Rapid and reversible inhibition of aquaporin-4 by zinc

Yoshinori Yukutake, Yoshinori Hirano, Makoto Suematsu, Masato Yasui

Research output: Contribution to journalArticle

35 Citations (Scopus)

Abstract

Aquaporin-4 (AQP4) is the predominant water channel in the brain. Although AQP4 plays an important role in brain water homeostasis, the molecular mechanisms of AQP4 regulation are not fully understood. In this report, we show how Zn2+ rapidly and reversibly decreases the water permeability of AQP4 when it is reconstituted into proteoliposomes. Mutagenesis analysis identified Cys178, located in cytoplasmic loop D, as a target residue of ZnCl2 inhibition. Moreover, treatment with diamide enhanced the inhibitory effects of ZnCl2. These results suggest that the water permeability of AQP4 may be regulated by dynamic changes in intracellular Zn2+ concentration linked to the cellular redox state.

Original languageEnglish
Pages (from-to)12059-12061
Number of pages3
JournalBiochemistry
Volume48
Issue number51
DOIs
Publication statusPublished - 2009 Dec 29

Fingerprint

Aquaporin 4
Zinc
Water
Permeability
Brain
Diamide
Mutagenesis
Aquaporins
Oxidation-Reduction
Homeostasis

ASJC Scopus subject areas

  • Biochemistry

Cite this

Rapid and reversible inhibition of aquaporin-4 by zinc. / Yukutake, Yoshinori; Hirano, Yoshinori; Suematsu, Makoto; Yasui, Masato.

In: Biochemistry, Vol. 48, No. 51, 29.12.2009, p. 12059-12061.

Research output: Contribution to journalArticle

Yukutake, Y, Hirano, Y, Suematsu, M & Yasui, M 2009, 'Rapid and reversible inhibition of aquaporin-4 by zinc', Biochemistry, vol. 48, no. 51, pp. 12059-12061. https://doi.org/10.1021/bi901762y
Yukutake, Yoshinori ; Hirano, Yoshinori ; Suematsu, Makoto ; Yasui, Masato. / Rapid and reversible inhibition of aquaporin-4 by zinc. In: Biochemistry. 2009 ; Vol. 48, No. 51. pp. 12059-12061.
@article{89c2f3cb5fe54cbe9b82bcfef0771082,
title = "Rapid and reversible inhibition of aquaporin-4 by zinc",
abstract = "Aquaporin-4 (AQP4) is the predominant water channel in the brain. Although AQP4 plays an important role in brain water homeostasis, the molecular mechanisms of AQP4 regulation are not fully understood. In this report, we show how Zn2+ rapidly and reversibly decreases the water permeability of AQP4 when it is reconstituted into proteoliposomes. Mutagenesis analysis identified Cys178, located in cytoplasmic loop D, as a target residue of ZnCl2 inhibition. Moreover, treatment with diamide enhanced the inhibitory effects of ZnCl2. These results suggest that the water permeability of AQP4 may be regulated by dynamic changes in intracellular Zn2+ concentration linked to the cellular redox state.",
author = "Yoshinori Yukutake and Yoshinori Hirano and Makoto Suematsu and Masato Yasui",
year = "2009",
month = "12",
day = "29",
doi = "10.1021/bi901762y",
language = "English",
volume = "48",
pages = "12059--12061",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "51",

}

TY - JOUR

T1 - Rapid and reversible inhibition of aquaporin-4 by zinc

AU - Yukutake, Yoshinori

AU - Hirano, Yoshinori

AU - Suematsu, Makoto

AU - Yasui, Masato

PY - 2009/12/29

Y1 - 2009/12/29

N2 - Aquaporin-4 (AQP4) is the predominant water channel in the brain. Although AQP4 plays an important role in brain water homeostasis, the molecular mechanisms of AQP4 regulation are not fully understood. In this report, we show how Zn2+ rapidly and reversibly decreases the water permeability of AQP4 when it is reconstituted into proteoliposomes. Mutagenesis analysis identified Cys178, located in cytoplasmic loop D, as a target residue of ZnCl2 inhibition. Moreover, treatment with diamide enhanced the inhibitory effects of ZnCl2. These results suggest that the water permeability of AQP4 may be regulated by dynamic changes in intracellular Zn2+ concentration linked to the cellular redox state.

AB - Aquaporin-4 (AQP4) is the predominant water channel in the brain. Although AQP4 plays an important role in brain water homeostasis, the molecular mechanisms of AQP4 regulation are not fully understood. In this report, we show how Zn2+ rapidly and reversibly decreases the water permeability of AQP4 when it is reconstituted into proteoliposomes. Mutagenesis analysis identified Cys178, located in cytoplasmic loop D, as a target residue of ZnCl2 inhibition. Moreover, treatment with diamide enhanced the inhibitory effects of ZnCl2. These results suggest that the water permeability of AQP4 may be regulated by dynamic changes in intracellular Zn2+ concentration linked to the cellular redox state.

UR - http://www.scopus.com/inward/record.url?scp=73149096944&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=73149096944&partnerID=8YFLogxK

U2 - 10.1021/bi901762y

DO - 10.1021/bi901762y

M3 - Article

C2 - 19928950

AN - SCOPUS:73149096944

VL - 48

SP - 12059

EP - 12061

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 51

ER -