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

被引:30
|
作者
Sanchez-Ponce, Diana [1 ,2 ,3 ,4 ]
DeFelipe, Javier [2 ,3 ,5 ]
Jose Garrido, Juan [1 ,5 ]
Munoz, Alberto [2 ,3 ,4 ]
机构
[1] CSIC, Inst Cajal, Dept Mol Cellular & Dev Neurobiol, Madrid, Spain
[2] CSIC, Inst Cajal, Dept Funct & Syst Neurobiol, Madrid, Spain
[3] Univ Politecn Madrid, Lab Cajal Circuitos Cort, Ctr Tecnol Biomed, Madrid, Spain
[4] Univ Complutense, Dept Cell Biol, E-28040 Madrid, Spain
[5] Ctr Invest Biomed Red Enfermedades Neurodegenerat, Madrid, Spain
来源
PLOS ONE | 2012年 / 7卷 / 10期
关键词
ACTION-POTENTIAL INITIATION; KV2.1 K+ CHANNEL; GATED ION CHANNELS; KAPPA-B-ALPHA; DELAYED RECTIFIER; SODIUM-CHANNELS; KCNQ CHANNELS; ANKYRIN-G; MOLECULAR RELATIONSHIPS; INTERNATIONAL-UNION;
D O I
10.1371/journal.pone.0048557
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
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页数:14
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