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

B Bánfi; A Maturana; S Jaconi; S Arnaudeau; T Laforge; B Sinha; E Ligeti; N Demaurex; K H Krause

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

B Bánfi
, A Maturana
, S Jaconi
, S Arnaudeau
, T Laforge
, B Sinha
, E Ligeti
, N Demaurex
, K H Krause

Research output: Contribution to journal › Article › Academic › peer-review

264 Citations (Scopus)

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).

Original language	English
Pages (from-to)	138-142
Number of pages	5
Journal	Science
Volume	287
Issue number	5450
Publication status	Published - 7-Jan-2000

Keywords

Alternative Splicing
Amino Acid Sequence
Cell Line
Cytosol
Electric Conductivity
Electron Transport
Expressed Sequence Tags
Humans
Hydrogen
Hydrogen-Ion Concentration
Ion Channel Gating
Ion Channels
Membrane Glycoproteins
Molecular Sequence Data
NADPH Oxidase
Patch-Clamp Techniques
Protons
Transfection
Tumor Cells, Cultured
Zinc

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

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 Splicing, Amino Acid Sequence, Cell Line, Cytosol, Electric Conductivity, Electron Transport, Expressed Sequence Tags, Humans, Hydrogen, Hydrogen-Ion Concentration, Ion Channel Gating, Ion Channels, Membrane Glycoproteins, Molecular Sequence Data, NADPH Oxidase, Patch-Clamp Techniques, Protons, Transfection, Tumor Cells, Cultured, Zinc",

author = "B B{\'a}nfi and A Maturana and S Jaconi and S Arnaudeau and T Laforge and B Sinha and E Ligeti and N Demaurex and Krause, \{K H\}",

year = "2000",

month = jan,

day = "7",

language = "English",

volume = "287",

pages = "138--142",

journal = "Science",

issn = "0036-8075",

publisher = "AMER ASSOC ADVANCEMENT SCIENCE",

number = "5450",

}

TY - JOUR

T1 - A mammalian H+ channel generated through alternative splicing of the NADPH oxidase homolog NOH-1

AU - Bánfi, B

AU - Maturana, A

AU - Jaconi, S

AU - Arnaudeau, S

AU - Laforge, T

AU - Sinha, B

AU - Ligeti, E

AU - Demaurex, N

AU - Krause, K H

PY - 2000/1/7

Y1 - 2000/1/7

N2 - 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).

AB - 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).

KW - Alternative Splicing

KW - Amino Acid Sequence

KW - Cell Line

KW - Cytosol

KW - Electric Conductivity

KW - Electron Transport

KW - Expressed Sequence Tags

KW - Humans

KW - Hydrogen

KW - Hydrogen-Ion Concentration

KW - Ion Channel Gating

KW - Ion Channels

KW - Membrane Glycoproteins

KW - Molecular Sequence Data

KW - NADPH Oxidase

KW - Patch-Clamp Techniques

KW - Protons

KW - Transfection

KW - Tumor Cells, Cultured

KW - Zinc

M3 - Article

C2 - 10615049

SN - 0036-8075

VL - 287

SP - 138

EP - 142

JO - Science

JF - Science

IS - 5450

ER -

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

Abstract

Keywords

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