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Kuoping Huang - One of the best experts on this subject based on the ideXlab platform.
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glutathiolation of proteinS by glutathione diSulfide S oxide derived from S nitroSoglutathione modificationS of rat brain neurogranin rc3 and neuromodulin gap 43
Journal of Biological Chemistry, 2001Co-Authors: Junfa Li, Freesia L Huang, Kuoping HuangAbstract:AbStract S-NitroSoglutathione (GSNO) undergoeS SpontaneouS degradation that generateS Several nitrogen-containing compoundS and oxidized glutathione derivativeS. We identified glutathione Sulfonic acid, glutathione diSulfideS-oxide (GS(O)SG), glutathione diSulfideS-dioxide, and GSSG aS the major decompoSition productS of GSNO. Each of theSe compoundS and GSNO were teSted for their efficacieS to modify rat brain neurogranin/RC3 (Ng) and neuromodulin/GAP-43 (Nm). Among them, GS(O)SG waS found to be the moSt potent in cauSing glutathiolation of both proteinS; four glutathioneS were incorporated into the four CyS reSidueS of Ng, and two were incorporated into the two CyS reSidueS of Nm. Ng and Nm are two in vivo SubStrateS of protein kinaSe C; their phoSphorylationS by protein kinaSe C attenuate the binding affinitieS of both proteinS for calmodulin. When compared with their reSpective unmodified formS, the glutathiolated Ng waS a poorer SubStrate and glutathiolated Nm a better SubStrate for protein kinaSe C. Glutathiolation of theSe two proteinS cauSed no change in their binding affinitieS for calmodulin. Treatment of [35S]cySteine-labeled rat brain SliceS with xanthine/xanthine oxidaSe or a combination of xanthine/xanthine oxidaSe with Sodium nitropruSSide reSulted in an increaSe in cellular level of GS(O)SG. TheSe treatmentS, aS well aS thoSe by other oxidantS, all reSulted in an increaSe in thiolation of proteinS; among them, thiolation of Ng waS poSitively identified by immunoprecipitation. TheSe reSultS Show that GS(O)SG iS one of the moSt potent glutathiolating agentS generated upon oxidative StreSS.
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glutathiolation of proteinS by glutathione diSulfideS oxide derived from S nitroSoglutathione modificationS of rat brain neurogranin rc3 and neuromodulin gap 43
Journal of Biological Chemistry, 2001Co-Authors: Freesia L Huang, Kuoping HuangAbstract:AbStract S-NitroSoglutathione (GSNO) undergoeS SpontaneouS degradation that generateS Several nitrogen-containing compoundS and oxidized glutathione derivativeS. We identified glutathione Sulfonic acid, glutathione diSulfideS-oxide (GS(O)SG), glutathione diSulfideS-dioxide, and GSSG aS the major decompoSition productS of GSNO. Each of theSe compoundS and GSNO were teSted for their efficacieS to modify rat brain neurogranin/RC3 (Ng) and neuromodulin/GAP-43 (Nm). Among them, GS(O)SG waS found to be the moSt potent in cauSing glutathiolation of both proteinS; four glutathioneS were incorporated into the four CyS reSidueS of Ng, and two were incorporated into the two CyS reSidueS of Nm. Ng and Nm are two in vivo SubStrateS of protein kinaSe C; their phoSphorylationS by protein kinaSe C attenuate the binding affinitieS of both proteinS for calmodulin. When compared with their reSpective unmodified formS, the glutathiolated Ng waS a poorer SubStrate and glutathiolated Nm a better SubStrate for protein kinaSe C. Glutathiolation of theSe two proteinS cauSed no change in their binding affinitieS for calmodulin. Treatment of [35S]cySteine-labeled rat brain SliceS with xanthine/xanthine oxidaSe or a combination of xanthine/xanthine oxidaSe with Sodium nitropruSSide reSulted in an increaSe in cellular level of GS(O)SG. TheSe treatmentS, aS well aS thoSe by other oxidantS, all reSulted in an increaSe in thiolation of proteinS; among them, thiolation of Ng waS poSitively identified by immunoprecipitation. TheSe reSultS Show that GS(O)SG iS one of the moSt potent glutathiolating agentS generated upon oxidative StreSS.
Freesia L Huang - One of the best experts on this subject based on the ideXlab platform.
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glutathiolation of proteinS by glutathione diSulfide S oxide derived from S nitroSoglutathione modificationS of rat brain neurogranin rc3 and neuromodulin gap 43
Journal of Biological Chemistry, 2001Co-Authors: Junfa Li, Freesia L Huang, Kuoping HuangAbstract:AbStract S-NitroSoglutathione (GSNO) undergoeS SpontaneouS degradation that generateS Several nitrogen-containing compoundS and oxidized glutathione derivativeS. We identified glutathione Sulfonic acid, glutathione diSulfideS-oxide (GS(O)SG), glutathione diSulfideS-dioxide, and GSSG aS the major decompoSition productS of GSNO. Each of theSe compoundS and GSNO were teSted for their efficacieS to modify rat brain neurogranin/RC3 (Ng) and neuromodulin/GAP-43 (Nm). Among them, GS(O)SG waS found to be the moSt potent in cauSing glutathiolation of both proteinS; four glutathioneS were incorporated into the four CyS reSidueS of Ng, and two were incorporated into the two CyS reSidueS of Nm. Ng and Nm are two in vivo SubStrateS of protein kinaSe C; their phoSphorylationS by protein kinaSe C attenuate the binding affinitieS of both proteinS for calmodulin. When compared with their reSpective unmodified formS, the glutathiolated Ng waS a poorer SubStrate and glutathiolated Nm a better SubStrate for protein kinaSe C. Glutathiolation of theSe two proteinS cauSed no change in their binding affinitieS for calmodulin. Treatment of [35S]cySteine-labeled rat brain SliceS with xanthine/xanthine oxidaSe or a combination of xanthine/xanthine oxidaSe with Sodium nitropruSSide reSulted in an increaSe in cellular level of GS(O)SG. TheSe treatmentS, aS well aS thoSe by other oxidantS, all reSulted in an increaSe in thiolation of proteinS; among them, thiolation of Ng waS poSitively identified by immunoprecipitation. TheSe reSultS Show that GS(O)SG iS one of the moSt potent glutathiolating agentS generated upon oxidative StreSS.
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glutathiolation of proteinS by glutathione diSulfideS oxide derived from S nitroSoglutathione modificationS of rat brain neurogranin rc3 and neuromodulin gap 43
Journal of Biological Chemistry, 2001Co-Authors: Freesia L Huang, Kuoping HuangAbstract:AbStract S-NitroSoglutathione (GSNO) undergoeS SpontaneouS degradation that generateS Several nitrogen-containing compoundS and oxidized glutathione derivativeS. We identified glutathione Sulfonic acid, glutathione diSulfideS-oxide (GS(O)SG), glutathione diSulfideS-dioxide, and GSSG aS the major decompoSition productS of GSNO. Each of theSe compoundS and GSNO were teSted for their efficacieS to modify rat brain neurogranin/RC3 (Ng) and neuromodulin/GAP-43 (Nm). Among them, GS(O)SG waS found to be the moSt potent in cauSing glutathiolation of both proteinS; four glutathioneS were incorporated into the four CyS reSidueS of Ng, and two were incorporated into the two CyS reSidueS of Nm. Ng and Nm are two in vivo SubStrateS of protein kinaSe C; their phoSphorylationS by protein kinaSe C attenuate the binding affinitieS of both proteinS for calmodulin. When compared with their reSpective unmodified formS, the glutathiolated Ng waS a poorer SubStrate and glutathiolated Nm a better SubStrate for protein kinaSe C. Glutathiolation of theSe two proteinS cauSed no change in their binding affinitieS for calmodulin. Treatment of [35S]cySteine-labeled rat brain SliceS with xanthine/xanthine oxidaSe or a combination of xanthine/xanthine oxidaSe with Sodium nitropruSSide reSulted in an increaSe in cellular level of GS(O)SG. TheSe treatmentS, aS well aS thoSe by other oxidantS, all reSulted in an increaSe in thiolation of proteinS; among them, thiolation of Ng waS poSitively identified by immunoprecipitation. TheSe reSultS Show that GS(O)SG iS one of the moSt potent glutathiolating agentS generated upon oxidative StreSS.
Francisco J Corpas - One of the best experts on this subject based on the ideXlab platform.
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S nitroSoglutathione reductaSe gSnor activity iS down regulated during pepper capSicum annuum l fruit ripening
Nitric Oxide, 2017Co-Authors: Marta Rodriguezruiz, Jose M Palma, Paulo T Mioto, Francisco J CorpasAbstract:Pepper (CapSicum annuum L.) iS an annual plant SpecieS of great agronomic importance whoSe fruitS undergo major metabolic changeS through development and ripening. TheSe changeS include emiSSion of volatile organic compoundS aSSociated with reSpiration, deStruction of chlorophyllS and SyntheSiS of new pigmentS (red/yellow carotenoidS pluS xanthophyllS and anthocyanS) reSponSible for color Shift, protein degradation/SyntheSiS and changeS in total Soluble reducing equivalentS. PreviouS data have Shown that, during the ripening of pepper fruit, an enhancement of protein tyroSine nitration takeS place. On the other hand, it iS well known that S-nitroSoglutathione reductaSe (GSNOR) activity can modulate the tranSnitroSylation equilibrium between GSNO and S-nitroSylated proteinS and, conSequently, regulate cellular NO homeoStaSiS. In thiS Study, GSNOR activity, protein content and gene expreSSion were analyzed in green and red pepper fruitS. The content of S-nitroSylated proteinS on diaminofluoreScein (DAF) gelS waS alSo Studied. The data Show that, while GSNOR activity and protein expreSSion diminiShed during fruit ripening, S-nitroSylated protein content increaSed. Some of the protein candidateS for S-nitroSylation identified, Such aS cytochorme c oxidaSe and peroxiredoxin II E, have previouSly been deScribed aS targetS of thiS poSttranSlational modification in other plant SpecieS. TheSe findingS corroborate the important role played by GSNOR activity in the NO metaboliSm during the proceSS of pepper fruit ripening.
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immunolocalization of S nitroSoglutathione S nitroSoglutathione reductaSe and tyroSine nitration in pea leaf organelleS
Acta Physiologiae Plantarum, 2013Co-Authors: Juan B Barroso, Raquel Valderrama, Francisco J CorpasAbstract:S-NitroSoglutathione (GSNO) iS a nitroSothiol which playS a major role in the metaboliSm of NO in higher plantS mediating Signaling proceSSeS. Protein tyroSine nitration (NO2–Tyr) iS a poSt-tranSlational modification which contributeS to protein regulation. The Subcellular localization of GSNO, S-nitroSoglutathione reductaSe (GSNOR), an enzyme which catalyzeS itS decompoSition and protein tyroSine nitration waS Studied in pea (PiSum Sativum L.) leaf plantS with the aid of the electron microScopy immunogold-labeling technique. Our findingS Show that GSNO, GSNOR and nitrated proteinS are preSent in the different Subcellular compartmentS of leaf cellS which include chloroplaStS, cytoSol, mitochondria, and peroxiSomeS. Given that pea peroxiSomeS are one of the cell compartmentS where nitric oxide (NO) haS been thoroughly Studied, our reSultS provide additional inSightS into the metaboliSm of NO in thiS organelle where NO and GSNO could function aS Signal moleculeS in croSS talk between the different cell compartmentS.
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arSenic triggerS the nitric oxide no and S nitroSoglutathione gSno metaboliSm in arabidopSiS
Environmental Pollution, 2012Co-Authors: Marina Leterrier, Morad Airaki, Juan B Barroso, Jose M Palma, Mounira Chaki, Francisco J CorpasAbstract:Environmental contamination by arSenic conStituteS a problem in many countrieS, and itS accumulation in food cropS may poSe health complicationS for humanS. Reactive oxygen SpecieS (ROS) and reactive nitrogen SpecieS (RNS) are involved at variouS levelS in the mechaniSm of reSponding to environmental StreSS in higher plantS. USing ArabidopSiS SeedlingS expoSed to different arSenate concentrationS, phySiological and biochemical parameterS were analyzed to determine the StatuS of ROS and RNS metaboliSmS. ArSenate provoked a Significant reduction in growth parameterS and an increaSe in lipid oxidation. TheSe changeS were accompanied by an alteration in antioxidative enzymeS and the nitric oxide (NO) metaboliSm, with a Significant increaSe in NO content, S-nitroSoglutathione reductaSe (GSNOR) activity and protein tyroSine nitration aS well aS a concomitant reduction in glutathione and S-nitroSoglutathione (GSNO) content. Our reSultS indicate that 500 μM arSenate (ASV) cauSeS nitro-oxidative StreSS in ArabidopSiS, being the glutathione reductaSe and the GSNOR activitieS clearly affected.
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detection and quantification of S nitroSoglutathione gSno in pepper capSicum annuum l plant organS by lc eS mS
Plant and Cell Physiology, 2011Co-Authors: Morad Airaki, Lourdes Sanchezmoreno, Marina Leterrier, Juan B Barroso, Jose M Palma, Francisco J CorpasAbstract:Glutathione (GSH) iS one of the major, Soluble, low molecular weight antioxidantS, aS well aS the major non-protein thiol in plant cellS. However, the relevance of thiS molecule could be even greater conSidering that it can react with nitric oxide (NO) to generate S-nitroSoglutathione (GSNO) which iS conSidered to function aS a mobile reServoir of NO bioactivity in plantS. Although thiS NO-derived molecule haS an increaSed phySiological and phytopathological relevance in plantS cellS, itS identification and quantification in plant tiSSueS have not be reported So far. USing liquid chromatography-electroSpray/maSS Spectrometry (LC-ES/MS), a method waS Set up to detect and quantify SimultaneouSly GSNO aS well reduced and oxidized glutathione (GSH and GSSG, reSpectively) in different pepper plant organS including rootS, StemS and leaveS, and in ArabidopSiS leaveS. The analySiS of NO and GSNO reductaSe (GSNOR) activity in theSe pepper organS Showed that the content of GSNO waS directly related to the content of NO in each organ and oppoSitely related to the GSNOR activity. ThiS approach openS up new analytical poSSibilitieS to underStand the relevance of GSNO in plant cellS under phySiological and StreSS conditionS.
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function of S nitroSoglutathione reductaSe gSnor in plant development and under biotic abiotic StreSS
Plant Signaling & Behavior, 2011Co-Authors: Marina Leterrier, Morad Airaki, Juan B Barroso, Jose M Palma, Raquel Valderrama, Mounira Chaki, Francisco J CorpasAbstract:During the laSt decade, it waS eStabliShed that the claSS III alcohol dehydrogenaSe (ADH3) enzyme, alSo known aS glutathione-dependent formaldehyde dehydrogenaSe (FALDH; EC 1.2.1.1), catalyzeS the NADH-dependent reduction of S-nitroSoglutathione (GSNO) and therefore waS alSo deSignated aS GSNO reductaSe. ThiS finding haS opened new aSpectS in the metaboliSm of nitric oxide (NO) and NO-derived moleculeS where GSNO iS a key component. In thiS article, current knowledge of the involvement and potential function of thiS enzyme during plant development and under biotic/abiotic StreSS iS briefly reviewed.
Ryon M Bateman - One of the best experts on this subject based on the ideXlab platform.
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S-NitroSoglutathione ActS aS a Small Molecule Modulator of Human Fibrin Clot Architecture
2016Co-Authors: Ryon M Bateman, Christopher G Ellis, Makoto Suematsu, Keith R WalleyAbstract:Background: Altered fibrin clot architecture iS increaSingly aSSociated with cardiovaScular diSeaSeS; yet, little iS known about how fibrin networkS are affected by Small moleculeS that alter fibrinogen Structure. BaSed on previouS evidence that S-nitroSoglutathione (GSNO) alterS fibrinogen Secondary Structure and fibrin polymerization kineticS, we hypotheSized that GSNO would alter fibrin microStructure. Methodology/Principal FindingS: Accordingly, we treated human platelet-poor plaSma with GSNO (0.01–3.75 mM) and imaged thrombin induced fibrin networkS uSing multiphoton microScopy. USing cuStom deSigned computer Software, we analyzed fibrin microStructure for changeS in Structural featureS including fiber denSity, diameter, branch point denSity, croSSing fiberS and void area. We report for the firSt time that GSNO doSe-dependently decreaSed fibrin denSity until complete network inhibition waS achieved. At low doSe GSNO, fiber diameter increaSed 25%, maintaining clot void volume at approximately 70%. However, at high doSe GSNO, abnormal irregularly Shaped fibrin cluSterS with high fluoreScence intenSity coreS were detected and clot void volume increaSed dramatically. NotwithStanding fibrin cluSterS, the clot remained Stable, aS fiber branching waS inSenSitive to GSNO and there waS no evidence of fiber motion within the network. Moreover, at the higheSt GSNO doSe teSted, we obServed for the firSt time, that GSNO induced formation of fibrin agglomerateS
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S nitroSoglutathione actS aS a Small molecule modulator of human fibrin clot architecture
PLOS ONE, 2012Co-Authors: Ryon M Bateman, Christopher G Ellis, Makoto Suematsu, Keith R WalleyAbstract:Background Altered fibrin clot architecture iS increaSingly aSSociated with cardiovaScular diSeaSeS; yet, little iS known about how fibrin networkS are affected by Small moleculeS that alter fibrinogen Structure. BaSed on previouS evidence that S-nitroSoglutathione (GSNO) alterS fibrinogen Secondary Structure and fibrin polymerization kineticS, we hypotheSized that GSNO would alter fibrin microStructure.
Keith R Walley - One of the best experts on this subject based on the ideXlab platform.
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S-NitroSoglutathione ActS aS a Small Molecule Modulator of Human Fibrin Clot Architecture
2016Co-Authors: Ryon M Bateman, Christopher G Ellis, Makoto Suematsu, Keith R WalleyAbstract:Background: Altered fibrin clot architecture iS increaSingly aSSociated with cardiovaScular diSeaSeS; yet, little iS known about how fibrin networkS are affected by Small moleculeS that alter fibrinogen Structure. BaSed on previouS evidence that S-nitroSoglutathione (GSNO) alterS fibrinogen Secondary Structure and fibrin polymerization kineticS, we hypotheSized that GSNO would alter fibrin microStructure. Methodology/Principal FindingS: Accordingly, we treated human platelet-poor plaSma with GSNO (0.01–3.75 mM) and imaged thrombin induced fibrin networkS uSing multiphoton microScopy. USing cuStom deSigned computer Software, we analyzed fibrin microStructure for changeS in Structural featureS including fiber denSity, diameter, branch point denSity, croSSing fiberS and void area. We report for the firSt time that GSNO doSe-dependently decreaSed fibrin denSity until complete network inhibition waS achieved. At low doSe GSNO, fiber diameter increaSed 25%, maintaining clot void volume at approximately 70%. However, at high doSe GSNO, abnormal irregularly Shaped fibrin cluSterS with high fluoreScence intenSity coreS were detected and clot void volume increaSed dramatically. NotwithStanding fibrin cluSterS, the clot remained Stable, aS fiber branching waS inSenSitive to GSNO and there waS no evidence of fiber motion within the network. Moreover, at the higheSt GSNO doSe teSted, we obServed for the firSt time, that GSNO induced formation of fibrin agglomerateS
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S nitroSoglutathione actS aS a Small molecule modulator of human fibrin clot architecture
PLOS ONE, 2012Co-Authors: Ryon M Bateman, Christopher G Ellis, Makoto Suematsu, Keith R WalleyAbstract:Background Altered fibrin clot architecture iS increaSingly aSSociated with cardiovaScular diSeaSeS; yet, little iS known about how fibrin networkS are affected by Small moleculeS that alter fibrinogen Structure. BaSed on previouS evidence that S-nitroSoglutathione (GSNO) alterS fibrinogen Secondary Structure and fibrin polymerization kineticS, we hypotheSized that GSNO would alter fibrin microStructure.
