Cold sensitivity of TRPA1 is unveiled by the prolyl hydroxylation blockade-induced sensitization to ROS

The transient receptor potential ankyrin 1 (TRPA1) is a cation channel that is involved in nociceptive pain sensing. Here, the authors show that hydroxylation of a proline in the N terminus of TRPA1 renders it sensitive to reactive oxygen species resulting from noxious cold.

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Autores principales:	Takahito Miyake, Saki Nakamura, Meng Zhao, Kanako So, Keisuke Inoue, Tomohiro Numata, Nobuaki Takahashi, Hisashi Shirakawa, Yasuo Mori, Takayuki Nakagawa, Shuji Kaneko
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/918799dc010744d1bfbd4954e4daa919
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spelling	oai:doaj.org-article:918799dc010744d1bfbd4954e4daa9192021-12-02T14:39:30ZCold sensitivity of TRPA1 is unveiled by the prolyl hydroxylation blockade-induced sensitization to ROS10.1038/ncomms128402041-1723https://doaj.org/article/918799dc010744d1bfbd4954e4daa9192016-09-01T00:00:00Zhttps://doi.org/10.1038/ncomms12840https://doaj.org/toc/2041-1723The transient receptor potential ankyrin 1 (TRPA1) is a cation channel that is involved in nociceptive pain sensing. Here, the authors show that hydroxylation of a proline in the N terminus of TRPA1 renders it sensitive to reactive oxygen species resulting from noxious cold.Takahito MiyakeSaki NakamuraMeng ZhaoKanako SoKeisuke InoueTomohiro NumataNobuaki TakahashiHisashi ShirakawaYasuo MoriTakayuki NakagawaShuji KanekoNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-10 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Takahito Miyake Saki Nakamura Meng Zhao Kanako So Keisuke Inoue Tomohiro Numata Nobuaki Takahashi Hisashi Shirakawa Yasuo Mori Takayuki Nakagawa Shuji Kaneko Cold sensitivity of TRPA1 is unveiled by the prolyl hydroxylation blockade-induced sensitization to ROS
description	The transient receptor potential ankyrin 1 (TRPA1) is a cation channel that is involved in nociceptive pain sensing. Here, the authors show that hydroxylation of a proline in the N terminus of TRPA1 renders it sensitive to reactive oxygen species resulting from noxious cold.
format	article
author	Takahito Miyake Saki Nakamura Meng Zhao Kanako So Keisuke Inoue Tomohiro Numata Nobuaki Takahashi Hisashi Shirakawa Yasuo Mori Takayuki Nakagawa Shuji Kaneko
author_facet	Takahito Miyake Saki Nakamura Meng Zhao Kanako So Keisuke Inoue Tomohiro Numata Nobuaki Takahashi Hisashi Shirakawa Yasuo Mori Takayuki Nakagawa Shuji Kaneko
author_sort	Takahito Miyake
title	Cold sensitivity of TRPA1 is unveiled by the prolyl hydroxylation blockade-induced sensitization to ROS
title_short	Cold sensitivity of TRPA1 is unveiled by the prolyl hydroxylation blockade-induced sensitization to ROS
title_full	Cold sensitivity of TRPA1 is unveiled by the prolyl hydroxylation blockade-induced sensitization to ROS
title_fullStr	Cold sensitivity of TRPA1 is unveiled by the prolyl hydroxylation blockade-induced sensitization to ROS
title_full_unstemmed	Cold sensitivity of TRPA1 is unveiled by the prolyl hydroxylation blockade-induced sensitization to ROS
title_sort	cold sensitivity of trpa1 is unveiled by the prolyl hydroxylation blockade-induced sensitization to ros
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/918799dc010744d1bfbd4954e4daa919
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Cold sensitivity of TRPA1 is unveiled by the prolyl hydroxylation blockade-induced sensitization to ROS

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