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Subcellular localization of the K+ channel subunit Kv3.1b in selected rat CNS neurons.
Brain Res. 1997 Aug 22; 766(1-2):173-87.BR

Abstract

Voltage-gated potassium channels constitute the largest group of heteromeric ion channels discovered to date. Over 20 genes have been isolated, encoding different channel subunit proteins which form functional tetrameric K+ channels. We have analyzed the subcellular localization of subunit Kv3.1b, a member of the Kv3 (Shaw-like) subfamily, in rat brain at the light and electron microscopic level, using immunocytochemical detection. Detailed localization was carried out in specific neurons of the neocortex, hippocampus and cerebellum. The identity of Kv3.1b-positive neurons was established using double labeling with markers for specific neuronal populations. In the neocortex, the Kv3.1b subunit was expressed in most parvalbumin-containing bipolar, basket or chandelier cells, and in some bipolar or double bouquet neurons containing calbindin. In the hippocampus, Kv3.1b was expressed in many parvalbumin-containing basket cells, as well as in calbindin-positive neurons in the stratum oriens, and in a small number of interneurons that did not stain for either parvalbumin or calbindin. Kv3.1b protein was not present in pyramidal cells in the neocortex and the hippocampus, but these cells were outlined by labeled presynaptic terminals from interneuron axons that surround the postsynaptic cell. In the cerebellar cortex, granule cells were the only population expressing the channel protein. Careful examination of individual granule cells revealed a non-uniform distribution of Kv3.1 staining on the somata: circular bands of labeling were present in the vicinity of the axon hillock. In cortical and hippocampal interneurons, as well as in cerebellar granule cells, the Kv3.1b subunit was present in somatic and unmyelinated axonal membranes and adjacent cytoplasm, as well as in the most proximal portion of dendritic processes, but not throughout most of the dendrite. Labeling was also seen in the terminals of labeled axons, but not at a higher concentration than in other parts of the axon. The distribution in the cells analyzed supports a role in action potential transmission by regulating action potential duration.

Authors+Show Affiliations

Department of Neuroscience, University of California at San Diego, La Jolla 92092, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

9359601

Citation

Sekirnjak, C, et al. "Subcellular Localization of the K+ Channel Subunit Kv3.1b in Selected Rat CNS Neurons." Brain Research, vol. 766, no. 1-2, 1997, pp. 173-87.
Sekirnjak C, Martone ME, Weiser M, et al. Subcellular localization of the K+ channel subunit Kv3.1b in selected rat CNS neurons. Brain Res. 1997;766(1-2):173-87.
Sekirnjak, C., Martone, M. E., Weiser, M., Deerinck, T., Bueno, E., Rudy, B., & Ellisman, M. (1997). Subcellular localization of the K+ channel subunit Kv3.1b in selected rat CNS neurons. Brain Research, 766(1-2), 173-87.
Sekirnjak C, et al. Subcellular Localization of the K+ Channel Subunit Kv3.1b in Selected Rat CNS Neurons. Brain Res. 1997 Aug 22;766(1-2):173-87. PubMed PMID: 9359601.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Subcellular localization of the K+ channel subunit Kv3.1b in selected rat CNS neurons. AU - Sekirnjak,C, AU - Martone,M E, AU - Weiser,M, AU - Deerinck,T, AU - Bueno,E, AU - Rudy,B, AU - Ellisman,M, PY - 1997/8/22/pubmed PY - 1997/11/14/medline PY - 1997/8/22/entrez SP - 173 EP - 87 JF - Brain research JO - Brain Res VL - 766 IS - 1-2 N2 - Voltage-gated potassium channels constitute the largest group of heteromeric ion channels discovered to date. Over 20 genes have been isolated, encoding different channel subunit proteins which form functional tetrameric K+ channels. We have analyzed the subcellular localization of subunit Kv3.1b, a member of the Kv3 (Shaw-like) subfamily, in rat brain at the light and electron microscopic level, using immunocytochemical detection. Detailed localization was carried out in specific neurons of the neocortex, hippocampus and cerebellum. The identity of Kv3.1b-positive neurons was established using double labeling with markers for specific neuronal populations. In the neocortex, the Kv3.1b subunit was expressed in most parvalbumin-containing bipolar, basket or chandelier cells, and in some bipolar or double bouquet neurons containing calbindin. In the hippocampus, Kv3.1b was expressed in many parvalbumin-containing basket cells, as well as in calbindin-positive neurons in the stratum oriens, and in a small number of interneurons that did not stain for either parvalbumin or calbindin. Kv3.1b protein was not present in pyramidal cells in the neocortex and the hippocampus, but these cells were outlined by labeled presynaptic terminals from interneuron axons that surround the postsynaptic cell. In the cerebellar cortex, granule cells were the only population expressing the channel protein. Careful examination of individual granule cells revealed a non-uniform distribution of Kv3.1 staining on the somata: circular bands of labeling were present in the vicinity of the axon hillock. In cortical and hippocampal interneurons, as well as in cerebellar granule cells, the Kv3.1b subunit was present in somatic and unmyelinated axonal membranes and adjacent cytoplasm, as well as in the most proximal portion of dendritic processes, but not throughout most of the dendrite. Labeling was also seen in the terminals of labeled axons, but not at a higher concentration than in other parts of the axon. The distribution in the cells analyzed supports a role in action potential transmission by regulating action potential duration. SN - 0006-8993 UR - https://www.unboundmedicine.com/medline/citation/9359601/Subcellular_localization_of_the_K+_channel_subunit_Kv3_1b_in_selected_rat_CNS_neurons_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-8993(97)00527-1 DB - PRIME DP - Unbound Medicine ER -