Inhibition of creatine kinase by <i>S</i>‐nitrosoglutathione

Wolosker, Herman; Panizzutti, Rogério; Engelender, Simone

doi:10.1016/0014-5793(96)00829-0

Cited by 138 publications

(74 citation statements)

References 19 publications

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“…Cys-160 and Cys-257 in ADP͞ATP translocase are known to be primary targets for oxidative stress and undergo disulfide bond formation, resulting in formation of the permeability transition pore in mitochondria, triggering apoptosis (34). Cys-283 of cytosolic creatine kinase and the homologous Cys-317 of sarcomeric mitochondrial isoform are active site thiols at which S-nitrosylation was shown to be inactivating (35). In the case of DJ-1, the identified SNO peptide contained two Cys residues; one of them, Cys-106, was reported to be a primary target for oxidation, leading to mitochondrial relocation and neuroprotectant activity of DJ-1 (36,37).…”

Section: Identification Of Sno-cys By Nlc-ms͞ms and Database Searchingmentioning

confidence: 99%

SNOSID, a proteomic method for identification of cysteine S-nitrosylation sites in complex protein mixtures

Hao

Derakhshan

Shi

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

316

320

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Reversible addition of NO to Cys-sulfur in proteins, a modification termed S-nitrosylation, has emerged as a ubiquitous signaling mechanism for regulating diverse cellular processes. A key first-step toward elucidating the mechanism by which S-nitrosylation modulates a protein's function is specification of the targeted Cys (SNO-Cys) residue. To date, S-nitrosylation site specification has been laboriously tackled on a protein-by-protein basis. Here we describe a high-throughput proteomic approach that enables simultaneous identification of SNO-Cys sites and their cognate proteins in complex biological mixtures. The approach, termed SNOSID (SNO Site Identification), is a modification of the biotin-swap technique [Jaffrey, S. R., Erdjument-Bromage, H., Ferris, C. D., Tempst, P. & Snyder, S. H. (2001) Nat. Cell. Biol. 3, 193–197], comprising biotinylation of protein SNO-Cys residues, trypsinolysis, affinity purification of biotinylated-peptides, and amino acid sequencing by liquid chromatography tandem MS. With this approach, 68 SNO-Cys sites were specified on 56 distinct proteins in S -nitrosoglutathione-treated (2–10 μM) rat cerebellum lysates. In addition to enumerating these S-nitrosylation sites, the method revealed endogenous SNO-Cys modification sites on cerebellum proteins, including α-tubulin, β-tubulin, GAPDH, and dihydropyrimidinase-related protein-2. Whereas these endogenous SNO proteins were previously recognized, we extend prior knowledge by specifying the SNO-Cys modification sites. Considering all 68 SNO-Cys sites identified, a machine learning approach failed to reveal a linear Cys-flanking motif that predicts stable transnitrosation by S -nitrosoglutathione under test conditions, suggesting that undefined 3D structural features determine S-nitrosylation specificity. SNOSID provides the first effective tool for unbiased elucidation of the SNO proteome, identifying Cys residues that undergo reversible S-nitrosylation.

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Section: Identification Of Sno-cys By Nlc-ms͞ms and Database Searchingmentioning

confidence: 99%

SNOSID, a proteomic method for identification of cysteine S-nitrosylation sites in complex protein mixtures

Hao

Derakhshan

Shi

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

316

320

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“…It has been shown that NO is capable of nitrosating critical thiol residues on creatinine phosphokinase which is irreversible and de-energizes mitochondria thus disrupting its ATP supply [119][120][121]. Nanomolar concentrations of NO are capable of reversible binding to heme as of cytochrome c oxidase [122].…”

Section: Effect Of No On Mitochondriamentioning

confidence: 99%

Biochemistry of Nitric Oxide

2011

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Nitric oxide (NO) a free radical having both cytoprotective as well as tumor promoting agent is formed from L-arginine by converting it to L-citrulline via nitric oxide synthase enzymes. The reaction product of nitric oxide with superoxide generates potent oxidizing agent, peroxynitrite which is the main mediator of tissue and cellular injury. Peroxynitrite is reactive towards many biomolecules which includes amino acids, nucleic acid bases; metal containing compounds, etc. NO metabolites may play a key role in mediating many of the genotoxic/ carcinogenic effects as DNA damage, protein or lipid modification, etc. The basic reactions of nitric oxide can be divided as direct effect of the radical where it alone plays a role in either damaging or protecting the cell milieu and an indirect effect in which the byproducts of nitric oxide formed by convergence of two independent radical generating pathways play the role in biological reactions which mainly involve oxidative and nitrosative stress. Nitric oxide is also capable of directly interacting with mitochondria through inhibition of respiration or by permeability transition. Reaction of nitric oxide with metal ions include its direct interaction with the metals or with oxo complexes thereby reducing them to lower valent state. Excessive production of nitric oxide can be studied by inhibiting the synthetic pathway of nitric oxide using both selective or specific nitric oxide synthase inhibitor or nonselective nitric oxide synthase inhibitor with respect to isoforms of nitric oxide.Keywords Nitric oxide Á Nitric oxide synthase Á Nitric oxide inhibitors Á Generation of nitric oxide Á Cancer Á Systemic lupus erythematosus Á Direct and indirect effect of nitric oxide Á Effect of nitric oxide on mitochondria

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“…One of the more rapid effects is an inactivation of complex I, possibly due to S-nitrosylation of the complex (15,24), followed by inhibition of aconitase and complex II, possibly due to removal of iron from iron-sulphur centers (25)(26)(27). Peroxynitrite can inhibit complex I, complex II, cytochrome oxidase, the ATP synthase, aconitase, Mn-SOD, creatine kinase, and probably many other proteins (2,10,28). Peroxynitrite is a strong oxidant and can also cause DNA damage, induce lipid peroxidation, and increase mitochondrial proton (and other ion) permeability (probably by lipid peroxidation or thiol cross-linking) (29).…”

Section: No Actions On Mitochondriamentioning

confidence: 99%