Peroxynitrite-mediated tyrosine nitration catalyzed by superoxide dismutase

Ischiropoulos, Harry; Zhu, Ling; Chen, Jun; Tsai, Michael Y.; Martin, J. C.; Smith, Craig D.; Beckman, Joseph S.

doi:10.1016/0003-9861(92)90431-u

Cited by 1,437 publications

(794 citation statements)

References 33 publications

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“…The inability of either compound to induce strong hepatic protein nitration in the SOD1-/-mice as in the WT indicates a general need for SOD1 to catalyze the process in vivo. Because the catalytic role of SOD1 in protein nitration has been shown in vitro [9,10,40,50], our results provide direct evidence for such a role of SOD1 in vivo.The diminished hepatic protein nitration in the SOD1-/-mice was unlikely due to a limited NO formation or secondary changes associated with SOD1 knockout. Both treatments of APAP and LPS resulted in similar differences in hepatic protein nitration between the SOD1-/-and WT mice, despite a large variation (0 to 79%) of genotype differences in plasma NO concentrations.…”

supporting

confidence: 63%

See 1 more Smart Citation

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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supporting

confidence: 63%

“…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]. …”

mentioning

confidence: 99%

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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“…By blocking ribonucleotide reductase, NO impairs DNA synthesis and cell division. Peroxynitrite (Figure l), but not NO, nitrosylates tyrosine residues on iron, manganese, and copperzinc superoxide dismutases, as well as other coppercontaining proteins (51). The reaction appears to be catalyzed by transition metals at the active sites of these enzymes.…”

Section: Biochemical Properties Of Nitric Oxidementioning

confidence: 96%

Nitric oxide and arthritis

Stefanović-Račić

Stadler

Evans

1993

Arthritis & Rheumatism

273

136

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“…However, 200/.tM peroxynitrite (panel IV) form significant yields of nitrotyrosine which can be slightly enhanced by the addition of SOD (panel V). It has been shown that SOD can catalyze the nitration of tyrosine [11]. However, the small effect of SOD on the nitration of SERCA2a may be rationalized by the large size of the membrane protein potentially hampering interaction of a peroxynitrite-SOD complex with tyrosine residues of SERCA2a.…”

Section: The Reaction Of Skeletal Muscle Sr Vesicles Withmentioning

confidence: 99%

“…to ortho-nitrotyrosine [11,12]. The latter has been discussed as a biological marker for the assessment of the exposure of tissue to oxidative stress, and, in particular, nitric oxide-derived reactive oxygen species.…”

Section: Introductionmentioning

confidence: 99%

Accumulation of nitrotyrosine on the SERCA2a isoform of SR Ca‐ATPase of rat skeletal muscle during aging: a peroxynitrite‐mediated process?

Viner¹,

Ferrington²,

Hühmer³

et al. 1996

FEBS Letters

132

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The SR Ca-ATPase in skeletal muscle SR vesicles isolated from young adult (5 months) and aged (28 months) rats was analyzed for nitrotyrosine. Only the SERCA2a isoform contained significant amounts with approximately one and four nitrotyrosine residues per young and old Ca-ATPase, respectively. The in vitro exposure of SR vesicles of young rats to peroxynitrite yielded selective nitration of the SERCA2a Ca-ATPase even in the presence of excess SERCAla. No nitration was observed during the exposure of SR vesicles to nitric oxide in the presence of 02. These data suggest the in vivo presence of peroxynitrite in skeletal muscle. The greater nitrotyrosine content of SERCA2a from aged tissue implies an age-associated increase in susceptibility to oxidation by this species.

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Peroxynitrite-mediated tyrosine nitration catalyzed by superoxide dismutase

Cited by 1,437 publications

References 33 publications

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

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

Nitric oxide and arthritis

Accumulation of nitrotyrosine on the SERCA2a isoform of SR Ca‐ATPase of rat skeletal muscle during aging: a peroxynitrite‐mediated process?

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