Proteolytic Degradation of Tyrosine Nitrated Proteins

Souza, José Maria de; Choi, Irene; Chen, Qiping; Weisse, Marie; Daikhin, Evgueni; Yudkoff, Marc; Obin, Martin S.; Ara, Jahan; Horwitz, Joel; Ischiropoulos, Harry

doi:10.1006/abbi.2000.1940

Cited by 239 publications

(188 citation statements)

References 29 publications

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“…The new putative enzyme was termed "nitrotyrosine denitrase". In contrast nitrated proteins can be also rapidly degraded by the proteasome pathway (Souza et al, 2000), which seems not to be the case for PGIS.…”

Section: Discussionmentioning

confidence: 92%

Superoxide as a Messenger of Endothelial Function

Ullrich

Bachschmid²

2000

Biochemical and Biophysical Research Communications

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Section: Discussionmentioning

confidence: 92%

Superoxide as a Messenger of Endothelial Function

Ullrich

Bachschmid²

2000

Biochemical and Biophysical Research Communications

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Section: Discussionmentioning

confidence: 94%

“…Only the holo-SOD1 enzyme, but not the Cu,Zn-depleted apo-SOD1 protein, was able to enhance the peroxynitritemediated nitrotyrosine formation in BSA and liver homogenates. These types of rescues strongly suggest that the lack of SOD1 activity per se, instead of compensatory changes or an accelerated nitrotyrosine degradation [52,53] caused by the SOD1 knockout, was responsible for the greatly attenuated hepatic protein nitration in the APAP or LPS-treated SOD1-/-mice.The catalytic or promoting role of SOD1 in in vivo hepatic protein nitration demonstrated in the present study is in contrast to observations from several previous experiments. Overexpression of SOD1 in mice prevented nitration of tyrosine hydroxylase [54] and APAP toxicity [31].…”

mentioning

confidence: 94%

Role of copper,zinc-superoxide dismutase in catalyzing nitrotyrosine formation in murine liver

Zhu

Zhang

Roneker

et al. 2008

Free Radical Biology and Medicine

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The solely known function of Cu,Zn-superoxide dismutase (SOD1) is to catalyze the dismutation of superoxide anion into hydrogen peroxide. Our objective was to determine if SOD1 catalyzed murine liver protein nitration induced by acetaminophen (APAP) and lipopolysaccharide (LPS). Liver and plasma samples were collected from young adult SOD1 knockout mice (SOD1-/-) and wild-type (WT) mice at 5 or 6 h after an ip injection of saline, APAP, or LPS. Hepatic nitrotyrosine formation was induced by APAP and LPS only in the WT mice. The diminished hepatic protein nitration in the SOD1-/-mice was not directly related to plasma nitrite and nitrate concentrations. Similar genotype differences were seen in liver homogenates treated with a bolus of peroxynitrite. Adding only the holo, but not the apo-SOD1 enzyme into the liver homogenates enhanced the reaction in an activity-dependent fashion and nearly eliminated the genotype difference at the high doses. Mass Spectrometry showed 4 more nitrotyrosine residues in bovine serum albumin and 10 more nitrated protein candidates in the SOD1-/-liver homogenates by peroxynitrite with added SOD1. In conclusion, the diminished hepatic protein nitration mediated by APAP or LPS in the SOD1-/-mice was due to the lack of SOD1 activity per se. Keywords SOD1; Protein nitration; Acetaminophen; Peroxynitrite; Lipopolysaccharide; Mouse Although copper,zinc-superoxide dismutase (SOD1) has been widely considered a major intracellular antioxidant enzyme in mammals, its solely known function is to catalyze the conversion of superoxide anion into less active hydrogen peroxide. Indeed, SOD1 is protective against oxidative stress associated with acute paraquat toxicity, myocardial ischemia/reperfusion injury, and N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced dopaminergic neurodegeneration [1][2][3]. Mice deficient in SOD1 develop Address correspondence to: Xin Gen Lei, Department of Animal Science, Cornell University, Ithaca, NY 14853, Tel. 607-254-4703; Fax. 607-255-9829; E-Mail: XL20@cornell.edu. Publisher's Disclaimer: This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final citable form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. [7,8]. These paradoxical findings strongly suggest that SOD1 may exert functions more than just superoxide dismutation. In fact, SOD1 was shown to promote peroxynitrite-mediated nitrotyrosine formation in vitro [9,10]. NIH Public AccessPeroxynitrite is formed by a rapid diffusion-limited, radical-radical coupling reaction between nitric oxide (NO) and superoxide anion [11,12] [24,25,33,34] provide us with an unprecedented opportunity to study the in vivo role of SOD1 in nitrotyrosine formation. Furtherm...

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“…Second, proinflammatory excesses of superoxide anion and nitric oxide might satisfy the temporal and spatial requirements needed to generate post-translational chemical protein modifications such as tyrosine nitration, detectable as 3'-nitrotyrosine (NT). [13][14][15][16] Such nitrations have been further linked to polyubiquitination and overt proteosomal protein degradation. Therefore the present study was undertaken to determine whether a relationship exists between the mitochondrial content of specific muscle fiber types and the capacity for a given fiber to generate nitrated proteins and be more subject to atrophy.…”

Section: Introductionmentioning

confidence: 99%

“…Therefore the present study was undertaken to determine whether a relationship exists between the mitochondrial content of specific muscle fiber types and the capacity for a given fiber to generate nitrated proteins and be more subject to atrophy. 16,17 …”

Section: Introductionmentioning

confidence: 99%

Protein tyrosine nitration in chronic intramuscular parasitism: immunohistochemical evaluation of relationships between nitration, and fiber type-specific responses to infection

et al. 2011

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The present study was conducted to determine whether preferential muscle catabolism [psoas major (PM) > rectus femoris (RF)] observed during the chronic intramuscular stage of Sarcocystis cruzi infection could be associated with the pathological consequences of increased protein tyrosine nitration in fibers characteristically more metabolically active due to higher mitochondrial density. Holstein calves were assigned to control (C), or S. cruzi-infected (I) groups, n=5/group. Calves were euthanized on day 63 of infection. Samples of RF and PM were prepared for metabolic fiber typing (MFT: slow oxidative, SOType I; fast oxidative glycolytic, FOG -Type IIa; fast glycolytic, FG -Type IIb), fiber area, and immunohistochemical localization of fast myosin heavy chain 2a and 2b, nitrotyrosine (NT), and mitochondrial Complex V ATP-synthase. MFT analysis documented that PM contained twice the number of SO fibers compared to RF (32 v 16%, P<0.002). SO and FOG fibers (Both higher in mitochondrial density than FG fibers) in both PM and RF were significantly smaller in area in I calves with mean FG areas not different between C and I. Muscle NT content (Western blot of myofibrillar protein fraction) increased with infection; NT was immunohistochemically localized into three distinct patterns in fibers: i) sparse fiber staining, ii) dense punctuate intrafiber staining, and iii) pericystic staining. By image analysis, the greatest punctuate intrafiber pixel density of NT was associated with SO fibers from I calves with the NT colocalizing with mitochondrial Complex V -F1F0 ATP synthase. More fibers were positive for the colocalization in PM than RF (P<0.04). The data are consistent with the concept that fibers rich in mitochondria possessing more inherent oxidative energy capacity generate more nitrated proteins than glycolytic fibers and as such are more affected by the proinflammatory response to infections like Sarcocystosis.

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Proteolytic Degradation of Tyrosine Nitrated Proteins

Cited by 239 publications

References 29 publications

Superoxide as a Messenger of Endothelial Function

Superoxide as a Messenger of Endothelial Function

Role of copper,zinc-superoxide dismutase in catalyzing nitrotyrosine formation in murine liver

Protein tyrosine nitration in chronic intramuscular parasitism: immunohistochemical evaluation of relationships between nitration, and fiber type-specific responses to infection

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