Infrared Snake Eyes: TRPA1 and the Thermal Sensitivity of the Snake Pit Organ

Panzano, Vincent C.; Kang, Kyung-In; Garrity, Paul

doi:10.1126/scisignal.3127pe22

Cited by 27 publications

(18 citation statements)

References 26 publications

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“…Several TRP channels have recently been proposed as thermosensors, of which the majority is involved in warm sensation (1)(2)(3)39). However, to define a TRP channel as a thermosensor would require examination of the purified channel protein in a defined membrane environment, and to date, only rat TRPM8 and rat TRPV1 have been shown to be intrinsically thermosensitive proteins (4,5).…”

Section: Discussionmentioning

confidence: 99%

“…cold sensing | irritants | pain | sensory neuron | TRP channels A number of vertebrate and invertebrate transient receptor potential (TRP) ion channels have been implicated in temperature sensation (1)(2)(3), but only the rat menthol receptor TRP subtype M8 (TRPM8) and the rat capsaicin receptor TRP subtype V1 (TRPV1) have been shown to possess intrinsic thermosensitivity (4,5). In 2003, Story et al (6) proposed that the mouse TRPA1 is a noxious cold sensor.…”

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confidence: 99%

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Human TRPA1 is intrinsically cold- and chemosensitive with and without its N-terminal ankyrin repeat domain

Moparthi

Survery

Kreir

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

137

162

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We have purified and reconstituted human transient receptor potential (TRP) subtype A1 (hTRPA1) into lipid bilayers and recorded single-channel currents to understand its inherent thermo-and chemosensory properties as well as the role of the ankyrin repeat domain (ARD) of the N terminus in channel behavior. We report that hTRPA1 with and without its N-terminal ARD (Δ1-688 hTRPA1) is intrinsically cold-sensitive, and thus, cold-sensing properties of hTRPA1 reside outside the N-terminal ARD. We show activation of hTRPA1 by the thiol oxidant 2-((biotinoyl)amino)ethyl methanethiosulfonate (MTSEA-biotin) and that electrophilic compounds activate hTRPA1 in the presence and absence of the N-terminal ARD. The nonelectrophilic compounds menthol and the cannabinoid Δ 9 -tetrahydrocannabiorcol (C16) directly activate hTRPA1 at different sites independent of the N-terminal ARD. The TRPA1 antagonist HC030031 inhibited cold and chemical activation of hTRPA1 and Δ1-688 hTRPA1, supporting a direct interaction with hTRPA1 outside the N-terminal ARD. These findings show that hTRPA1 is an intrinsically cold-and chemosensitive ion channel. Thus, second messengers, including Ca 2+ , or accessory proteins are not needed for hTRPA1 responses to cold or chemical activators. We suggest that conformational changes outside the N-terminal ARD by cold, electrophiles, and nonelectrophiles are important in hTRPA1 channel gating and that targeting chemical interaction sites outside the N-terminal ARD provides possibilities to fine tune TRPA1-based drug therapies (e.g., for treatment of pain associated with cold hypersensitivity and cardiovascular disease).cold sensing | irritants | pain | sensory neuron | TRP channels A number of vertebrate and invertebrate transient receptor potential (TRP) ion channels have been implicated in temperature sensation (1-3), but only the rat menthol receptor TRP subtype M8 (TRPM8) and the rat capsaicin receptor TRP subtype V1 (TRPV1) have been shown to possess intrinsic thermosensitivity (4, 5). In 2003, Story et al. (6) proposed that the mouse TRPA1 is a noxious cold sensor. Story et al. (6) showed that TRPA1 was present in nociceptive primary sensory neurons and that CHO cells heterologously expressing the mouse TRPA1 displayed cold sensitivity. Most subsequent studies of cold responses in heterologous TRPA1 expression systems, isolated primary sensory neurons, and whole animals have provided evidence in support of mouse and rat TRPA1 being involved in noxious cold transduction (7). Interestingly, a familial episodic pain syndrome triggered by cold is caused by a gain-of-function mutation in the TRPA1 gene, indicating that TRPA1 may have a key role in human noxious cold sensation (8). Thus, human TRPA1 (hTRPA1) may be a relevant drug target for treatment of this condition and other pathological conditions, such as inflammation, nerve injury, and chemotherapy-induced neuropathy, that are characterized by TRPA1-dependent cold allodynia or hypersensitivity (7). However, in vitro studies of the expressed hTRPA1 h...

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Human TRPA1 is intrinsically cold- and chemosensitive with and without its N-terminal ankyrin repeat domain

Moparthi

Survery

Kreir

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

137

162

View full text Add to dashboard Cite

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“…Several TRPA1 homologues exist in the animal kingdom, and the ability of TRPA1 to sense potentially harmful electrophilic compounds has been conserved for ϳ500 million years, whereas the ancestral thermosensitive properties of TRPA1 are unclear and diverged later (5,11). A role for mammalian TRPA1, and especially the human TRPA1 (hTRPA1), as noxious cold sensors has been controversial ever since it was proposed (13), whereas the heat-sensitive role of TRPA1 homologues in non-mammalians has been easily accepted (5,10).…”

mentioning

confidence: 99%

The N-terminal Ankyrin Repeat Domain Is Not Required for Electrophile and Heat Activation of the Purified Mosquito TRPA1 Receptor

Survery

Moparthi

Kjellbom

et al. 2016

Journal of Biological Chemistry

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Temperature sensors are crucial for animals to optimize living conditions. The temperature response of the ion channel transient receptor potential A1 (TRPA1) is intriguing; some orthologs have been reported to be activated by cold and others by heat, but the molecular mechanisms responsible for its activation remain elusive. Single-channel electrophysiological recordings of heterologously expressed and purified Anopheles gambiae TRPA1 (AgTRPA1), with and without the N-terminal ankyrin repeat domain, demonstrate that both proteins are functional because they responded to the electrophilic compounds allyl isothiocyanate and cinnamaldehyde as well as heat. The proteins' similar intrinsic fluorescence properties and corresponding quenching when activated by allyl isothiocyanate or heat suggest lipid bilayer-independent conformational changes outside the N-terminal domain. The results show that Ag-TRPA1 is an inherent thermo-and chemoreceptor, and analogous to what has been reported for the human TRPA1 ortholog, the N-terminal domain may tune the response but is not required for the activation by these stimuli.

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“…Esse canal está localizado nos neurônios das fossetas e produz de 100 a 400 vezes mais RNA no gânglio trigêmeo do que nos gânglios dorsais (que são responsáveis de fornecer ao cérebro a informação sensorial que provém do pescoço para baixo). Quando a radiação atinge a fosseta loreal, aquece a membrana localizada na fosseta e consequentemente o canal TRPA1, que se abre quando um limiar de temperatura é alcançado (27.6°C), (5,10,14,18) permitindo que os íons fluam para os neurônios, desencadeando assim o impulso nervoso.…”

Section: Cascavéisunclassified

“…(14,18) Este canal (TRPA1) em humanos (e mamíferos em geral) é o responsável por alertar o sistema sobre dores inflamatórias e detectar irritantes químicos nocivos ao corpo. (14,18) A fosseta loreal da cobra é caracterizada por uma cavidade, ou seja, um recinto fechado no qual há um pequeno furo, em que toda a radiação incidente é absorvida e as reflexões existentes se transformam em praticamente uma absorção completa.…”

Section: Cascavéisunclassified

Desenvolvimento de estímulos dinâmicos térmicos para análise do sistema sensorial infravermelho em serpentes

Batista¹,

Slaets²

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The present work describe a creation of an experimental environment capable of measuring the neural response of vision (thermal) -in snakes -when stimulated by infrared radiation.There will be a creation of artificial dynamic stimuli of which the temperature and displacement velocity can be controlled. The response of the snake, when presented to these stimuli, captured directly from the brain (tecto optic), which corresponds to visual and infrared process in the central nervous system of the rattlesnake. We showed that with these stimuli created, it is possible to obtain experimental data which will allow analysis of sensitivity of the infrared sensory system in relation to contrast in temperature and speed of movement of false prey.

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Infrared Snake Eyes: TRPA1 and the Thermal Sensitivity of the Snake Pit Organ

Cited by 27 publications

References 26 publications

Human TRPA1 is intrinsically cold- and chemosensitive with and without its N-terminal ankyrin repeat domain

Human TRPA1 is intrinsically cold- and chemosensitive with and without its N-terminal ankyrin repeat domain

The N-terminal Ankyrin Repeat Domain Is Not Required for Electrophile and Heat Activation of the Purified Mosquito TRPA1 Receptor

Desenvolvimento de estímulos dinâmicos térmicos para análise do sistema sensorial infravermelho em serpentes

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