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Modulation of TRPA1 thermal sensitivity enables sensory discrimination in Drosophila

Authors :
Paul A. Garrity
Marc A. T. Muskavitch
Alexandra M. Dainis
Elaine Chang
Adam M. Jenkins
Lina Ni
KyeongJin Kang
Vincent C. Panzano
Kimberly Regna
Source :
Nature
Publication Year :
2011

Abstract

Our bodies are constantly bombarded by a diversity of environmental stimuli, such as touch, taste, sound, smell, light, etc. To detect and process this broad array of signals, nature has evolved a variety of cellular sensory mechanisms and pathways that interface with the environment and transmit neural signals back to the CNS where they are translated into behavioral decisions. Transient Response Potential (TRP) cation channels were first identified in invertebrates (i.e., Drosophila) and represent a sizeable receptor/channel family in mammals, consisting of 28 individual members grouped into subclasses denoted TRPC, TRPV, TRPM, TRPML, TRPP and TRPA (for a recent review, see ref. 1). Although originally described as ion channels, we now know that many members of the TRP family also function as receptors for a range of stimuli, including temperature, pH, chemical compounds and membrane voltage. In fact, several TRP isoforms display multimodal sensitivity, meaning that they can respond to more than one stimulus. For example, TRPV1, or the capcaisin receptor, displays both thermal and chemical sensitivity, and the two stimuli may act synergistically to increase channel activity. Physiologically, TRP family members are expressed in a variety of sensory afferent nerves that feed environmental information to the CNS, and also in smaller C-type afferent fibers responsible for peripheral pain sensation and transmission. Therapeutically, manipulation of TRP channel activity may represent an effective strategy to treat peripheral pain associated with inflammation and chronic tissue injury.

Details

Language :
English
ISSN :
14764687 and 00280836
Volume :
481
Issue :
7379
Database :
OpenAIRE
Journal :
Nature
Accession number :
edsair.doi.dedup.....183631ff3684ca76493b6e27c1868ae5