Oxidation sensitizes TRPV2 to chemical and heat stimuli, but not mechanical stimulation

The transient receptor potential vanilloid 2 (TRPV2) ion channel is activated by a chemical ligand (2-aminoethoxydiphenyl borate; 2-APB), noxious heat and mechanical stimulation. In a heterologous mammalian cell expression system, the oxidant chloramine T (ChT) sensitizes TRPV2 activation in respons...

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Published inBiochemistry and biophysics reports Vol. 28; p. 101173
Main Authors Oda, Mai, Fujiwara, Yuichiro, Ishizaki, Yasuki, Shibasaki, Koji
Format Journal Article
LanguageEnglish
Published Elsevier B.V 01.12.2021
Elsevier
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Summary:The transient receptor potential vanilloid 2 (TRPV2) ion channel is activated by a chemical ligand (2-aminoethoxydiphenyl borate; 2-APB), noxious heat and mechanical stimulation. In a heterologous mammalian cell expression system, the oxidant chloramine T (ChT) sensitizes TRPV2 activation in response to 2-APB and heat by oxidation of methionine residues at positions 528 and 607 in rat TRPV2. Here, we used a Xenopus oocyte expression system to determine whether ChT-mediated oxidation can also sensitize TRPV2 to mechanical stimulation. In this system, we confirmed that ChT sensitized TRPV2 activation in response to 2-APB and heat, but we detected no sensitization to mechanical stimulation. This result suggests that the activation mechanism of TRPV2 by a chemical ligand and heat differs from that for mechanical stimulation. Further, we demonstrated that two-electrode voltage clamp recording in the Xenopus oocyte expression system is an excellent format for high throughput analysis of oxidization of redox-sensitive TRP channels.
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Current Affiliation: Cellular & Molecular Physiology, Yale University School of Medicine, New Heaven, CT, 06520-8026.
ISSN:2405-5808
2405-5808
DOI:10.1016/j.bbrep.2021.101173