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TRPA1

Zygmunt, Peter LU and Högestätt, Edward LU (2014) In Mammalian Transient Receptor Potential (TRP) Cation Channels: Handbook of Experimental Pharmacology I. p.583-630
Abstract
The transient receptor potential ankyrin subtype 1 protein (TRPA1) is a nonselective cation channel permeable to Ca(2+), Na(+), and K(+). TRPA1 is a promiscuous chemical nocisensor that is also involved in noxious cold and mechanical sensation. It is present in a subpopulation of Aδ- and C-fiber nociceptive sensory neurons as well as in other sensory cells including epithelial cells. In primary sensory neurons, Ca(2+) and Na(+) flowing through TRPA1 into the cell cause membrane depolarization, action potential discharge, and neurotransmitter release both at peripheral and central neural projections. In addition to being activated by cysteine and lysine reactive electrophiles and oxidants, TRPA1 is indirectly activated by pro-inflammatory... (More)
The transient receptor potential ankyrin subtype 1 protein (TRPA1) is a nonselective cation channel permeable to Ca(2+), Na(+), and K(+). TRPA1 is a promiscuous chemical nocisensor that is also involved in noxious cold and mechanical sensation. It is present in a subpopulation of Aδ- and C-fiber nociceptive sensory neurons as well as in other sensory cells including epithelial cells. In primary sensory neurons, Ca(2+) and Na(+) flowing through TRPA1 into the cell cause membrane depolarization, action potential discharge, and neurotransmitter release both at peripheral and central neural projections. In addition to being activated by cysteine and lysine reactive electrophiles and oxidants, TRPA1 is indirectly activated by pro-inflammatory agents via the phospholipase C signaling pathway, in which cytosolic Ca(2+) is an important regulator of channel gating. The finding that non-electrophilic compounds, including menthol and cannabinoids, activate TRPA1 may provide templates for the design of non-tissue damaging activators to fine-tune the activity of TRPA1 and raises the possibility that endogenous ligands sharing binding sites with such non-electrophiles exist and regulate TRPA1 channel activity. TRPA1 is promising as a drug target for novel treatments of pain, itch, and sensory hyperreactivity in visceral organs including the airways, bladder, and gastrointestinal tract. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Chapter in Book/Report/Conference proceeding
publication status
published
subject
in
Mammalian Transient Receptor Potential (TRP) Cation Channels: Handbook of Experimental Pharmacology
editor
Nilius, Bernd and Flockerzi, Veit
volume
I
pages
583 - 630
external identifiers
  • PMID:24756722
  • Scopus:84904476162
ISBN
9783642542152
DOI
10.1007/978-3-642-54215-2_23
language
English
LU publication?
yes
id
49c84e24-f468-436a-84e6-39f13b2626ec (old id 4429586)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/24756722?dopt=Abstract
date added to LUP
2014-05-04 15:08:36
date last changed
2016-12-04 04:48:31
@misc{49c84e24-f468-436a-84e6-39f13b2626ec,
  abstract     = {The transient receptor potential ankyrin subtype 1 protein (TRPA1) is a nonselective cation channel permeable to Ca(2+), Na(+), and K(+). TRPA1 is a promiscuous chemical nocisensor that is also involved in noxious cold and mechanical sensation. It is present in a subpopulation of Aδ- and C-fiber nociceptive sensory neurons as well as in other sensory cells including epithelial cells. In primary sensory neurons, Ca(2+) and Na(+) flowing through TRPA1 into the cell cause membrane depolarization, action potential discharge, and neurotransmitter release both at peripheral and central neural projections. In addition to being activated by cysteine and lysine reactive electrophiles and oxidants, TRPA1 is indirectly activated by pro-inflammatory agents via the phospholipase C signaling pathway, in which cytosolic Ca(2+) is an important regulator of channel gating. The finding that non-electrophilic compounds, including menthol and cannabinoids, activate TRPA1 may provide templates for the design of non-tissue damaging activators to fine-tune the activity of TRPA1 and raises the possibility that endogenous ligands sharing binding sites with such non-electrophiles exist and regulate TRPA1 channel activity. TRPA1 is promising as a drug target for novel treatments of pain, itch, and sensory hyperreactivity in visceral organs including the airways, bladder, and gastrointestinal tract.},
  author       = {Zygmunt, Peter and Högestätt, Edward},
  editor       = {Nilius, Bernd and Flockerzi, Veit},
  isbn         = {9783642542152},
  language     = {eng},
  pages        = {583--630},
  series       = {Mammalian Transient Receptor Potential (TRP) Cation Channels: Handbook of Experimental Pharmacology},
  title        = {TRPA1},
  url          = {http://dx.doi.org/10.1007/978-3-642-54215-2_23},
  volume       = {I},
  year         = {2014},
}