Home LiteratureArticle Details
PMID: 17568746 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Sensory neuron sodium channel Nav1.8 is essential for pain at low temperatures.

Nature ·Vol. 447 ·No. 7146 ·2007-06-14 ·Pages 855-8

Zimmermann K, Leffler A, Babes A, Cendan CM, Carr RW, Kobayashi J, Nau C, Wood JN, Reeh PW

Abstract

Sensory acuity and motor dexterity deteriorate when human limbs cool down, but pain perception persists and cold-induced pain can become excruciating. Evolutionary pressure to enforce protective behaviour requires that damage-sensing neurons (nociceptors) continue to function at low temperatures. Here we show that this goal is achieved by endowing superficial endings of slowly conducting nociceptive fibres with the tetrodotoxin-resistant voltage-gated sodium channel (VGSC) Na(v)1.8 (ref. 2). This channel is essential for sustained excitability of nociceptors when the skin is cooled. We show that cooling excitable membranes progressively enhances the voltage-dependent slow inactivation of tetrodotoxin-sensitive VGSCs. In contrast, the inactivation properties of Na(v)1.8 are entirely cold-resistant. Moreover, low temperatures decrease the activation threshold of the sodium currents and increase the membrane resistance, augmenting the voltage change caused by any membrane current. Thus, in the cold, Na(v)1.8 remains available as the sole electrical impulse generator in nociceptors that transmits nociceptive information to the central nervous system. Consistent with this concept is the observation that Na(v)1.8-null mutant mice show negligible responses to noxious cold and mechanical stimulation at low temperatures. Our data present strong evidence for a specialized role of Na(v)1.8 in nociceptors as the critical molecule for the perception of cold pain and pain in the cold.

MeSH Terms
Action Potentials/drug effects Animals Cold Temperature NAV1.8 Voltage-Gated Sodium Channel Neurons, Afferent/drug effects,metabolism Pain/metabolism,physiopathology Rats Rats, Wistar Sodium Channels/metabolism Tetrodotoxin/pharmacology
Chemicals
NAV1.8 Voltage-Gated Sodium Channel SCN10A protein, human Scn10a protein, mouse Scn10a protein, rat Sodium Channels Tetrodotoxin
Authors & Affiliations
9 authors, click to expand affiliations / ORCID
Zimmermann Katharina
Department of Physiology and Pathophysiology, Faculty of Medicine, Friedrich-Alexander University Erlangen-Nuremberg, 91054 Erlangen, Germany. [email protected]
Leffler Andreas
Babes Alexandru
Cendan Cruz Miguel
Carr Richard W
Kobayashi Jin-ichi
Nau Carla
Wood John N
Reeh Peter W
Article Info
Journal
Nature
Abbr.
Nature
ISSN
1476-4687
Published
2007-06-14
Pages
855-8
Language
English
Region
England
NLM ID
0410462
Subset
IM
Grants
Medical Research Council · G9717869 · United Kingdom
Wellcome Trust · United Kingdom
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]