Quantitative evaluation of tryptophan oxidation in actin and troponin I from skeletal muscles using a rat model of acute oxidative stress

Fedorova, Maria; Todorovsky, Toni; Kuleva, N. V.; Hoffmann, Ralf

doi:10.1002/pmic.201000147

Cited by 34 publications

(25 citation statements)

References 34 publications

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“…Generation of NFK and NFK in Other Proteins-NFK has been identified in other proteins by mass spectrometry, including bovine heart mitochondrial proteins (72), rat skeletal muscle proteins (73), bovine ␣-crystalline (74), and spinach LHCII (32). NFK is formed by the reaction of ROS with tryptophan side chains in proteins (67 (22).…”

Section: Discussionmentioning

confidence: 99%

N-Formylkynurenine as a Marker of High Light Stress in Photosynthesis

Dreaden

Chen²,

Rexroth³

et al. 2011

Journal of Biological Chemistry

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Photosystem II (PSII) is the membrane protein complex that catalyzes the photo-induced oxidation of water at a manganesecalcium active site. Light-dependent damage and repair occur in PSII under conditions of high light stress. The core reaction center complex is composed of the D1, D2, CP43, and CP47 intrinsic polypeptides. In this study, a new chromophore formed from the oxidative post-translational modification of tryptophan is identified in the CP43 subunit. Tandem mass spectrometry peptide sequencing is consistent with the oxidation of the CP43 tryptophan side chain, Trp-365, to produce N-formylkynurenine (NFK). Characterization with ultraviolet visible absorption and ultraviolet resonance Raman spectroscopy supports this assignment. An optical assay suggests that the yield of NFK increases 2-fold (2.2 ؎ 0.5) under high light illumination. A concomitant 2.4 ؎ 0.5-fold decrease is observed in the steady-state rate of oxygen evolution under the high light conditions. NFK is the product formed from reaction of tryptophan with singlet oxygen, which can be produced under high light stress in PSII. Reactive oxygen species reactions lead to oxidative damage of the reaction center, D1 protein turnover, and inhibition of electron transfer. Our results are consistent with a role for the CP43 NFK modification in photoinhibition.Oxygenic photosynthesis is the enzyme-catalyzed conversion of light energy to biochemical energy, and this process occurs in the membranes of plants, algae, and cyanobacteria. In oxygenic photosynthesis, photosystem II (PSII) 4 catalyzes the light-driven oxidation of water and reduction of plastoquinone. On the acceptor side of PSII, electrons are transferred sequentially to two quinone molecules, Q A and Q B (1). On the donor side, a Mn 4 Ca active site is the binding site for water and the site of oxygen production. Each monomer is composed of 20 protein subunits, chlorophylls, carotenoids, and redox-active plastoquinones (2, 3). Calcium and chloride are required for activity under physiological conditions (4). The chloride binding site has been assigned near the active site (2, 3).The D1, D2, CP43, and CP47 polypeptides form the intrinsic core complex of PSII. The D1 and D2 membrane spanning proteins bind the electron transfer cofactors active in water oxidation (2, 3). This central heterodimeric core is symmetrically flanked by the CP43 and CP47 proteins, which bind light-harvesting antennae chlorophyll (Chl) molecules (5). Each of these core polypeptides is composed of intrinsic membrane-spanning helices, as well as several hydrophilic loops that protrude into the interior lumen of the thylakoid membrane (2, 3). The lumenal loop regions of CP43 have been implicated as important in assembly and protection from photoinhibition (see Ref. and references therein).The active site of water oxidation, the Mn 4 Ca cluster, is located on the lumenal surface and is protected by three extrinsic polypeptides (6). In plants, these extrinsic proteins, the 18-kDa, 24-kDa, and psbO (or the 33-kDa, manganes...

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Section: Discussionmentioning

confidence: 99%

N-Formylkynurenine as a Marker of High Light Stress in Photosynthesis

Dreaden

Chen²,

Rexroth³

et al. 2011

Journal of Biological Chemistry

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“…3B). In addition, histidyl (40,87,173), as well as tryptophyl residues (79,86,340,356) can be irreversibly oxidised [62,59,63].…”

Section: Redox Modifications and Regulation Of Actinmentioning

confidence: 98%

Redox regulation of cytoskeletal dynamics during differentiation and de-differentiation

Gellert

Hanschmann

Lepka

et al. 2015

Biochimica et Biophysica Acta (BBA) - General Subjects

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“…2) or those that modify amino-acid side chains (27,60,78,90,263,264). The former group includes the direct attack by a hydroxyl radical on glutamate residues, which converts the amino acid into pyruvic acid and ammonia or a reaction of the hydroxyl radical with a proline residue, forming aminobutyric acid and carbon dioxide (CO 2 ).…”

Section: Fig 1 Interaction Of Proteome With Reactive Nitrogen Oxygementioning

confidence: 99%

“…LC-MS has identified oxidation products of Trp in the serum in association with atherosclerosis and in cardiac and skeletal muscle tissue (78,108). Several of these modified proteins include actin, troponin, H-FABP, and complex V. However, due to the multiple isomeric oxidative degradation products (e.g., serotonin or 5-hydroxytryptamine and oxyindolylalanine) that occur, it has been difficult to distinguish these in a complex protein mixture.…”

Section: Tryptophanmentioning

confidence: 99%

Cardiovascular Redox and Ox Stress Proteomics

Kumar

Calamaras

Haeussler

et al. 2012

Antioxidants & Redox Signaling

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Significance: Oxidative post-translational modifications (OPTMs) have been demonstrated as contributing to cardiovascular physiology and pathophysiology. These modifications have been identified using antibodies as well as advanced proteomic methods, and the functional importance of each is beginning to be understood using transgenic and gene deletion animal models. Given that OPTMs are involved in cardiovascular pathology, the use of these modifications as biomarkers and predictors of disease has significant therapeutic potential. Adequate understanding of the chemistry of the OPTMs is necessary to determine what may occur in vivo and which modifications would best serve as biomarkers. Recent Advances: By using mass spectrometry, advanced labeling techniques, and antibody identification, OPTMs have become accessible to a larger proportion of the scientific community. Advancements in instrumentation, database search algorithms, and processing speed have allowed MS to fully expand on the proteome of OPTMs. In addition, the role of enzymatically reversible OPTMs has been further clarified in preclinical models. Critical Issues: The identification of OPTMs suffers from limitations in analytic detection based on the methodology, instrumentation, sample complexity, and bioinformatics. Currently, each type of OPTM requires a specific strategy for identification, and generalized approaches result in an incomplete assessment. Future Directions: Novel types of highly sensitive MS instrumentation that allow for improved separation and detection of modified proteins and peptides have been crucial in the discovery of OPTMs and biomarkers. To further advance the identification of relevant OPTMs in advanced search algorithms, standardized methods for sample processing and depository of MS data will be required. Antioxid. Redox Signal. 17, 1528-1559.

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Quantitative evaluation of tryptophan oxidation in actin and troponin I from skeletal muscles using a rat model of acute oxidative stress

Cited by 34 publications

References 34 publications

N-Formylkynurenine as a Marker of High Light Stress in Photosynthesis

N-Formylkynurenine as a Marker of High Light Stress in Photosynthesis

Redox regulation of cytoskeletal dynamics during differentiation and de-differentiation

Cardiovascular Redox and Ox Stress Proteomics

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