Modulation of the activity of the NADPH oxidase system by reactive oxygen species: influence of catalase

The nicotinamide adenine dinucleotide phosphate oxidase complex (Nox) is a major source of non-mitochondrial reactive oxygen species in cells. Nox contains both membrane (Cytb(558)) and cytosolic (p40(phox), p47(phox), p67(phox) and Rac) components. Nox has been submitted to a combination of oxygen...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Radiation protection dosimetry 2011-02, Vol.143 (2-4), p.166-171
Hauptverfasser:	Ostuni, Mariano A, Bizouarn, Tania, Baciou, Laura, Houée-Levin, Chantal
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Catalase - metabolism Cattle Cell Membrane - metabolism Cell-Free System Dosimetry Enzyme Activation Enzyme Stability hydrogen peroxide inactivation Irradiation Membranes NADP - metabolism Oxygen Phosphates Reactive Oxygen Species - metabolism
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

container_end_page	171
container_issue	2-4
container_start_page	166
container_title	Radiation protection dosimetry
container_volume	143
creator	Ostuni, Mariano A Bizouarn, Tania Baciou, Laura Houée-Levin, Chantal
description	The nicotinamide adenine dinucleotide phosphate oxidase complex (Nox) is a major source of non-mitochondrial reactive oxygen species in cells. Nox contains both membrane (Cytb(558)) and cytosolic (p40(phox), p47(phox), p67(phox) and Rac) components. Nox has been submitted to a combination of oxygen free radicals produced by irradiation and to hydrogen peroxide. Irradiation of a single component with high doses led to partial inactivation; however, the irradiation of the whole system during its assembly phase with lower doses (2-10 Gy) led either to activation (2.7 Gy) or to strong inactivation if irradiation took place during the first minute of the assembly. Incubation of the membrane fractions or of p67(phox) with H(2)O(2) led to fast inactivation. Catalase protected weakly p67(phox) from H(2)O(2). Conversely, incubation of the membrane fractions with catalase led to over-activation of the system.
doi_str_mv	10.1093/rpd/ncq518
format	Article
fullrecord	<record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_918057110</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>855198531</sourcerecordid><originalsourceid>FETCH-LOGICAL-c318t-1a447604b9595da0c4fb427590f28ab5a348a4afe194df3079082f3af1d552d03</originalsourceid><addsrcrecordid>eNqFkctOwzAQRS0EoqWw4QOQd0hIoZ7Ybmx2VXkUqTwWsI4cZ0yD0iSNE0T-npS2bFmNRnPuXcwh5BzYNTDNx3WVjgu7lqAOyBAiEQZcsMkhGTIQIlAiZANy4v0nY2GkpTgmgxBAccnVkCyfyrTNTZOVBS0dbZZIjW2yr6zp9vvz9PZ1TsvvLDUeqe98gyuadLTGXxL7U_eBBfUV2gz9Dc0Kl7dYWNw0WNOYvA-ekiNnco9nuzki7_d3b7N5sHh5eJxNF4HloJoAjBDRhIlESy1Tw6xwiQgjqZkLlUmk4UIZYRyCFqnjLNJMhY4bB6mUYcr4iFxue6u6XLfom3iVeYt5bgosWx9rUExGAP-TSkrQSnLoyastaevS-xpdXNXZytRdDCzeKIh7BfFWQQ9f7GrbZIXpH7r_Of8BbQiCjg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>855198531</pqid></control><display><type>article</type><title>Modulation of the activity of the NADPH oxidase system by reactive oxygen species: influence of catalase</title><source>Oxford University Press Journals All Titles (1996-Current)</source><source>MEDLINE</source><source>Alma/SFX Local Collection</source><creator>Ostuni, Mariano A ; Bizouarn, Tania ; Baciou, Laura ; Houée-Levin, Chantal</creator><creatorcontrib>Ostuni, Mariano A ; Bizouarn, Tania ; Baciou, Laura ; Houée-Levin, Chantal</creatorcontrib><description>The nicotinamide adenine dinucleotide phosphate oxidase complex (Nox) is a major source of non-mitochondrial reactive oxygen species in cells. Nox contains both membrane (Cytb(558)) and cytosolic (p40(phox), p47(phox), p67(phox) and Rac) components. Nox has been submitted to a combination of oxygen free radicals produced by irradiation and to hydrogen peroxide. Irradiation of a single component with high doses led to partial inactivation; however, the irradiation of the whole system during its assembly phase with lower doses (2-10 Gy) led either to activation (2.7 Gy) or to strong inactivation if irradiation took place during the first minute of the assembly. Incubation of the membrane fractions or of p67(phox) with H(2)O(2) led to fast inactivation. Catalase protected weakly p67(phox) from H(2)O(2). Conversely, incubation of the membrane fractions with catalase led to over-activation of the system.</description><identifier>ISSN: 0144-8420</identifier><identifier>EISSN: 1742-3406</identifier><identifier>DOI: 10.1093/rpd/ncq518</identifier><identifier>PMID: 21183538</identifier><language>eng</language><publisher>England</publisher><subject>Animals ; Catalase - metabolism ; Cattle ; Cell Membrane - metabolism ; Cell-Free System ; Dosimetry ; Enzyme Activation ; Enzyme Stability ; hydrogen peroxide ; inactivation ; Irradiation ; Membranes ; NADP - metabolism ; Oxygen ; Phosphates ; Reactive Oxygen Species - metabolism</subject><ispartof>Radiation protection dosimetry, 2011-02, Vol.143 (2-4), p.166-171</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c318t-1a447604b9595da0c4fb427590f28ab5a348a4afe194df3079082f3af1d552d03</citedby><cites>FETCH-LOGICAL-c318t-1a447604b9595da0c4fb427590f28ab5a348a4afe194df3079082f3af1d552d03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21183538$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ostuni, Mariano A</creatorcontrib><creatorcontrib>Bizouarn, Tania</creatorcontrib><creatorcontrib>Baciou, Laura</creatorcontrib><creatorcontrib>Houée-Levin, Chantal</creatorcontrib><title>Modulation of the activity of the NADPH oxidase system by reactive oxygen species: influence of catalase</title><title>Radiation protection dosimetry</title><addtitle>Radiat Prot Dosimetry</addtitle><description>The nicotinamide adenine dinucleotide phosphate oxidase complex (Nox) is a major source of non-mitochondrial reactive oxygen species in cells. Nox contains both membrane (Cytb(558)) and cytosolic (p40(phox), p47(phox), p67(phox) and Rac) components. Nox has been submitted to a combination of oxygen free radicals produced by irradiation and to hydrogen peroxide. Irradiation of a single component with high doses led to partial inactivation; however, the irradiation of the whole system during its assembly phase with lower doses (2-10 Gy) led either to activation (2.7 Gy) or to strong inactivation if irradiation took place during the first minute of the assembly. Incubation of the membrane fractions or of p67(phox) with H(2)O(2) led to fast inactivation. Catalase protected weakly p67(phox) from H(2)O(2). Conversely, incubation of the membrane fractions with catalase led to over-activation of the system.</description><subject>Animals</subject><subject>Catalase - metabolism</subject><subject>Cattle</subject><subject>Cell Membrane - metabolism</subject><subject>Cell-Free System</subject><subject>Dosimetry</subject><subject>Enzyme Activation</subject><subject>Enzyme Stability</subject><subject>hydrogen peroxide</subject><subject>inactivation</subject><subject>Irradiation</subject><subject>Membranes</subject><subject>NADP - metabolism</subject><subject>Oxygen</subject><subject>Phosphates</subject><subject>Reactive Oxygen Species - metabolism</subject><issn>0144-8420</issn><issn>1742-3406</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkctOwzAQRS0EoqWw4QOQd0hIoZ7Ybmx2VXkUqTwWsI4cZ0yD0iSNE0T-npS2bFmNRnPuXcwh5BzYNTDNx3WVjgu7lqAOyBAiEQZcsMkhGTIQIlAiZANy4v0nY2GkpTgmgxBAccnVkCyfyrTNTZOVBS0dbZZIjW2yr6zp9vvz9PZ1TsvvLDUeqe98gyuadLTGXxL7U_eBBfUV2gz9Dc0Kl7dYWNw0WNOYvA-ekiNnco9nuzki7_d3b7N5sHh5eJxNF4HloJoAjBDRhIlESy1Tw6xwiQgjqZkLlUmk4UIZYRyCFqnjLNJMhY4bB6mUYcr4iFxue6u6XLfom3iVeYt5bgosWx9rUExGAP-TSkrQSnLoyastaevS-xpdXNXZytRdDCzeKIh7BfFWQQ9f7GrbZIXpH7r_Of8BbQiCjg</recordid><startdate>20110201</startdate><enddate>20110201</enddate><creator>Ostuni, Mariano A</creator><creator>Bizouarn, Tania</creator><creator>Baciou, Laura</creator><creator>Houée-Levin, Chantal</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7ST</scope><scope>C1K</scope><scope>SOI</scope></search><sort><creationdate>20110201</creationdate><title>Modulation of the activity of the NADPH oxidase system by reactive oxygen species: influence of catalase</title><author>Ostuni, Mariano A ; Bizouarn, Tania ; Baciou, Laura ; Houée-Levin, Chantal</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c318t-1a447604b9595da0c4fb427590f28ab5a348a4afe194df3079082f3af1d552d03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Animals</topic><topic>Catalase - metabolism</topic><topic>Cattle</topic><topic>Cell Membrane - metabolism</topic><topic>Cell-Free System</topic><topic>Dosimetry</topic><topic>Enzyme Activation</topic><topic>Enzyme Stability</topic><topic>hydrogen peroxide</topic><topic>inactivation</topic><topic>Irradiation</topic><topic>Membranes</topic><topic>NADP - metabolism</topic><topic>Oxygen</topic><topic>Phosphates</topic><topic>Reactive Oxygen Species - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ostuni, Mariano A</creatorcontrib><creatorcontrib>Bizouarn, Tania</creatorcontrib><creatorcontrib>Baciou, Laura</creatorcontrib><creatorcontrib>Houée-Levin, Chantal</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><collection>Environment Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Environment Abstracts</collection><jtitle>Radiation protection dosimetry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ostuni, Mariano A</au><au>Bizouarn, Tania</au><au>Baciou, Laura</au><au>Houée-Levin, Chantal</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Modulation of the activity of the NADPH oxidase system by reactive oxygen species: influence of catalase</atitle><jtitle>Radiation protection dosimetry</jtitle><addtitle>Radiat Prot Dosimetry</addtitle><date>2011-02-01</date><risdate>2011</risdate><volume>143</volume><issue>2-4</issue><spage>166</spage><epage>171</epage><pages>166-171</pages><issn>0144-8420</issn><eissn>1742-3406</eissn><abstract>The nicotinamide adenine dinucleotide phosphate oxidase complex (Nox) is a major source of non-mitochondrial reactive oxygen species in cells. Nox contains both membrane (Cytb(558)) and cytosolic (p40(phox), p47(phox), p67(phox) and Rac) components. Nox has been submitted to a combination of oxygen free radicals produced by irradiation and to hydrogen peroxide. Irradiation of a single component with high doses led to partial inactivation; however, the irradiation of the whole system during its assembly phase with lower doses (2-10 Gy) led either to activation (2.7 Gy) or to strong inactivation if irradiation took place during the first minute of the assembly. Incubation of the membrane fractions or of p67(phox) with H(2)O(2) led to fast inactivation. Catalase protected weakly p67(phox) from H(2)O(2). Conversely, incubation of the membrane fractions with catalase led to over-activation of the system.</abstract><cop>England</cop><pmid>21183538</pmid><doi>10.1093/rpd/ncq518</doi><tpages>6</tpages></addata></record>
fulltext	fulltext
identifier	ISSN: 0144-8420
ispartof	Radiation protection dosimetry, 2011-02, Vol.143 (2-4), p.166-171
issn	0144-8420 1742-3406
language	eng
recordid	cdi_proquest_miscellaneous_918057110
source	Oxford University Press Journals All Titles (1996-Current); MEDLINE; Alma/SFX Local Collection
subjects	Animals Catalase - metabolism Cattle Cell Membrane - metabolism Cell-Free System Dosimetry Enzyme Activation Enzyme Stability hydrogen peroxide inactivation Irradiation Membranes NADP - metabolism Oxygen Phosphates Reactive Oxygen Species - metabolism
title	Modulation of the activity of the NADPH oxidase system by reactive oxygen species: influence of catalase
url	https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-05T06%3A26%3A29IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Modulation%20of%20the%20activity%20of%20the%20NADPH%20oxidase%20system%20by%20reactive%20oxygen%20species:%20influence%20of%20catalase&rft.jtitle=Radiation%20protection%20dosimetry&rft.au=Ostuni,%20Mariano%20A&rft.date=2011-02-01&rft.volume=143&rft.issue=2-4&rft.spage=166&rft.epage=171&rft.pages=166-171&rft.issn=0144-8420&rft.eissn=1742-3406&rft_id=info:doi/10.1093/rpd/ncq518&rft_dat=%3Cproquest_cross%3E855198531%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=855198531&rft_id=info:pmid/21183538&rfr_iscdi=true