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Aquaporin‐2 and Na + /H + exchanger isoform 1 modulate the efficiency of renal cell migration
Author(s) -
Di Giusto Gisela,
Pizzoni Alejandro,
Rivarola Valeria,
Beltramone Natalia,
White Alan,
Ford Paula,
Capurro Claudia
Publication year - 2020
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.29320
Subject(s) - lamellipodium , sodium–hydrogen antiporter , aquaporin 2 , focal adhesion , cell migration , chemistry , microbiology and biotechnology , intracellular ph , gene isoform , intracellular , biophysics , cell , biochemistry , biology , water channel , sodium , mechanical engineering , organic chemistry , gene , engineering , inlet
Aquaporin‐2 (AQP2) promotes renal cell migration by the modulation of integrin β1 trafficking and the turnover of focal adhesions. The aim of this study was to investigate whether AQP2 also works in cooperation with Na + /H + exchanger isoform 1 (NHE1), another well‐known protein involved in the regulation of cell migration. Our results showed that the lamellipodia of AQP2‐expressing cells exhibit significantly smaller volumes and areas of focal adhesions and more alkaline intracellular pH due to increased NHE1 activity than AQP2‐null cells. The blockage of AQP2, or its physically‐associated calcium channel TRPV4, significantly reduced lamellipodia NHE1 activity. NHE1 blockage significantly reduced the rate of cell migration, the number of lamellipodia, and the assembly of F‐actin only in AQP2‐expressing cells. Our data suggest that AQP2 modulates the activity of NHE1 through its calcium channel partner TRPV4, thereby determining pH‐dependent actin polymerization, providing mechanical stability to delineate lamellipodia structure and defining the efficiency of cell migration.