A Mammalian H + Channel Generated Through Alternative Splicing of the NADPH Oxidase Homolog NOH-1

Author:

Bánfi Botond1,Maturana Andrés23,Jaconi Stefano,Arnaudeau Serge2,Laforge Terese,Sinha Bhanu4,Ligeti Erzsébet1,Demaurex Nicolas2,Krause Karl-Heinz

Affiliation:

1. Department of Physiology, Semmelweis Medical University, H-1444 Budapest 8, Hungary.

2. Department of Physiology,

3. Fondation pour Recherches Médicales,

4. Division of Infectious Diseases, Geneva University Hospitals, Geneva Medical School, CH-1211 Geneva 4, Switzerland.

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).

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference37 articles.

1. We use the consensus terminology “channel” because voltage-dependent H + currents mimic several electrophysiological properties of ion channels. However as previously recognized (5) the mechanism of permeation might not necessarily involve a water-filled pore.

2. Hydrogen ion currents and intracellular pH in depolarized voltage-clamped snail neurones

3. Hydrogen ion currents in rat alveolar epithelial cells

4. Demaurex N., et al., J. Physiol. (London) 466, 329 (1993).

5. DeCoursey T. E., Cherny V. V., J. Membr. Biol. 141, 203 (1994).

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