An SOD mimic protects NADP+-dependent isocitrate dehydrogenase against oxidative inactivation
The isocitrate dehydrogenases (ICDs) catalyse the oxidative decarboxylation of isocitrate to alpha-ketoglutarate and can use either NAD+ or NADP+ as a cofactor. Recent studies demonstrate that the NADP+-dependent isocitrate dehydrogenase, as a source of electrons for cellular antioxidants, is import...
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| Veröffentlicht in: | Free radical research 2008-07, Vol.42 (7), p.618-624 |
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| creator | Batinic-Haberle, Ines Benov, Ludmil T. |
| description | The isocitrate dehydrogenases (ICDs) catalyse the oxidative decarboxylation of isocitrate to alpha-ketoglutarate and can use either NAD+ or NADP+ as a cofactor. Recent studies demonstrate that the NADP+-dependent isocitrate dehydrogenase, as a source of electrons for cellular antioxidants, is important for protection against oxidative damage. ICD, however, is susceptible to oxidative inactivation, which in turn compromises cellular antioxidant defense. This study investigates the effect of a superoxide dismutase (SOD) mimic, MnTM-2-PyP5+, on the inactivation of NADP+-dependent ICD in SOD-deficient Escherichia coli and in diabetic rats. The findings show that E. coli ICD is inactivated by superoxide, but the inactivated enzyme is replaced by de novo protein synthesis. Statistically significant decrease of ICD activity was found in the hearts of diabetic rats. MnTM-2-PyP5+ protected ICD in both models. |
| doi_str_mv | 10.1080/10715760802209639 |
| format | Article |
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Recent studies demonstrate that the NADP+-dependent isocitrate dehydrogenase, as a source of electrons for cellular antioxidants, is important for protection against oxidative damage. ICD, however, is susceptible to oxidative inactivation, which in turn compromises cellular antioxidant defense. This study investigates the effect of a superoxide dismutase (SOD) mimic, MnTM-2-PyP5+, on the inactivation of NADP+-dependent ICD in SOD-deficient Escherichia coli and in diabetic rats. The findings show that E. coli ICD is inactivated by superoxide, but the inactivated enzyme is replaced by de novo protein synthesis. Statistically significant decrease of ICD activity was found in the hearts of diabetic rats. MnTM-2-PyP5+ protected ICD in both models.</description><identifier>ISSN: 1071-5762</identifier><identifier>EISSN: 1029-2470</identifier><identifier>DOI: 10.1080/10715760802209639</identifier><identifier>PMID: 18608518</identifier><language>eng</language><publisher>England: Informa UK Ltd</publisher><subject>Aconitate Hydratase - metabolism ; Animals ; diabetes ; Diabetes Mellitus, Experimental - drug therapy ; Diabetes Mellitus, Experimental - enzymology ; Enzyme Activation ; Escherichia coli - drug effects ; Escherichia coli - enzymology ; Escherichia coli - genetics ; Escherichia coli Proteins - genetics ; Escherichia coli Proteins - metabolism ; Free Radical Scavengers - pharmacology ; Isocitrate Dehydrogenase - biosynthesis ; Isocitrate Dehydrogenase - genetics ; Isocitrate Dehydrogenase - metabolism ; Isocitrate dehydrogenase inactivation ; Male ; manganese porphyrin ; Metalloporphyrins - pharmacology ; MnTM-2-PyP ; Myocardium - enzymology ; Oxidation-Reduction ; Oxidative Stress - drug effects ; Protein Biosynthesis ; Rats ; Rats, Wistar ; Reactive Nitrogen Species - metabolism ; SOD mimic ; Superoxide Dismutase - deficiency ; Superoxide Dismutase - genetics ; Superoxide Dismutase - metabolism ; Superoxides - metabolism ; Time Factors</subject><ispartof>Free radical research, 2008-07, Vol.42 (7), p.618-624</ispartof><rights>2008 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted 2008</rights><rights>2008 Informa UK Ltd. 2008</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4179-a38d5b5c79c4676a6a8ef6729507042180e414079c12337406c958fc529177ff3</citedby><cites>FETCH-LOGICAL-c4179-a38d5b5c79c4676a6a8ef6729507042180e414079c12337406c958fc529177ff3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.tandfonline.com/doi/pdf/10.1080/10715760802209639$$EPDF$$P50$$Ginformaworld$$H</linktopdf><linktohtml>$$Uhttps://www.tandfonline.com/doi/full/10.1080/10715760802209639$$EHTML$$P50$$Ginformaworld$$H</linktohtml><link.rule.ids>230,314,780,784,885,27924,27925,59647,60436,61221,61402</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18608518$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Batinic-Haberle, Ines</creatorcontrib><creatorcontrib>Benov, Ludmil T.</creatorcontrib><title>An SOD mimic protects NADP+-dependent isocitrate dehydrogenase against oxidative inactivation</title><title>Free radical research</title><addtitle>Free Radic Res</addtitle><description>The isocitrate dehydrogenases (ICDs) catalyse the oxidative decarboxylation of isocitrate to alpha-ketoglutarate and can use either NAD+ or NADP+ as a cofactor. Recent studies demonstrate that the NADP+-dependent isocitrate dehydrogenase, as a source of electrons for cellular antioxidants, is important for protection against oxidative damage. ICD, however, is susceptible to oxidative inactivation, which in turn compromises cellular antioxidant defense. This study investigates the effect of a superoxide dismutase (SOD) mimic, MnTM-2-PyP5+, on the inactivation of NADP+-dependent ICD in SOD-deficient Escherichia coli and in diabetic rats. The findings show that E. coli ICD is inactivated by superoxide, but the inactivated enzyme is replaced by de novo protein synthesis. Statistically significant decrease of ICD activity was found in the hearts of diabetic rats. MnTM-2-PyP5+ protected ICD in both models.</description><subject>Aconitate Hydratase - metabolism</subject><subject>Animals</subject><subject>diabetes</subject><subject>Diabetes Mellitus, Experimental - drug therapy</subject><subject>Diabetes Mellitus, Experimental - enzymology</subject><subject>Enzyme Activation</subject><subject>Escherichia coli - drug effects</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli Proteins - genetics</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Free Radical Scavengers - pharmacology</subject><subject>Isocitrate Dehydrogenase - biosynthesis</subject><subject>Isocitrate Dehydrogenase - genetics</subject><subject>Isocitrate Dehydrogenase - metabolism</subject><subject>Isocitrate dehydrogenase inactivation</subject><subject>Male</subject><subject>manganese porphyrin</subject><subject>Metalloporphyrins - pharmacology</subject><subject>MnTM-2-PyP</subject><subject>Myocardium - enzymology</subject><subject>Oxidation-Reduction</subject><subject>Oxidative Stress - drug effects</subject><subject>Protein Biosynthesis</subject><subject>Rats</subject><subject>Rats, Wistar</subject><subject>Reactive Nitrogen Species - metabolism</subject><subject>SOD mimic</subject><subject>Superoxide Dismutase - deficiency</subject><subject>Superoxide Dismutase - genetics</subject><subject>Superoxide Dismutase - metabolism</subject><subject>Superoxides - metabolism</subject><subject>Time Factors</subject><issn>1071-5762</issn><issn>1029-2470</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kF9LHDEUxUOpqF39AH0peS_TJplMMqGlsGhbBVFBfSzhbiazG5lJliT-2W9vll2qIviUE-75nXs5CH2m5BslLflOiaSNFEUyRpSo1Qe0TwlTFeOSfFxrSatiYHvoU0q3hNCaN3IX7dG2QA1t99G_qcdXF8d4dKMzeBlDtiYnfD49vvxadXZpfWd9xi4F43KEbHFnF6suhrn1kCyGOTifMg6ProPs7i12HkwR5RP8AdrpYUj2cPtO0M2f39dHJ9XZxd_To-lZZTiVqoK67ZpZY6QyXEgBAlrbC8lUQyThjLbEcspJGVNW15ITYVTT9qZhikrZ9_UE_drkLu9mo-1MOTnCoJfRjRBXOoDTryfeLfQ83OtacNIKVQLoJsDEkFK0_X-WEr3uWr_pujBfXi59JrblFsPPjcH5PsQRHkIcOp1hNYTYR_DGJV2_l__jFb6wMOSFgWj1bbiLvhT6znVP6ZWfow</recordid><startdate>200807</startdate><enddate>200807</enddate><creator>Batinic-Haberle, Ines</creator><creator>Benov, Ludmil T.</creator><general>Informa UK Ltd</general><general>Taylor & Francis</general><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>5PM</scope></search><sort><creationdate>200807</creationdate><title>An SOD mimic protects NADP+-dependent isocitrate dehydrogenase against oxidative inactivation</title><author>Batinic-Haberle, Ines ; Benov, Ludmil T.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4179-a38d5b5c79c4676a6a8ef6729507042180e414079c12337406c958fc529177ff3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Aconitate Hydratase - metabolism</topic><topic>Animals</topic><topic>diabetes</topic><topic>Diabetes Mellitus, Experimental - drug therapy</topic><topic>Diabetes Mellitus, Experimental - enzymology</topic><topic>Enzyme Activation</topic><topic>Escherichia coli - drug effects</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli Proteins - genetics</topic><topic>Escherichia coli Proteins - metabolism</topic><topic>Free Radical Scavengers - pharmacology</topic><topic>Isocitrate Dehydrogenase - biosynthesis</topic><topic>Isocitrate Dehydrogenase - genetics</topic><topic>Isocitrate Dehydrogenase - metabolism</topic><topic>Isocitrate dehydrogenase inactivation</topic><topic>Male</topic><topic>manganese porphyrin</topic><topic>Metalloporphyrins - pharmacology</topic><topic>MnTM-2-PyP</topic><topic>Myocardium - enzymology</topic><topic>Oxidation-Reduction</topic><topic>Oxidative Stress - drug effects</topic><topic>Protein Biosynthesis</topic><topic>Rats</topic><topic>Rats, Wistar</topic><topic>Reactive Nitrogen Species - metabolism</topic><topic>SOD mimic</topic><topic>Superoxide Dismutase - deficiency</topic><topic>Superoxide Dismutase - genetics</topic><topic>Superoxide Dismutase - metabolism</topic><topic>Superoxides - metabolism</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Batinic-Haberle, Ines</creatorcontrib><creatorcontrib>Benov, Ludmil T.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Free radical research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Batinic-Haberle, Ines</au><au>Benov, Ludmil T.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>An SOD mimic protects NADP+-dependent isocitrate dehydrogenase against oxidative inactivation</atitle><jtitle>Free radical research</jtitle><addtitle>Free Radic Res</addtitle><date>2008-07</date><risdate>2008</risdate><volume>42</volume><issue>7</issue><spage>618</spage><epage>624</epage><pages>618-624</pages><issn>1071-5762</issn><eissn>1029-2470</eissn><abstract>The isocitrate dehydrogenases (ICDs) catalyse the oxidative decarboxylation of isocitrate to alpha-ketoglutarate and can use either NAD+ or NADP+ as a cofactor. Recent studies demonstrate that the NADP+-dependent isocitrate dehydrogenase, as a source of electrons for cellular antioxidants, is important for protection against oxidative damage. ICD, however, is susceptible to oxidative inactivation, which in turn compromises cellular antioxidant defense. This study investigates the effect of a superoxide dismutase (SOD) mimic, MnTM-2-PyP5+, on the inactivation of NADP+-dependent ICD in SOD-deficient Escherichia coli and in diabetic rats. The findings show that E. coli ICD is inactivated by superoxide, but the inactivated enzyme is replaced by de novo protein synthesis. Statistically significant decrease of ICD activity was found in the hearts of diabetic rats. MnTM-2-PyP5+ protected ICD in both models.</abstract><cop>England</cop><pub>Informa UK Ltd</pub><pmid>18608518</pmid><doi>10.1080/10715760802209639</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Taylor & Francis Journals Complete |
| subjects | Aconitate Hydratase - metabolism Animals diabetes Diabetes Mellitus, Experimental - drug therapy Diabetes Mellitus, Experimental - enzymology Enzyme Activation Escherichia coli - drug effects Escherichia coli - enzymology Escherichia coli - genetics Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Free Radical Scavengers - pharmacology Isocitrate Dehydrogenase - biosynthesis Isocitrate Dehydrogenase - genetics Isocitrate Dehydrogenase - metabolism Isocitrate dehydrogenase inactivation Male manganese porphyrin Metalloporphyrins - pharmacology MnTM-2-PyP Myocardium - enzymology Oxidation-Reduction Oxidative Stress - drug effects Protein Biosynthesis Rats Rats, Wistar Reactive Nitrogen Species - metabolism SOD mimic Superoxide Dismutase - deficiency Superoxide Dismutase - genetics Superoxide Dismutase - metabolism Superoxides - metabolism Time Factors |
| title | An SOD mimic protects NADP+-dependent isocitrate dehydrogenase against oxidative inactivation |
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