Abstract
Voltage-gated proton (H+) channels are found in many human and animal tissues and play an important role in cellular defense against acidic stress. However, a molecular identification of these unique ion conductances has so far not been achieved. A 191-amino acid protein is described that, upon heterologous expression, has properties indistinguishable from those of native H+ channels. This protein is generated through alternative splicing of messenger RNA derived from the gene NOH-1 (NADPH oxidase homolog 1, where NADPH is the reduced form of nicotinamide adenine dinucleotide phosphate).
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Alternative Splicing*
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Amino Acid Sequence
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Cell Line
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Cytosol / metabolism
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Electric Conductivity
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Electron Transport
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Expressed Sequence Tags
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Humans
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Hydrogen / metabolism*
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Hydrogen-Ion Concentration
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Ion Channel Gating
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Ion Channels / chemistry
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Ion Channels / genetics*
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Ion Channels / metabolism
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Membrane Glycoproteins / chemistry
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Membrane Glycoproteins / genetics*
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Molecular Sequence Data
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NADPH Oxidase 1
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NADPH Oxidase 2
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NADPH Oxidases / chemistry
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NADPH Oxidases / genetics*
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Patch-Clamp Techniques
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Protons
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Transfection
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Tumor Cells, Cultured
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Zinc / pharmacology
Substances
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Ion Channels
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Membrane Glycoproteins
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Protons
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Hydrogen
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CYBB protein, human
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NADPH Oxidase 1
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NADPH Oxidase 2
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NADPH Oxidases
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NOX1 protein, human
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Zinc
Associated data
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GENBANK/AF166326
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GENBANK/AF166327
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GENBANK/AF166328
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GENBANK/AI821410