TRPA1
Zygmunt, Peter LU
and Högestätt, Edward
LU
(2014)
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:
https://lup.lub.lu.se/record/4429586
- author
- Zygmunt, Peter
LU
and Högestätt, Edward
LU
- organization
- publishing date
- 2014
- type
- Chapter in Book/Report/Conference proceeding
- publication status
- published
- subject
- host publication
- 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
- pmid:24756722
- 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
- 2016-04-04 14:05:47
- date last changed
- 2022-04-24 05:20:33
@inbook{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}},
booktitle = {{Mammalian Transient Receptor Potential (TRP) Cation Channels: Handbook of Experimental Pharmacology}},
editor = {{Nilius, Bernd and Flockerzi, Veit}},
isbn = {{9783642542152}},
language = {{eng}},
pages = {{583--630}},
title = {{TRPA1}},
url = {{http://dx.doi.org/10.1007/978-3-642-54215-2_23}},
doi = {{10.1007/978-3-642-54215-2_23}},
volume = {{I}},
year = {{2014}},
}