Issue 5, 2016
From the journal:

Molecular BioSystems

Exploring the gating mechanisms of aquaporin-3: new clues for the design of inhibitors?†

A. de Almeida,‡a   A. P. Martins,‡bc   A. F. Mósca,bc   H. J. Wijma,d   C. Prista,e   G. Soveral*bc  and  A. Casini*af  

* Corresponding authors

a Dept. of Pharmacokinetics, Toxicology and Targeting, Groningen Research Institute of Pharmacy, University of Groningen, A. Deusinglaan 1, 9713 AV Groningen, The Netherlands

b Research Institute for Medicines (iMed.ULisboa), Faculty of Pharmacy, Universidade de Lisboa, 1649-003 Lisboa, Portugal
E-mail: gsoveral@ff.ulisboa.pt

c Dept. Bioquímica e Biologia Humana, Faculty of Pharmacy, Universidade de Lisboa, 1649-003 Lisboa, Portugal

d Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands

e Research Center “Linking Landscape, Environment, Agriculture and Food” (LEAF), Instituto Superior de Agronomia, Universidade de Lisboa, 1349-017 Lisboa, Portugal

f School of Chemistry, Cardiff University, Main Building, Park Place, Cardiff CF10 3AT, UK
E-mail: casinia@cardiff.ac.uk

Abstract

The pH gating of human AQP3 and its effects on both water and glycerol permeabilities have been fully characterized for the first time using a human red blood cell model (hRBC). For comparison, the effects of pH on the gating of rat AQP3 have also been characterized in yeast. The obtained results highlight similarities as well as differences between the two isoforms. In addition, we investigated the molecular mechanism of hAQP3 pH gating in silico, which may disclose new pathways to AQP regulation by small molecule inhibitors, and therefore may be important for drug development.

Graphical abstract: Exploring the gating mechanisms of aquaporin-3: new clues for the design of inhibitors?

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Article information

DOI
https://doi.org/10.1039/C6MB00013D
Article type
Paper
Submitted
26 ربيع الأول 1437
Accepted
22 جمادى الأولى 1437
First published
22 جمادى الأولى 1437

Mol. BioSyst., 2016,12, 1564-1573

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Exploring the gating mechanisms of aquaporin-3: new clues for the design of inhibitors?

A. de Almeida, A. P. Martins, A. F. Mósca, H. J. Wijma, C. Prista, G. Soveral and A. Casini, Mol. BioSyst., 2016, 12, 1564 DOI: 10.1039/C6MB00013D

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