Hemin–H2O2–NO2− induced protein oxidation and tyrosine nitration are different from those of SIN-1: A study on glutamate dehydrogenase nitrative/oxidative modification

2009 ◽  
Vol 41 (4) ◽  
pp. 907-915 ◽  
Author(s):  
Yan Zhang ◽  
Naihao Lu ◽  
Zhonghong Gao
Keyword(s):  
Glutamate Dehydrogenase ◽  
Protein Oxidation ◽  
Oxidative Modification ◽  
Tyrosine Nitration

Exacerbated Protein Oxidation and Tyrosine Nitration through Nitrite-Enhanced Fenton Chemistry

2021 ◽  
Author(s):  
Rui Peng ◽  
Li Wang ◽  
Pinting Yu ◽  
Andrew J. Carrier ◽  
Ken D. Oakes ◽  
...  
Keyword(s):  
Protein Oxidation ◽  
Tyrosine Nitration ◽  
Fenton Chemistry

scholarly journals Features of oxidative modification of proteins and erythrocyte functional state in pregnancy complicated by placental insufficiency

2015 ◽  
Vol 64 (5) ◽  
pp. 62-68
Author(s):  
Anna Aleksandrovna Shevelkova ◽  
Eduard Karpovich Aylamazyan ◽  
Inna Ivanovna Evsyukova
Keyword(s):  
Functional State ◽  
Protein Oxidation ◽  
Placental Insufficiency ◽  
Oxidative Modification ◽  
Oxidative Modification Of Proteins ◽  
In Pregnancy

Protein oxidation intensity and reduced thiols level were studied in comparison with erythrocyte functional state in pregnancy complicated by placental insufficiency. 31 women with placental insufficiency, 41 healthy pregnant and 37 healthy nonpregnant women were included. Induced protein oxidation intensity and reduced thiols level were shown to be decreased in pregnancy complicated by placental insufficiency. Erythrocyte functional state was also worsened. It correlated with protein oxidation intensity and reduced thiols level. So protein oxidation intensity, reduced thiols level and erythrocyte functional state were shown to be indicators of placental insufficiency and can be used to identify this pathology and to evaluate the effectiveness of treatment.

scholarly journals Redox Homeostasis of Albumin in Relation to Alpha-Lipoic Acid and Dihydrolipoic Acid

2010 ◽  
Vol 3 (3) ◽  
pp. 206-213 ◽  
Author(s):  
Pinar Atukeren ◽  
Seval Aydin ◽  
Ezel Uslu ◽  
MKoray Gumustas ◽  
Ufuk Cakatay
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Lipoic Acid ◽  
Protein Oxidation ◽  
Antioxidant Properties ◽  
Oxidative Modification ◽  
Breakdown Product ◽  
Alpha Lipoic Acid ◽  
Dihydrolipoic Acid

Albumin represents the predominant circulating antioxidant agent in plasma exposed to continuous oxidative stress and a change in serum albumin structure accounts for its antioxidant properties. Alterations in the redox status of albumin may result in impairments of its biological properties. Alpha-lipoic acid (LA), a naturally occurring thiol compound found in virtually all species, is a potent antioxidant with high efficacy which is also involved in the chelation of metal ions, regeneration of antioxidants, and repair of oxidatively damaged proteins. In human body LA is rapidly reduced to dihydrolipoic acid (DHLA) after intake into the cell. Both, LA and DHLA are amphipathic molecules which act as antioxidants both in hydrophilic and lipophilic environments. The present study aimed to investigate the antioxidant/pro-oxidant effects of LA and DHLA due to their concentrations in metal-catalyzed protein oxidation (MCO) of human serum albumin (HSA). Progressive oxidative modification of albumin was found in MCO system by an increased content of protein hydroperoxides (POOH), protein carbonyl groups (PCO) which is the former's major breakdown product, and other protein oxidation markers such as advanced oxidized protein products (AOPP) and protein thiol groups (P-SH). The possible antioxidant protective effects of LA and DHLA were observed with 25 µM and 50 µM; DHLA being more influential. Protein oxidation parameters were found to be lower and P-SH levels seemed higher. However, prooxidant effects of both LA and DHLA came on the scene with increased concentrations of 75 µM and 100 µM where the latter seemed the most hazardous with contradicted results. It is clear that the loss of biological activity of human serum albumin by MCO system appears of medical relevance and if LA exerts similar effects seen in the present study, it is possible that cellular prooxidant activity can also result consuming this unique antioxidant in certain doses.

Tyrosine nitration limits stretch-induced CD40 expression and disconnects CD40 signaling in human endothelial cells

Blood ◽  
2011 ◽  
Vol 118 (13) ◽  
pp. 3734-3742 ◽  
Author(s):  
Andreas H. Wagner ◽  
Anke Hildebrandt ◽  
Sebastian Baumgarten ◽  
Andreas Jungmann ◽  
Oliver J. Müller ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Costimulatory Molecule ◽  
Oxidative Modification ◽  
Cyclic Stretch ◽  
Mass Spectrometry Analysis ◽  
Cell Phenotype ◽  
Mononuclear Leukocytes ◽  
Tyrosine Nitration ◽  
Cd40 Expression ◽  
Static Conditions

Abstract Hemodynamic forces are important effectors of endothelial cell phenotype and function. Because CD40-CD154 interactions between endothelial cells and mononuclear leukocytes or activated platelets play an important role in vascular dysfunction, we investigated the effects of cyclic stretch on CD40 expression in human cultured endothelial cells. Short-term stretch transiently up-regulated CD40 expression while long-term stretch resulted in a distinct decline in CD40 protein which was prevented by inhibition of the 20S proteasome or scavenging of peroxynitrite. Tyrosine nitration of CD40 also occurred under static conditions on addition of authentic peroxynitrite, and according to mass spectrometry analysis Tyr-82 but not Tyr-31 was its target in the native protein. Immunofluorescence analysis of endothelial cells transduced with a control or Tyr-82 to Ala mutated AAV9-CD40-eGFP expression construct confirmed a peroxynitrite-dependent redistribution of the protein from the cell membrane to the cytoplasm, which was prevented by methyl-β-cyclodextrin. Moreover, CD154-stimulated IL-12p40 and E-selectin expression markedly decreased after exposure to authentic peroxynitrite or cyclic stretch, respectively. Coimmunoprecipitation demonstrated a decreased binding of TRAF2 and TRAF6 to the CD40 protein after tyrosine nitration. Through this posttranslational oxidative modification of an important costimulatory molecule, endothelial cells are able to quickly adapt to unfavorable hemodynamics and maintain their anti-inflammatory phenotype.

scholarly journals Protein Tyrosine Nitration of the Flavin Subunit Is Associated with Oxidative Modification of Mitochondrial Complex II in the Post-ischemic Myocardium

2008 ◽  
Vol 283 (41) ◽  
pp. 27991-28003 ◽  
Author(s):  
Chwen-Lih Chen ◽  
Jingfeng Chen ◽  
Sharad Rawale ◽  
Saradhadevi Varadharaj ◽  
Pravin P. T. Kaumaya ◽  
...  
Keyword(s):  
Oxidative Modification ◽  
Ischemic Myocardium ◽  
Tyrosine Nitration ◽  
Mitochondrial Complex ◽  
Complex Ii ◽  
Protein Tyrosine ◽  
Protein Tyrosine Nitration

Myofibrillar protein oxidation and contractile dysfunction in hyperthyroid rat diaphragm

2007 ◽  
Vol 102 (5) ◽  
pp. 1850-1855 ◽  
Author(s):  
Takashi Yamada ◽  
Takaaki Mishima ◽  
Makoto Sakamoto ◽  
Minako Sugiyama ◽  
Satoshi Matsunaga ◽  
...  
Keyword(s):  
Protein Oxidation ◽  
Force Production ◽  
Oxidative Modification ◽  
Fiber Bundles ◽  
Daily Injection ◽  
Myofibrillar Proteins ◽  
Carbonyl Groups ◽  
Carbonyl Content ◽  
Tetanic Force ◽  
Isometric Forces

The purpose of the present study was to test the hypothesis that administration of thyroid hormone [3,5,3′-triiodo-l-thyronine (T3)] could result in oxidation of myofibrillar proteins and, in turn, induce alterations in respiratory muscle function. Daily injection of T3 for 21 days depressed isometric forces of diaphragm fiber bundles across a range of stimulus frequencies (1, 10, 20, 40, 75, and 100 Hz) ( P < 0.05). These reductions in force production were accompanied by a remarkable increment (104%; P < 0.05) in carbonyl groups of myofibrillar proteins. In contrast, T3 treatment has no effects on the carbonyl content in myosin heavy chain. In additional experiments, we have also tested the efficacy of carvedilol, a nonselective β1- β2-blocker that possesses antioxidative properties. Treatment with carvedilol dramatically improved isometric tetanic force production at stimulus frequencies from 40 to 100 Hz ( P < 0.05). Carvedilol also prevented T3-induced contractile protein oxidation ( P < 0.05). These data suggest that the oxidative modification of myofibrillar proteins may account, at least in part, for an impairment of diaphragm in hyperthyroidism.

Abstract P096: Vascular Protein Oxidation and Redox Proteomics in Human Hypertension

Hypertension ◽  
2015 ◽  
Vol 66 (suppl_1) ◽  
Author(s):  
Sofia Tsiropoulou ◽  
Augusto C Montezano ◽  
Alan Scott ◽  
Richard J Burchmore ◽  
Rhian M Touyz
Keyword(s):  
Vascular Injury ◽  
Protein Oxidation ◽  
Protein Tyrosine Phosphatases ◽  
Redox Status ◽  
Oxidative Modification ◽  
Fk506 Binding Protein ◽  
Proteomic Data ◽  
Irreversible Oxidation ◽  
Health And Disease ◽  
Polymerase I

Oxidative stress has been implicated in the pathophysiology of hypertension (HTN) through redox-sensitive processes that cause vascular damage. Despite recent advances in the field of vascular redox signalling in HTN, it still remains unclear exactly how ROS cause vascular injury. We hypothesise that regulation of redox-sensitive protein tyrosine phosphatases (PTP) through post-translational oxidative modification, is impaired in HTN where ROS levels are increased. Vascular smooth muscle cells (VSMC) from small arteries of normotensive (NT) and hypertensive (HT) individuals were stimulated with AngII (10-7 M) and ET-1 (10-7 M). Irreversible oxidation of proteins and PTPs was assessed by oxyblot and immunoblotting, respectively. Differential gel electrophoresis (DiGE) and CyDye thiol labelling were employed for screening of reversibly oxidised proteome. Irreversible protein oxidation was not affected by AngII or ET-1 in VSMCs from NT and HT subjects. PTP hyperoxidation tended to increase in VSMCs from NT upon stimulation with AngII (FC=2.12 at 60min) and ET-1 (FC=1.60 at 60min), whereas a similar trend was observed only after AngII treatment (FC=1.38 at 60min) in HTN (p>0.05). Proteomic data, filtered for FC>2, detected 2051 spots with 1899 (92.5%) being equally oxidised between NT and HT. In addition, oxidation of 57 (2.9%) spots was increased, while 95 (4.6%) were decreased in HT. Candidate proteins exhibiting consistent changes across three experimental replicates included β-actin (FC=-2.86), annexin A1 (-2.23), galectin-1 (-1.67), FK506 binding protein (-2.35) and polymerase I and transcript release factor (PTRF, -1.92). Stimulation with AngII altered the redox status in 2-3% of proteins, both in HT and NT. However, vimentin was the only target changing consistently across the replicates (FC=2.48). Our findings indicate that pro-hypertensive agents may not impact significantly on irreversible protein and PTP oxidation in health and disease, but may have effects on reversible oxidation. Our proteomic data, in agreement with our previous rat studies, support decreased reversible thiol oxidation in HTN. Moreover, these novel findings identify differentially oxidised proteins which may contribute to oxidative vascular injury in HTN.

scholarly journals Carbonic anhydrase III and four-and-a-half LIM protein 1 are preferentially oxidized with muscle unloading

2008 ◽  
Vol 105 (5) ◽  
pp. 1554-1561 ◽  
Author(s):  
Chiao-nan Chen ◽  
Deborah A. Ferrington ◽  
LaDora V. Thompson
Keyword(s):  
Carbonic Anhydrase ◽  
Protein Oxidation ◽  
Oxidative Modification ◽  
Lim Protein ◽  
Oxidized Proteins ◽  
Carbonic Anhydrase Iii ◽  
Muscle Disuse ◽  
Old Rats ◽  
Modified Proteins ◽  
Muscle Unloading

The identities of proteins that show disuse-related changes in the content of oxidative modification are unknown. Furthermore, it is unknown whether the global accumulation of oxidized proteins is greater in aged animals with muscle disuse. The purposes of this study are 1) to identify the exact proteins that show disuse-related changes in oxidation levels and 2) to test the hypothesis that the global accumulation of oxidized proteins with muscle disuse would be greater in aged animals. Adult and old rats were randomized into four groups: weight bearing and 3, 7, or 14 days of hindlimb unloading. Soleus muscles were harvested to investigate the protein oxidation with unloading. Slot blot, SDS-PAGE, and Western blot analyses were used to detect the accumulation of 4-hydroxy-2-nonenol (HNE)- and nitrotyrosine (NT)-modified proteins. Matrix-assisted laser desorption ionization-time of flight and tandem mass spectroscopy were used to identify modified proteins. We found that global HNE- and NT-modified proteins accumulated significantly with aging but not with muscle unloading. Two HNE and NT target proteins, four-and-a-half LIM protein 1 (FHL1) and carbonic anhydrase III (CAIII), showed changes in the oxidation levels with muscle unloading. The changes in the oxidation levels happened to adult rats but not old rats. However, old rats had higher baseline levels of HNE-modified FHL1. In summary, the data suggest that the muscle unloading-related changes of protein oxidation are more significant in specific proteins and that the changes are age related.

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