Functional role of the C-terminus of voltage-gated sodium channel Na v1.8

Jin Sung Choi; Lynda Tyrrell; Stephen G. Waxman; Sulayman D. Dib-Hajj

doi:10.1016/j.febslet.2004.07.047

Functional role of the C-terminus of voltage-gated sodium channel Na _v1.8

Jin Sung Choi
, Lynda Tyrrell
, Stephen G. Waxman
, Sulayman D. Dib-Hajj

Pharmacy

Yale University
Department of Veterans Affairs

Research output: Contribution to journal › Article › peer-review

22 Scopus citations

Abstract

Sodium channel Na_v1.8 requires stronger depolarization than other sodium channels for activation and inactivation. The contribution of Na_v1.8 C-terminus to this property was investigated by producing Na_v1.8 and Na_v1.4 chimeras and expressing them in ND7/23 cells. Current densities of the chimeras were significantly different than in parental channels, and the voltage-dependence of activation was depolarized in Na_v1.4/1.8C compared to Na_v1.4. Analysis of steady-state inactivation showed that only Na_v1.8 and Na_v1.4/1.8C currents demonstrate a non-inactivated fraction. Thus, the C-terminus of Na _v1.8 contributes to regulation of channel density at the cell surface, modulates channel gating, and regulates the generation of sustained current.

Original language	English
Pages (from-to)	256-260
Number of pages	5
Journal	FEBS Letters
Volume	572
Issue number	1-3
DOIs	https://doi.org/10.1016/j.febslet.2004.07.047
State	Published - 13 Aug 2004

Bibliographical note

Funding Information:
We thank Drs. Tony Rush and Ted Cummins for valuable discussions, and Youping Zhao and Bart Toftness for technical assistance. This work was supported in part by grants from the National Multiple Sclerosis Society and the Rehabilitation Research Service and Medical Research Service, Department of Veterans Affairs. The Center for Neuroscience and Regeneration Research is a Collaboration of the Paralyzed Veterans of America and the United Spinal Association with Yale University.

Keywords

Na1.8
Sodium channel
Voltage-gated sodium channel

Access to Document

10.1016/j.febslet.2004.07.047

Cite this

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title = "Functional role of the C-terminus of voltage-gated sodium channel Na v1.8",

abstract = "Sodium channel Nav1.8 requires stronger depolarization than other sodium channels for activation and inactivation. The contribution of Nav1.8 C-terminus to this property was investigated by producing Nav1.8 and Nav1.4 chimeras and expressing them in ND7/23 cells. Current densities of the chimeras were significantly different than in parental channels, and the voltage-dependence of activation was depolarized in Nav1.4/1.8C compared to Nav1.4. Analysis of steady-state inactivation showed that only Nav1.8 and Nav1.4/1.8C currents demonstrate a non-inactivated fraction. Thus, the C-terminus of Na v1.8 contributes to regulation of channel density at the cell surface, modulates channel gating, and regulates the generation of sustained current.",

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author = "Choi, \{Jin Sung\} and Lynda Tyrrell and Waxman, \{Stephen G.\} and Dib-Hajj, \{Sulayman D.\}",

note = "Funding Information: We thank Drs. Tony Rush and Ted Cummins for valuable discussions, and Youping Zhao and Bart Toftness for technical assistance. This work was supported in part by grants from the National Multiple Sclerosis Society and the Rehabilitation Research Service and Medical Research Service, Department of Veterans Affairs. The Center for Neuroscience and Regeneration Research is a Collaboration of the Paralyzed Veterans of America and the United Spinal Association with Yale University.",

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AU - Tyrrell, Lynda

AU - Waxman, Stephen G.

AU - Dib-Hajj, Sulayman D.

N1 - Funding Information: We thank Drs. Tony Rush and Ted Cummins for valuable discussions, and Youping Zhao and Bart Toftness for technical assistance. This work was supported in part by grants from the National Multiple Sclerosis Society and the Rehabilitation Research Service and Medical Research Service, Department of Veterans Affairs. The Center for Neuroscience and Regeneration Research is a Collaboration of the Paralyzed Veterans of America and the United Spinal Association with Yale University.

PY - 2004/8/13

Y1 - 2004/8/13

N2 - Sodium channel Nav1.8 requires stronger depolarization than other sodium channels for activation and inactivation. The contribution of Nav1.8 C-terminus to this property was investigated by producing Nav1.8 and Nav1.4 chimeras and expressing them in ND7/23 cells. Current densities of the chimeras were significantly different than in parental channels, and the voltage-dependence of activation was depolarized in Nav1.4/1.8C compared to Nav1.4. Analysis of steady-state inactivation showed that only Nav1.8 and Nav1.4/1.8C currents demonstrate a non-inactivated fraction. Thus, the C-terminus of Na v1.8 contributes to regulation of channel density at the cell surface, modulates channel gating, and regulates the generation of sustained current.

AB - Sodium channel Nav1.8 requires stronger depolarization than other sodium channels for activation and inactivation. The contribution of Nav1.8 C-terminus to this property was investigated by producing Nav1.8 and Nav1.4 chimeras and expressing them in ND7/23 cells. Current densities of the chimeras were significantly different than in parental channels, and the voltage-dependence of activation was depolarized in Nav1.4/1.8C compared to Nav1.4. Analysis of steady-state inactivation showed that only Nav1.8 and Nav1.4/1.8C currents demonstrate a non-inactivated fraction. Thus, the C-terminus of Na v1.8 contributes to regulation of channel density at the cell surface, modulates channel gating, and regulates the generation of sustained current.

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KW - Voltage-gated sodium channel

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