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A mammalian H+ channel generated through alternative splicing of the NADPH oxidase homolog NOH-1

Jaconi, S.
Laforge, Terese
Sinha, B.
Ligeti, E.
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Published in Science. 2000, vol. 287, no. 5450, p. 138-142
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).
Keywords Alternative SplicingAmino Acid SequenceCell LineCytosol/metabolismElectric ConductivityElectron TransportExpressed Sequence TagsHumansHydrogen/ metabolismHydrogen-Ion ConcentrationIon Channel GatingIon Channels/chemistry/ genetics/metabolismMembrane Glycoproteins/chemistry/ geneticsMolecular Sequence DataNADPH Oxidase/chemistry/ geneticsPatch-Clamp TechniquesProtonsTransfectionTumor Cells, CulturedZinc/pharmacology
PMID: 10615049
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Other version: http://www.sciencemag.org/cgi/reprint/287/5450/138.pdf
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BANFI, Botond et al. A mammalian H+ channel generated through alternative splicing of the NADPH oxidase homolog NOH-1. In: Science, 2000, vol. 287, n° 5450, p. 138-142. doi: 10.1126/science.287.5450.138 https://archive-ouverte.unige.ch/unige:11130

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Deposited on : 2010-08-27

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