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Ligand mediated protein‐protein interaction between the angiotensin receptor type AT1 and the human NHE6 isoform

The Renin Angiotensin System (RAS) plays a vital role in the regulation of blood pressure and fluid homeostasis. RAS is regulated through the hormone Angiotensin II (Ang II), a powerful vasoconstrictor that serves as a regulator of hypertension and other cardiovascular diseases. Involvement of Ang II in the regulation of sodium levels by activation of the Na+/H+ Exchangers (NHE) has been demonstrated in many tissues. Of the seven known NHE isoforms, only two, NHE1 and NHE6, exist in heart tissue. The activities of the NHE6 protein remain unclear. To analyze the conditions leading to activation of the NHE6 protein in mammalian cells, the human MCF‐7 cell line was used. The Heameagglutinin‐tagged NHE6 plasmid was introduced to the MCF‐7 cells via transient transfection. The transfected cells were exposed to Ang II and results implicated that the presence of Ang II was cardinal for strong interaction between AT1 and NHE6. It was ascertained that MCF‐7 co‐transfected with AT2 and Heameagglutinin‐tagged NHE6, also required the presence of Ang II for activation. Further investigation revealed that tyrosine and threonine phosphorylation of NHE6 occurred when AT1 was activated by ligand binding. In summary, our results insinuate Ang II activates NHE6 through the AT1 receptor and therefore may play a role in the development of the pathophysiological conditions leading to the onset of cardiac ischemia.