Ectodomain shedding of EGFR ligands serves as an activation readout for TRP channels

Manae Tatsumi, Takayuki Kishi, Satoru Ishida, Hiroki Kawana, Akiharu Uwamizu, Yuki Ono, Kouki Kawakami, Junken Aoki, Asuka Inoue

Research output: Contribution to journalArticlepeer-review

Abstract

Transient receptor potential (TRP) channels are activated by various extracellular and intracellular stimuli and are involved in many physiological events. Because compounds that act on TRP channels are potential candidates for therapeutic agents, a simple method for evaluating TRP channel activation is needed. In this study, we demonstrated that a transforming growth factor alpha (TGFα) shedding assay, previously developed for detecting G-protein- coupled receptor (GPCR) activation, can also detect TRP channel activation. This assay is a low-cost, easily accessible method that requires only an absorbance microplate reader. Mechanistically, TRP-channel-triggered TGFα shedding is achieved by both of a disintegrin and metalloproteinase domain-containing protein 10 (ADAM10) and 17 (ADAM17), whereas the GPCR-induced TGFα shedding response depends solely on ADAM17. This difference may be the result of qualitative or quantitative differences in intracellular Ca2+ kinetics between TRP channels and GPCRs. Use of epidermal growth factor (EGF) and betacellulin (BTC), substrates of ADAM10, improved the specificity of the shedding assay by reducing background responses mediated by endogenously expressed GPCRs. This assay for TRP channel measurement will not only facilitate the high-throughput screening of TRP channel ligands but also contribute to understanding the roles played by TRP channels as regulators of membrane protein ectodomain shedding.

Original languageEnglish
Article numbere0280448
JournalPloS one
Volume18
Issue number1 January
DOIs
Publication statusPublished - 2023 Jan
Externally publishedYes

ASJC Scopus subject areas

  • General

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