April 27, 2018Frontiers in ChemistryOpen Access

Identification of Loop D Domain Amino Acids in the Human Aquaporin-1 Channel Involved in Activation of the Ionic Conductance and Inhibition by AqB011

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Population

Xenopus laevis oocytes expressing human AQP1 wild type and mutant channels

Comparison

Site-directed mutagenesis of loop D domain amino… vs Wild-type human AQP1 channels and non-AQP…

Design

Preclinical

Authors

Discussion

Supports loop D as essential for AQP1 gating and AqB011 binding; leaves open translation to cardiovascular models.

Population

Xenopus laevis oocytes expressing human AQP1 wild type and mutant channels (R159A+R160A, T157P, D158P, R159P, R160P, G165P)

Intervention

Site-directed mutagenesis of loop D domain amino acids and application of AQP1 ion channel inhibitor AqB011 (50 µM)

Comparator

Wild-type human AQP1 channels and non-AQP expressing control oocytes

Outcome

Activation of ionic conductance and sensitivity to pharmacological block by AqB011surrogate

The loop D domain of human AQP1 is essential for ion channel gating and is the likely binding site for the selective inhibitor AqB011.

Kourghi et al. (2018) studied this question.

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