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Identification of phospholipase C β downstream effect on transient receptor potential canonical 1/4, transient receptor potential canonical 1/5 channels

Korean Journal of Physiology & Pharmacology 2019년 23권 5호 p.357 ~ 366
 ( Ko Ju-Yeon ) - Seoul National University College of Medicine Department of Physiology

 ( Myeong Jong-Yun ) - Seoul National University College of Medicine Department of Physiology
 ( Kwak Mi-Sun ) - Seoul National University College of Medicine Department of Physiology
 ( Jeon Ju-Hong ) - Seoul National University College of Medicine Department of Physiology
 ( So In-Suk ) - Seoul National University College of Medicine Department of Physiology

Abstract


Gαq-coupled receptor stimulation was implied in the activation process of transient receptor potential canonical (TRPC)1/4 and TRPC1/5 heterotetrameric channels. The inactivation occurs due to phosphatidylinositol 4,5-biphosphate (PI(4,5)P2) depletion. When PI(4,5)P2 depletion was induced by muscarinic stimulation or inositol polyphosphate 5-phosphatase (Inp54p), however, the inactivation by muscarinic stimulation was greater compared to that by Inp54p. The aim of this study was to investigate the complete inactivation mechanism of the heteromeric channels upon Gαq-phospholipase C β (Gαq-PLCβ) activation. We evaluated the activity of heteromeric channels with electrophysiological recording in HEK293 cells expressing TRPC channels. TRPC1/4 and TRPC1/5 heteromers undergo further inhibition in PLCβ activation and calcium/protein kinase C (PKC) signaling. Nevertheless, the key factors differ. For TRPC1/4, the inactivation process was facilitated by Ca2+ release from the endoplasmic reticulum, and for TRPC1/5, activation of PKC was concerned mostly. We conclude that the subsequent increase in cytoplasmic Ca2+ due to Ca2+ release from the endoplasmic reticulum and activation of PKC resulted in a second phase of channel inhibition following PI(4,5)P2 depletion.

키워드

Calcium; GTP-binding proteins; Protein kinase C; Transient receptor potential channels; Type C phospholipases
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