Human and Mouse TRPA1 Are Heat and Cold Sensors Differentially Tuned by Voltage
| Autor: | Kristyna Barvikova, Lucie Zimova, Ivan Barvík, Lucie Macikova, Viktor Sinica, Viktorie Vlachova |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Hot Temperature noxious heat Allosteric regulation thermoTRP noxious cold Gating Models Biological Article Mice 03 medical and health sciences Transient receptor potential channel 0302 clinical medicine Species Specificity TRP channel Animals Humans Voltage-Dependent Anion Channels Ankyrin Amino Acid Sequence lcsh:QH301-705.5 TRPA1 Cation Channel chemistry.chemical_classification ankyrin receptor subtype 1 food and beverages General Medicine Cold Temperature Electrophysiology HEK293 Cells 030104 developmental biology lcsh:Biology (General) chemistry transient receptor potential Biophysics Evolutionary divergence psychological phenomena and processes 030217 neurology & neurosurgery Voltage |
| Zdroj: | Cells Volume 9 Issue 1 Cells, Vol 9, Iss 1, p 57 (2019) |
| ISSN: | 2073-4409 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|