Vital but vulnerable: Human TRPV6 is a trade-off of powerful Ca2+ uptake and susceptibility to epithelial barrier dysfunction

Yasuo Mori; Mizuki Omori; Akito Nakao

doi:10.1016/j.ceca.2022.102652

Vital but vulnerable: Human TRPV6 is a trade-off of powerful Ca²⁺ uptake and susceptibility to epithelial barrier dysfunction

Cell Calcium. 2022 Nov:107:102652. doi: 10.1016/j.ceca.2022.102652. Epub 2022 Sep 13.

Authors

Yasuo Mori¹, Mizuki Omori², Akito Nakao²

Affiliations

¹ Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Kyoto 615-8510, Japan. Electronic address: mori@sbchem.kyoto-u.ac.jp.
² Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Kyoto 615-8510, Japan.

PMID: 36162385
DOI: 10.1016/j.ceca.2022.102652

Abstract

Robust Ca²⁺ absorption is controlled by the highly Ca²⁺-permeable channels TRPV5 and TRPV6 in the kidney and intestine of terrestrial vertebrates, to fulfill the body's demand for Ca²⁺. Recently, a pathogenic role of TRPV6 was revealed in alcohol-associated endotoxemia; the intestinal barrier function is compromised by oxidative stress via TRPV6-mediated Ca²⁺ dysregulation. TRPV6-mediated Ca²⁺ absorption vital to maintain homeostasis is vulnerable to alcohol-induced malactivation.

Keywords: Alcohol; Endotoxemia; Epithelial barrier; Intestinal Ca(2+) absorption; ROS; TRPV6.

MeSH terms

Animals
Biological Transport
Calcium / metabolism
Calcium Channels* / metabolism
Homeostasis
Humans
TRPV Cation Channels* / metabolism

Substances

Calcium Channels
TRPV Cation Channels
Calcium
TRPV6 protein, human