Title : LTRPC7 is a Mg.ATP-regulated divalent cation channel required for cell viability.

Pub. Date : 2001 May 31

PMID : 11385574






8 Functional Relationships(s)
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1 Here we describe the cloning and functional characterization of a Ca2+- and Mg2+-permeable divalent cation channel, LTRPC7 (nomenclature compatible with that proposed in ref. magnesium ion transient receptor potential cation channel subfamily M member 7 Homo sapiens
2 Electrophysiological analysis of HEK-293 cells overexpressing recombinant LTRPC7 showed large currents regulated by millimolar levels of intracellular Mg.ATP and Mg.GTP with the permeation properties of a voltage-independent divalent cation influx pathway. Magnesium transient receptor potential cation channel subfamily M member 7 Homo sapiens
3 Electrophysiological analysis of HEK-293 cells overexpressing recombinant LTRPC7 showed large currents regulated by millimolar levels of intracellular Mg.ATP and Mg.GTP with the permeation properties of a voltage-independent divalent cation influx pathway. Adenosine Triphosphate transient receptor potential cation channel subfamily M member 7 Homo sapiens
4 Electrophysiological analysis of HEK-293 cells overexpressing recombinant LTRPC7 showed large currents regulated by millimolar levels of intracellular Mg.ATP and Mg.GTP with the permeation properties of a voltage-independent divalent cation influx pathway. Magnesium transient receptor potential cation channel subfamily M member 7 Homo sapiens
5 Electrophysiological analysis of HEK-293 cells overexpressing recombinant LTRPC7 showed large currents regulated by millimolar levels of intracellular Mg.ATP and Mg.GTP with the permeation properties of a voltage-independent divalent cation influx pathway. Guanosine Triphosphate transient receptor potential cation channel subfamily M member 7 Homo sapiens
6 Analysis of several cultured cell types demonstrated small magnesium-nucleotide-regulated metal ion currents (MagNuM) with regulation and permeation properties essentially identical to the large currents observed in cells expressing recombinant LTRPC7. magnesium-nucleotide transient receptor potential cation channel subfamily M member 7 Homo sapiens
7 Analysis of several cultured cell types demonstrated small magnesium-nucleotide-regulated metal ion currents (MagNuM) with regulation and permeation properties essentially identical to the large currents observed in cells expressing recombinant LTRPC7. Metals transient receptor potential cation channel subfamily M member 7 Homo sapiens
8 Our data indicate that LTRPC7, by virtue of its sensitivity to physiological Mg.ATP levels, may be involved in a fundamental process that adjusts plasma membrane divalent cation fluxes according to the metabolic state of the cell. Adenosine Triphosphate transient receptor potential cation channel subfamily M member 7 Homo sapiens