Proton conductivity through the human TRPM7 channel and its molecular determinants.
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ABSTRACT: TRPM7 is a divalent cation-permeable channel that is ubiquitously expressed. Recently, mouse TRPM7 has been shown to be sensitive to, and even permeable to, protons when heterologously expressed. Here we have demonstrated that human TRPM7 expressed either heterologously or endogenously also exhibits proton conductivity. The gene silencing of TRPM7 by small interfering RNA suppressed H+ currents in human cervical epithelial HeLa cells. In HEK293T cells transfected with human TRPM7, the inward proton conductance was suppressed by extracellular Mg2+ or Ca2+ with IC(50) values of 0.5 and 1.9 mm, respectively. Anomalous mole fraction behavior of H+ currents in the presence of Mg2+ or Ca2+ indicated that these divalent cations compete with protons for binding sites. Systematic mutation of negati
SUBMITTER: Numata T
PROVIDER: S-EPMC3258882 | biostudies-literature | 2008 May
REPOSITORIES: biostudies-literature
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