the axon initial segment (AIS) are early events in the acquisition of neuronal polarity. The AIS is characterized by a high concentration of voltage-dependent sodium and potassium channels. However, the specific ion channel subunits present and their precise localization in this axonal subdomain vary both during development and among the types of neurons, probably determining their firing characteristics in response to stimulation. Here, we characterize the developmental expression of different subfamilies of voltage-gated potassium channels in the AISs of cultured mouse hippocampal neurons, including subunits Kv1.2, Kv2.2 and Kv7.2. In contrast to the early appearance of voltage-gated sodium channels and the Kv7.2 subunit at the AIS, Kv1.2 and Kv2.2 subunits were tethered at the AIS only after 10 days in vitro. Interestingly, we observed different patterns of Kv1.2 and Kv2.2 subunit expression, with each confined to distinct neuronal populations. The accumulation of Kv1.2 and Kv2.2 subunits at the AIS was dependent on ankyrin G tethering, it was not affected by disruption of the actin cytoskeleton and it was resistant to detergent extraction, as described previously for other AIS proteins. This distribution of potassium channels in the AIS further emphasizes the heterogeneity of this structure in different neuronal populations, as proposed previously, and suggests corresponding differences in action potential regulation.

Más información

ID de Registro: 19828
Identificador DC: http://oa.upm.es/19828/
Identificador OAI: oai:oa.upm.es:19828
Identificador DOI: 10.1371/journal.pone.0048557
URL Oficial: http://www.plosone.org/article/info:doi/10.1371/journal.pone.0048557
Depositado por: Memoria Investigacion
Depositado el: 11 Oct 2013 16:16
Ultima Modificación: 21 Abr 2016 21:24
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