Monoamine Oxidase B Induces ERK-Dependent Cell Mitogenesis by Hydrogen Peroxide Generation
The mitochondrial enzyme monoamine oxidase (MAO) A and B catalyze the oxidative deamination of various endogenous and exogenous biogenic amines. In the present study, we used human embryonic kidney 293 (HEK 293) cells stably transfected with human MAO-B cDNA to investigate the potential role of hydr...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2000-04, Vol.271 (1), p.181-185 |
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| creator | Vindis, Cécile Séguélas, Marie-Hélène Bianchi, Pascale Parini, Angelo Cambon, Claudie |
| description | The mitochondrial enzyme monoamine oxidase (MAO) A and B catalyze the oxidative deamination of various endogenous and exogenous biogenic amines. In the present study, we used human embryonic kidney 293 (HEK 293) cells stably transfected with human MAO-B cDNA to investigate the potential role of hydrogen peroxide (H2O2) produced by MAO-B isoform as an intracellular messenger involved in regulation of cell signaling and function. The MAO substrate tyramine induced tyrosine phosphorylation of Shc, ERK activation, and an increase in DNA synthesis in HEK 293 expressing MAO-B, but not in wild type HEK 293 cells, which do not express MAO. Tyramine effects were fully prevented by cell pretreatment with the MAO inhibitor pargyline or the antioxidant N-acetylcysteine. These results show that MAO-B induces MAPK/ERK activation and cell mitogenesis through H2O2 production. |
| doi_str_mv | 10.1006/bbrc.2000.2524 |
| format | Article |
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In the present study, we used human embryonic kidney 293 (HEK 293) cells stably transfected with human MAO-B cDNA to investigate the potential role of hydrogen peroxide (H2O2) produced by MAO-B isoform as an intracellular messenger involved in regulation of cell signaling and function. The MAO substrate tyramine induced tyrosine phosphorylation of Shc, ERK activation, and an increase in DNA synthesis in HEK 293 expressing MAO-B, but not in wild type HEK 293 cells, which do not express MAO. Tyramine effects were fully prevented by cell pretreatment with the MAO inhibitor pargyline or the antioxidant N-acetylcysteine. 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Séguélas, Marie-Hélène ; Bianchi, Pascale ; Parini, Angelo ; Cambon, Claudie</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c340t-d4a34ee62f340f3a90e8b4b3d038b84f60603b71184389d34523d7ce54f197a13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Adaptor Proteins, Signal Transducing</topic><topic>Adaptor Proteins, Vesicular Transport</topic><topic>Adrenergic Uptake Inhibitors - pharmacology</topic><topic>Blotting, Western</topic><topic>Cell Division - drug effects</topic><topic>Cell Line</topic><topic>DNA, Complementary - metabolism</topic><topic>Dose-Response Relationship, Drug</topic><topic>extracellular signal-regulated protein kinase</topic><topic>human embryonic kidney 293 cells</topic><topic>Humans</topic><topic>hydrogen peroxide</topic><topic>Hydrogen Peroxide - metabolism</topic><topic>Mitogen-Activated Protein Kinases - metabolism</topic><topic>mitogenesis</topic><topic>monoamine oxidase</topic><topic>Monoamine Oxidase - metabolism</topic><topic>Phosphorylation</topic><topic>Precipitin Tests</topic><topic>Proteins - metabolism</topic><topic>Shc Signaling Adaptor Proteins</topic><topic>Signal Transduction</topic><topic>Src Homology 2 Domain-Containing, Transforming Protein 1</topic><topic>Time Factors</topic><topic>Transfection</topic><topic>Tyramine - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vindis, Cécile</creatorcontrib><creatorcontrib>Séguélas, Marie-Hélène</creatorcontrib><creatorcontrib>Bianchi, Pascale</creatorcontrib><creatorcontrib>Parini, Angelo</creatorcontrib><creatorcontrib>Cambon, Claudie</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vindis, Cécile</au><au>Séguélas, Marie-Hélène</au><au>Bianchi, Pascale</au><au>Parini, Angelo</au><au>Cambon, Claudie</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Monoamine Oxidase B Induces ERK-Dependent Cell Mitogenesis by Hydrogen Peroxide Generation</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2000-04-29</date><risdate>2000</risdate><volume>271</volume><issue>1</issue><spage>181</spage><epage>185</epage><pages>181-185</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>The mitochondrial enzyme monoamine oxidase (MAO) A and B catalyze the oxidative deamination of various endogenous and exogenous biogenic amines. In the present study, we used human embryonic kidney 293 (HEK 293) cells stably transfected with human MAO-B cDNA to investigate the potential role of hydrogen peroxide (H2O2) produced by MAO-B isoform as an intracellular messenger involved in regulation of cell signaling and function. The MAO substrate tyramine induced tyrosine phosphorylation of Shc, ERK activation, and an increase in DNA synthesis in HEK 293 expressing MAO-B, but not in wild type HEK 293 cells, which do not express MAO. Tyramine effects were fully prevented by cell pretreatment with the MAO inhibitor pargyline or the antioxidant N-acetylcysteine. These results show that MAO-B induces MAPK/ERK activation and cell mitogenesis through H2O2 production.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>10777699</pmid><doi>10.1006/bbrc.2000.2524</doi><tpages>5</tpages></addata></record> |
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| subjects | Adaptor Proteins, Signal Transducing Adaptor Proteins, Vesicular Transport Adrenergic Uptake Inhibitors - pharmacology Blotting, Western Cell Division - drug effects Cell Line DNA, Complementary - metabolism Dose-Response Relationship, Drug extracellular signal-regulated protein kinase human embryonic kidney 293 cells Humans hydrogen peroxide Hydrogen Peroxide - metabolism Mitogen-Activated Protein Kinases - metabolism mitogenesis monoamine oxidase Monoamine Oxidase - metabolism Phosphorylation Precipitin Tests Proteins - metabolism Shc Signaling Adaptor Proteins Signal Transduction Src Homology 2 Domain-Containing, Transforming Protein 1 Time Factors Transfection Tyramine - pharmacology |
| title | Monoamine Oxidase B Induces ERK-Dependent Cell Mitogenesis by Hydrogen Peroxide Generation |
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