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      Immunocyte Ca2+ influx system mediated by LTRPC2.

      Science (New York, N.Y.)
      ADP-ribosyl Cyclase, Adenosine Diphosphate Ribose, metabolism, pharmacology, Adenosine Triphosphate, Antigens, CD, Antigens, CD38, Antigens, Differentiation, Apoptosis, Calcium, Calcium Channels, Cell Line, Eosinophils, Humans, Ion Channels, Jurkat Cells, Membrane Glycoproteins, Membrane Potentials, Membrane Proteins, Monocytes, NAD, NAD+ Nucleosidase, Patch-Clamp Techniques, Reverse Transcriptase Polymerase Chain Reaction, T-Lymphocytes, TRPM Cation Channels

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          Abstract

          We characterized an activation mechanism of the human LTRPC2 protein, a member of the transient receptor potential family of ion channels, and demonstrated that LTRPC2 mediates Ca2+ influx into immunocytes. Intracellular pyrimidine nucleotides, adenosine 5'-diphosphoribose (ADPR), and nicotinamide adenine dinucleotide (NAD), directly activated LTRPC2, which functioned as a Ca2+-permeable nonselective cation channel and enabled Ca2+ influx into cells. This activation was suppressed by intracellular adenosine triphosphate. These results reveal that ADPR and NAD act as intracellular messengers and may have an important role in Ca2+ influx by activating LTRPC2 in immunocytes.

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