Dopamine induces ERK activation in renal epithelial cells through H2O2 produced by monoamine oxidase
Dopamine induces ERK activation in renal epithelial cells through H2O2 produced by monoamine oxidase. The rat renal proximal tubule cells contain a large amount of monoamine oxidase, which catalyzes the oxidative deamination of catecholamines such as dopamine (DA). The aim of this study is to invest...
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| Veröffentlicht in: | Kidney international 2001-01, Vol.59 (1), p.76-86 |
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| description | Dopamine induces ERK activation in renal epithelial cells through H2O2 produced by monoamine oxidase.
The rat renal proximal tubule cells contain a large amount of monoamine oxidase, which catalyzes the oxidative deamination of catecholamines such as dopamine (DA). The aim of this study is to investigate the potential role of hydrogen peroxide (H2O2) produced by monoamine oxidase (MAO) isoform on regulation of cell signaling and function.
Primary rat proximal tubular cells, which contain almost exclusively MAO-A, and human embryonic kidney 293 (HEK 293) cells stably transfected with human MAO-B cDNA were treated with DA or tyramine in the presence or the absence of some inhibitors. Then, Shc protein tyrosine phosphorylation and extracellular-regulated kinase (ERK) activation were evaluated by immunoprecipitation/immunoblot analysis and cell proliferation by [3H]thymidine incorporation or cell counting.
In rat proximal tubule cells, DA induced tyrosine phosphorylation of Shc, ERK activation, and a significant increase in DNA synthesis. The involvement of MAO-dependent H2O2 generation induced by DA (5 μmol/L) was supported by the demonstration that the DA effects were (1) fully prevented by cell pretreatment with the MAO inhibitor pargyline, the antioxydant N-acetylcysteine (NAC), and the DA uptake inhibitor GBR 12909; (2) not abrogated by the D1 and D2 receptor antagonists; (3) observed in HEK 293 MAO-B cells but not in HEK 293 wild-type cells, which do not express MAO; and (4) similar to those induced by another MAO substrate, tyramine.
Taken together, these results show that in addition to the effects related to receptor stimulation, DA, and probably the other catecholamines, may induce some of its effects through the MAO-dependent H2O2 production. |
| doi_str_mv | 10.1046/j.1523-1755.2001.00468.x |
| format | Article |
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The rat renal proximal tubule cells contain a large amount of monoamine oxidase, which catalyzes the oxidative deamination of catecholamines such as dopamine (DA). The aim of this study is to investigate the potential role of hydrogen peroxide (H2O2) produced by monoamine oxidase (MAO) isoform on regulation of cell signaling and function.
Primary rat proximal tubular cells, which contain almost exclusively MAO-A, and human embryonic kidney 293 (HEK 293) cells stably transfected with human MAO-B cDNA were treated with DA or tyramine in the presence or the absence of some inhibitors. Then, Shc protein tyrosine phosphorylation and extracellular-regulated kinase (ERK) activation were evaluated by immunoprecipitation/immunoblot analysis and cell proliferation by [3H]thymidine incorporation or cell counting.
In rat proximal tubule cells, DA induced tyrosine phosphorylation of Shc, ERK activation, and a significant increase in DNA synthesis. The involvement of MAO-dependent H2O2 generation induced by DA (5 μmol/L) was supported by the demonstration that the DA effects were (1) fully prevented by cell pretreatment with the MAO inhibitor pargyline, the antioxydant N-acetylcysteine (NAC), and the DA uptake inhibitor GBR 12909; (2) not abrogated by the D1 and D2 receptor antagonists; (3) observed in HEK 293 MAO-B cells but not in HEK 293 wild-type cells, which do not express MAO; and (4) similar to those induced by another MAO substrate, tyramine.
Taken together, these results show that in addition to the effects related to receptor stimulation, DA, and probably the other catecholamines, may induce some of its effects through the MAO-dependent H2O2 production.</description><identifier>ISSN: 0085-2538</identifier><identifier>EISSN: 1523-1755</identifier><identifier>DOI: 10.1046/j.1523-1755.2001.00468.x</identifier><identifier>PMID: 11135060</identifier><identifier>CODEN: KDYIA5</identifier><language>eng</language><publisher>New York, NY: Elsevier Inc</publisher><subject>Adaptor Proteins, Signal Transducing ; Adaptor Proteins, Vesicular Transport ; amine oxidases ; Animals ; Biological and medical sciences ; catecholamines ; Cell Division - physiology ; Cells, Cultured ; Dopamine - pharmacology ; Enzyme Activation ; Fundamental and applied biological sciences. Psychology ; hydrogen peroxide ; Hydrogen Peroxide - metabolism ; Kidney Tubules, Proximal - cytology ; Kidney Tubules, Proximal - drug effects ; Kidney Tubules, Proximal - enzymology ; Kidney Tubules, Proximal - metabolism ; mitogen-activated protein kinases ; Mitogen-Activated Protein Kinases - metabolism ; Monoamine Oxidase - metabolism ; Phosphorylation ; Proteins - metabolism ; Rats ; Rats, Sprague-Dawley ; reactive oxygen species ; Shc Signaling Adaptor Proteins ; Src Homology 2 Domain-Containing, Transforming Protein 1 ; Substrate Specificity ; Thymidine - metabolism ; Tyramine - pharmacology ; Tyrosine - metabolism ; Vertebrates: urinary system</subject><ispartof>Kidney international, 2001-01, Vol.59 (1), p.76-86</ispartof><rights>2001 International Society of Nephrology</rights><rights>2001 INIST-CNRS</rights><rights>Copyright Nature Publishing Group Jan 2001</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c475t-5da20546ab9c4ae9a189af725bda8349f34943008216f922938faa8bad8ae0bb3</citedby><cites>FETCH-LOGICAL-c475t-5da20546ab9c4ae9a189af725bda8349f34943008216f922938faa8bad8ae0bb3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.proquest.com/docview/210172801?pq-origsite=primo$$EHTML$$P50$$Gproquest$$H</linktohtml><link.rule.ids>315,781,785,4025,27928,27929,27930,64390,64392,64394,72474</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=919535$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11135060$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Vindis, Cécile</creatorcontrib><creatorcontrib>Séguélas, Marie-Hélène</creatorcontrib><creatorcontrib>Lanier, Stephen</creatorcontrib><creatorcontrib>Parini, Angelo</creatorcontrib><creatorcontrib>Cambon, Claudie</creatorcontrib><title>Dopamine induces ERK activation in renal epithelial cells through H2O2 produced by monoamine oxidase</title><title>Kidney international</title><addtitle>Kidney Int</addtitle><description>Dopamine induces ERK activation in renal epithelial cells through H2O2 produced by monoamine oxidase.
The rat renal proximal tubule cells contain a large amount of monoamine oxidase, which catalyzes the oxidative deamination of catecholamines such as dopamine (DA). The aim of this study is to investigate the potential role of hydrogen peroxide (H2O2) produced by monoamine oxidase (MAO) isoform on regulation of cell signaling and function.
Primary rat proximal tubular cells, which contain almost exclusively MAO-A, and human embryonic kidney 293 (HEK 293) cells stably transfected with human MAO-B cDNA were treated with DA or tyramine in the presence or the absence of some inhibitors. Then, Shc protein tyrosine phosphorylation and extracellular-regulated kinase (ERK) activation were evaluated by immunoprecipitation/immunoblot analysis and cell proliferation by [3H]thymidine incorporation or cell counting.
In rat proximal tubule cells, DA induced tyrosine phosphorylation of Shc, ERK activation, and a significant increase in DNA synthesis. The involvement of MAO-dependent H2O2 generation induced by DA (5 μmol/L) was supported by the demonstration that the DA effects were (1) fully prevented by cell pretreatment with the MAO inhibitor pargyline, the antioxydant N-acetylcysteine (NAC), and the DA uptake inhibitor GBR 12909; (2) not abrogated by the D1 and D2 receptor antagonists; (3) observed in HEK 293 MAO-B cells but not in HEK 293 wild-type cells, which do not express MAO; and (4) similar to those induced by another MAO substrate, tyramine.
Taken together, these results show that in addition to the effects related to receptor stimulation, DA, and probably the other catecholamines, may induce some of its effects through the MAO-dependent H2O2 production.</description><subject>Adaptor Proteins, Signal Transducing</subject><subject>Adaptor Proteins, Vesicular Transport</subject><subject>amine oxidases</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>catecholamines</subject><subject>Cell Division - physiology</subject><subject>Cells, Cultured</subject><subject>Dopamine - pharmacology</subject><subject>Enzyme Activation</subject><subject>Fundamental and applied biological sciences. 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Psychology</topic><topic>hydrogen peroxide</topic><topic>Hydrogen Peroxide - metabolism</topic><topic>Kidney Tubules, Proximal - cytology</topic><topic>Kidney Tubules, Proximal - drug effects</topic><topic>Kidney Tubules, Proximal - enzymology</topic><topic>Kidney Tubules, Proximal - metabolism</topic><topic>mitogen-activated protein kinases</topic><topic>Mitogen-Activated Protein Kinases - metabolism</topic><topic>Monoamine Oxidase - metabolism</topic><topic>Phosphorylation</topic><topic>Proteins - metabolism</topic><topic>Rats</topic><topic>Rats, Sprague-Dawley</topic><topic>reactive oxygen species</topic><topic>Shc Signaling Adaptor Proteins</topic><topic>Src Homology 2 Domain-Containing, Transforming Protein 1</topic><topic>Substrate Specificity</topic><topic>Thymidine - metabolism</topic><topic>Tyramine - pharmacology</topic><topic>Tyrosine - metabolism</topic><topic>Vertebrates: urinary system</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vindis, Cécile</creatorcontrib><creatorcontrib>Séguélas, Marie-Hélène</creatorcontrib><creatorcontrib>Lanier, Stephen</creatorcontrib><creatorcontrib>Parini, Angelo</creatorcontrib><creatorcontrib>Cambon, Claudie</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Nursing & Allied Health Database</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>Proquest Central</collection><collection>ProQuest One Community College</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Nursing & Allied Health Premium</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>MEDLINE - Academic</collection><jtitle>Kidney international</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vindis, Cécile</au><au>Séguélas, Marie-Hélène</au><au>Lanier, Stephen</au><au>Parini, Angelo</au><au>Cambon, Claudie</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Dopamine induces ERK activation in renal epithelial cells through H2O2 produced by monoamine oxidase</atitle><jtitle>Kidney international</jtitle><addtitle>Kidney Int</addtitle><date>2001-01</date><risdate>2001</risdate><volume>59</volume><issue>1</issue><spage>76</spage><epage>86</epage><pages>76-86</pages><issn>0085-2538</issn><eissn>1523-1755</eissn><coden>KDYIA5</coden><abstract>Dopamine induces ERK activation in renal epithelial cells through H2O2 produced by monoamine oxidase.
The rat renal proximal tubule cells contain a large amount of monoamine oxidase, which catalyzes the oxidative deamination of catecholamines such as dopamine (DA). The aim of this study is to investigate the potential role of hydrogen peroxide (H2O2) produced by monoamine oxidase (MAO) isoform on regulation of cell signaling and function.
Primary rat proximal tubular cells, which contain almost exclusively MAO-A, and human embryonic kidney 293 (HEK 293) cells stably transfected with human MAO-B cDNA were treated with DA or tyramine in the presence or the absence of some inhibitors. Then, Shc protein tyrosine phosphorylation and extracellular-regulated kinase (ERK) activation were evaluated by immunoprecipitation/immunoblot analysis and cell proliferation by [3H]thymidine incorporation or cell counting.
In rat proximal tubule cells, DA induced tyrosine phosphorylation of Shc, ERK activation, and a significant increase in DNA synthesis. The involvement of MAO-dependent H2O2 generation induced by DA (5 μmol/L) was supported by the demonstration that the DA effects were (1) fully prevented by cell pretreatment with the MAO inhibitor pargyline, the antioxydant N-acetylcysteine (NAC), and the DA uptake inhibitor GBR 12909; (2) not abrogated by the D1 and D2 receptor antagonists; (3) observed in HEK 293 MAO-B cells but not in HEK 293 wild-type cells, which do not express MAO; and (4) similar to those induced by another MAO substrate, tyramine.
Taken together, these results show that in addition to the effects related to receptor stimulation, DA, and probably the other catecholamines, may induce some of its effects through the MAO-dependent H2O2 production.</abstract><cop>New York, NY</cop><pub>Elsevier Inc</pub><pmid>11135060</pmid><doi>10.1046/j.1523-1755.2001.00468.x</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adaptor Proteins, Signal Transducing Adaptor Proteins, Vesicular Transport amine oxidases Animals Biological and medical sciences catecholamines Cell Division - physiology Cells, Cultured Dopamine - pharmacology Enzyme Activation Fundamental and applied biological sciences. Psychology hydrogen peroxide Hydrogen Peroxide - metabolism Kidney Tubules, Proximal - cytology Kidney Tubules, Proximal - drug effects Kidney Tubules, Proximal - enzymology Kidney Tubules, Proximal - metabolism mitogen-activated protein kinases Mitogen-Activated Protein Kinases - metabolism Monoamine Oxidase - metabolism Phosphorylation Proteins - metabolism Rats Rats, Sprague-Dawley reactive oxygen species Shc Signaling Adaptor Proteins Src Homology 2 Domain-Containing, Transforming Protein 1 Substrate Specificity Thymidine - metabolism Tyramine - pharmacology Tyrosine - metabolism Vertebrates: urinary system |
| title | Dopamine induces ERK activation in renal epithelial cells through H2O2 produced by monoamine oxidase |
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