PMID- 22791718
OWN - NLM
STAT- MEDLINE
DCOM- 20121119
LR  - 20220223
IS  - 1083-351X (Electronic)
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 287
IP  - 36
DP  - 2012 Aug 31
TI  - Analysis of transient receptor potential ankyrin 1 (TRPA1) in frogs and lizards 
      illuminates both nociceptive heat and chemical sensitivities and coexpression 
      with TRP vanilloid 1 (TRPV1) in ancestral vertebrates.
PG  - 30743-54
LID - 10.1074/jbc.M112.362194 [doi]
AB  - Transient receptor potential ankyrin 1 (TRPA1) and TRP vanilloid 1 (V1) perceive 
      noxious temperatures and chemical stimuli and are involved in pain sensation in 
      mammals. Thus, these two channels provide a model for understanding how different 
      genes with similar biological roles may influence the function of one another 
      during the course of evolution. However, the temperature sensitivity of TRPA1 in 
      ancestral vertebrates and its evolutionary path are unknown as its temperature 
      sensitivities vary among different vertebrate species. To elucidate the 
      functional evolution of TRPA1, TRPA1s of the western clawed (WC) frogs and green 
      anole lizards were characterized. WC frog TRPA1 was activated by heat and noxious 
      chemicals that activate mammalian TRPA1. These stimuli also activated native 
      sensory neurons and elicited nocifensive behaviors in WC frogs. Similar to 
      mammals, TRPA1 was functionally co-expressed with TRPV1, another heat- and 
      chemical-sensitive nociceptive receptor, in native sensory neurons of the WC 
      frog. Green anole TRPA1 was also activated by heat and noxious chemical 
      stimulation. These results suggest that TRPA1 was likely a noxious heat and 
      chemical receptor and co-expressed with TRPV1 in the nociceptive sensory neurons 
      of ancestral vertebrates. Conservation of TRPV1 heat sensitivity throughout 
      vertebrate evolution could have changed functional constraints on TRPA1 and 
      influenced the functional evolution of TRPA1 regarding temperature sensitivity, 
      whereas conserving its noxious chemical sensitivity. In addition, our results 
      also demonstrated that two mammalian TRPA1 inhibitors elicited different effect 
      on the TRPA1s of WC frogs and green anoles, which can be utilized to clarify the 
      structural bases for inhibition of TRPA1.
FAU - Saito, Shigeru
AU  - Saito S
AD  - Division of Cell Signaling, Okazaki Institute for Integrative Bioscience 
      (National Institute for Physiological Sciences), National Institute of Natural 
      Sciences, Okazaki, Aichi, 444-8787, Japan. sshigeru@nips.ac.jp
FAU - Nakatsuka, Kazumasa
AU  - Nakatsuka K
FAU - Takahashi, Kenji
AU  - Takahashi K
FAU - Fukuta, Naomi
AU  - Fukuta N
FAU - Imagawa, Toshiaki
AU  - Imagawa T
FAU - Ohta, Toshio
AU  - Ohta T
FAU - Tominaga, Makoto
AU  - Tominaga M
LA  - eng
SI  - GENBANK/AB693189
SI  - GENBANK/AB693190
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20120712
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (TRPV Cation Channels)
RN  - 0 (TRPV1 protein, Xenopus)
RN  - 0 (Xenopus Proteins)
SB  - IM
MH  - Animals
MH  - Base Sequence
MH  - Cloning, Molecular
MH  - *Evolution, Molecular
MH  - Gene Expression Regulation/*physiology
MH  - Hot Temperature
MH  - Humans
MH  - Lizards
MH  - Mice
MH  - Molecular Sequence Data
MH  - Nociception/*physiology
MH  - Rats
MH  - *TRPV Cation Channels/genetics/metabolism
MH  - Xenopus
MH  - *Xenopus Proteins/genetics/metabolism
PMC - PMC3436318
EDAT- 2012/07/14 06:00
MHDA- 2012/12/10 06:00
PMCR- 2013/08/31
CRDT- 2012/07/14 06:00
PHST- 2012/07/14 06:00 [entrez]
PHST- 2012/07/14 06:00 [pubmed]
PHST- 2012/12/10 06:00 [medline]
PHST- 2013/08/31 00:00 [pmc-release]
AID - S0021-9258(20)63173-8 [pii]
AID - M112.362194 [pii]
AID - 10.1074/jbc.M112.362194 [doi]
PST - ppublish
SO  - J Biol Chem. 2012 Aug 31;287(36):30743-54. doi: 10.1074/jbc.M112.362194. Epub 
      2012 Jul 12.