Human and Mouse TRPA1 Are Heat and Cold Sensors Differentially Tuned by Voltage

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985823%3A_____%2F20%3A00524175" target="_blank" >RIV/67985823:_____/20:00524175 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216208:11310/20:10420691 RIV/00216208:11320/20:10420691

Výsledek na webu

<a href="https://www.mdpi.com/2073-4409/9/1/57" target="_blank" >https://www.mdpi.com/2073-4409/9/1/57</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.3390/cells9010057" target="_blank" >10.3390/cells9010057</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Human and Mouse TRPA1 Are Heat and Cold Sensors Differentially Tuned by Voltage

Popis výsledku v původním jazyce

Transient receptor potential ankyrin 1 channel (TRPA1) serves as a key sensor for reactive electrophilic compounds across all species. Its sensitivity to temperature, however, differs among species, a variability that has been attributed to an evolutionary divergence. Mouse TRPA1 was implicated in noxious cold detection but was later also identified as one of the prime noxious heat sensors. Moreover, human TRPA1, originally considered to be temperature-insensitive, turned out to act as an intrinsic bidirectional thermosensor that is capable of sensing both cold and heat. Using electrophysiology and modeling, we compare the properties of human and mouse TRPA1, and we demonstrate that both orthologues are activated by heat, and their kinetically distinct components of voltage-dependent gating are differentially modulated by heat and cold. Furthermore, we show that both orthologues can be strongly activated by cold after the concurrent application of voltage and heat. We propose an allosteric mechanism that could account for the variability in TRPA1 temperature responsiveness.

Název v anglickém jazyce

Human and Mouse TRPA1 Are Heat and Cold Sensors Differentially Tuned by Voltage

Popis výsledku anglicky

Transient receptor potential ankyrin 1 channel (TRPA1) serves as a key sensor for reactive electrophilic compounds across all species. Its sensitivity to temperature, however, differs among species, a variability that has been attributed to an evolutionary divergence. Mouse TRPA1 was implicated in noxious cold detection but was later also identified as one of the prime noxious heat sensors. Moreover, human TRPA1, originally considered to be temperature-insensitive, turned out to act as an intrinsic bidirectional thermosensor that is capable of sensing both cold and heat. Using electrophysiology and modeling, we compare the properties of human and mouse TRPA1, and we demonstrate that both orthologues are activated by heat, and their kinetically distinct components of voltage-dependent gating are differentially modulated by heat and cold. Furthermore, we show that both orthologues can be strongly activated by cold after the concurrent application of voltage and heat. We propose an allosteric mechanism that could account for the variability in TRPA1 temperature responsiveness.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

30103 - Neurosciences (including psychophysiology)

Projekt

<a href="/cs/project/GA19-03777S" target="_blank" >GA19-03777S: Molekulární mechanizmy regulace teplotně citlivých TRP iontových kanálů v nociceptivních neuronech</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2020

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Cells

ISSN

2073-4409

e-ISSN

—

Svazek periodika

9

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

CH - Švýcarská konfederace

Počet stran výsledku

24

Strana od-do

57

Kód UT WoS článku

000515398200057

EID výsledku v databázi Scopus

2-s2.0-85090250045