A Mammalian H⁺ Channel Generated through Alternative Splicing of the NADPH Oxidase Homolog NOH-1
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 hete...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 2000-01, Vol.287 (5450), p.138-142 |
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| creator | Bánfi, Botond Maturana, Andrés Jaconi, Stefano Arnaudeau, Serge Laforge, Terese Sinha, Bhanu Ligeti, Erzsébet Demaurex, Nicolas Krause, Karl-Heinz |
| description | 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). |
| doi_str_mv | 10.1126/science.287.5450.138 |
| format | Article |
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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).</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.287.5450.138</identifier><identifier>PMID: 10615049</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Society for the Advancement of Science</publisher><subject>Alternative Splicing ; Amino Acid Sequence ; Amino acids ; Biochemistry ; Biological and medical sciences ; Caco 2 cells ; Cell Line ; Cell lines ; Coding ; Cytosol - metabolism ; Electric Conductivity ; Electric current ; Electric potential ; Electron Transport ; Exons ; Expressed Sequence Tags ; Fundamental and applied biological sciences. Psychology ; Genes. Genome ; Geriatrics ; Humans ; Hydrogen - metabolism ; Hydrogen-Ion Concentration ; Ion Channel Gating ; Ion Channels - chemistry ; Ion Channels - genetics ; Ion Channels - metabolism ; Literary Devices ; Mammals ; Membrane Glycoproteins - chemistry ; Membrane Glycoproteins - genetics ; Molecular and cellular biology ; Molecular genetics ; Molecular Sequence Data ; NADPH Oxidase 1 ; NADPH Oxidase 2 ; NADPH Oxidases - chemistry ; NADPH Oxidases - genetics ; NIH 3T3 cells ; Oxidases ; Patch-Clamp Techniques ; Physiology ; Pipettes ; Proteins ; Protons ; Transfection ; Tumor Cells, Cultured ; Zinc - pharmacology</subject><ispartof>Science (American Association for the Advancement of Science), 2000-01, Vol.287 (5450), p.138-142</ispartof><rights>Copyright 1999 American Association for the Advancement of Science</rights><rights>2000 INIST-CNRS</rights><rights>Copyright American Association for the Advancement of Science Jan 7, 2000</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c442t-a24562fdfa35ef572086a130b0e9cac0872188fbf5e27bffbd5e121dde2551d33</citedby><cites>FETCH-LOGICAL-c442t-a24562fdfa35ef572086a130b0e9cac0872188fbf5e27bffbd5e121dde2551d33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3074278$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3074278$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,780,784,803,2884,2885,27924,27925,58017,58250</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1278355$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10615049$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bánfi, Botond</creatorcontrib><creatorcontrib>Maturana, Andrés</creatorcontrib><creatorcontrib>Jaconi, Stefano</creatorcontrib><creatorcontrib>Arnaudeau, Serge</creatorcontrib><creatorcontrib>Laforge, Terese</creatorcontrib><creatorcontrib>Sinha, Bhanu</creatorcontrib><creatorcontrib>Ligeti, Erzsébet</creatorcontrib><creatorcontrib>Demaurex, Nicolas</creatorcontrib><creatorcontrib>Krause, Karl-Heinz</creatorcontrib><title>A Mammalian H⁺ Channel Generated through Alternative Splicing of the NADPH Oxidase Homolog NOH-1</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>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).</description><subject>Alternative Splicing</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Caco 2 cells</subject><subject>Cell Line</subject><subject>Cell lines</subject><subject>Coding</subject><subject>Cytosol - metabolism</subject><subject>Electric Conductivity</subject><subject>Electric current</subject><subject>Electric potential</subject><subject>Electron Transport</subject><subject>Exons</subject><subject>Expressed Sequence Tags</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes. 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Maturana, Andrés ; Jaconi, Stefano ; Arnaudeau, Serge ; Laforge, Terese ; Sinha, Bhanu ; Ligeti, Erzsébet ; Demaurex, Nicolas ; Krause, Karl-Heinz</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c442t-a24562fdfa35ef572086a130b0e9cac0872188fbf5e27bffbd5e121dde2551d33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Alternative Splicing</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Caco 2 cells</topic><topic>Cell Line</topic><topic>Cell lines</topic><topic>Coding</topic><topic>Cytosol - metabolism</topic><topic>Electric Conductivity</topic><topic>Electric current</topic><topic>Electric potential</topic><topic>Electron Transport</topic><topic>Exons</topic><topic>Expressed Sequence Tags</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genes. Genome</topic><topic>Geriatrics</topic><topic>Humans</topic><topic>Hydrogen - metabolism</topic><topic>Hydrogen-Ion Concentration</topic><topic>Ion Channel Gating</topic><topic>Ion Channels - chemistry</topic><topic>Ion Channels - genetics</topic><topic>Ion Channels - metabolism</topic><topic>Literary Devices</topic><topic>Mammals</topic><topic>Membrane Glycoproteins - chemistry</topic><topic>Membrane Glycoproteins - genetics</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Molecular Sequence Data</topic><topic>NADPH Oxidase 1</topic><topic>NADPH Oxidase 2</topic><topic>NADPH Oxidases - chemistry</topic><topic>NADPH Oxidases - genetics</topic><topic>NIH 3T3 cells</topic><topic>Oxidases</topic><topic>Patch-Clamp Techniques</topic><topic>Physiology</topic><topic>Pipettes</topic><topic>Proteins</topic><topic>Protons</topic><topic>Transfection</topic><topic>Tumor Cells, Cultured</topic><topic>Zinc - 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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).</abstract><cop>Washington, DC</cop><pub>American Society for the Advancement of Science</pub><pmid>10615049</pmid><doi>10.1126/science.287.5450.138</doi><tpages>5</tpages></addata></record> |
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| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 2000-01, Vol.287 (5450), p.138-142 |
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| source | MEDLINE; American Association for the Advancement of Science; Jstor Complete Legacy |
| subjects | Alternative Splicing Amino Acid Sequence Amino acids Biochemistry Biological and medical sciences Caco 2 cells Cell Line Cell lines Coding Cytosol - metabolism Electric Conductivity Electric current Electric potential Electron Transport Exons Expressed Sequence Tags Fundamental and applied biological sciences. Psychology Genes. Genome Geriatrics Humans Hydrogen - metabolism Hydrogen-Ion Concentration Ion Channel Gating Ion Channels - chemistry Ion Channels - genetics Ion Channels - metabolism Literary Devices Mammals Membrane Glycoproteins - chemistry Membrane Glycoproteins - genetics Molecular and cellular biology Molecular genetics Molecular Sequence Data NADPH Oxidase 1 NADPH Oxidase 2 NADPH Oxidases - chemistry NADPH Oxidases - genetics NIH 3T3 cells Oxidases Patch-Clamp Techniques Physiology Pipettes Proteins Protons Transfection Tumor Cells, Cultured Zinc - pharmacology |
| title | A Mammalian H⁺ Channel Generated through Alternative Splicing of the NADPH Oxidase Homolog NOH-1 |
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