CoChat
Sign Up
Cited by 295Redox biology and oxidative stressAntioxidant Activity and Oxidative StressAdvanced Glycation End Products research

Determination of protein carbonyls in plasma, cell extracts, tissue homogenates, isolated proteins: Focus on sample preparation and derivatization conditions

Open access
Weber, Daniela, Davies, Michael J., Grune, Tilman·2015·Redox Biology
DOI 10.1016/j.redox.2015.06.005PMC PMC4506980
Open this paper in CoChat — free accountOpen PDF

Abstract

Protein oxidation is involved in regulatory physiological events as well as in damage to tissues and is thought to play a key role in the pathophysiology of diseases and in the aging process. Protein-bound carbonyls represent a marker of global protein oxidation, as they are generated by multiple different reactive oxygen species in blood, tissues and cells. Sample preparation and stabilization are key steps in the accurate quantification of oxidation-related products and examination of physiological/pathological processes. This review therefore focuses on the sample preparation processes used in the most relevant methods to detect protein carbonyls after derivatization with 2,4-dinitrophenylhydrazine with an emphasis on measurement in plasma, cells, organ homogenates, isolated proteins and organelles. Sample preparation, derivatization conditions and protein handling are presented for the spectrophotometric and HPLC method as well as for immunoblotting and ELISA. An extensive overview covering these methods in previously published articles is given for researchers who plan to measure protein carbonyls in different samples.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1016/j.redox.2015.06.005

Cites

1 of 1 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • Protein carbonyls, 3-nitrotyrosine and methionine sulfoxide are biomarkers of protein oxidation commonly analyzed via immunochemical methods.

    “Protein carbonyls, 3-NT and methionine sulfoxide are biomarkers of protein oxidation which are commonly analyzed via immunochemical methods [75,82,92].”

    From Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases (2021) · cites this paper as [82]

    The Introduction identifies protein carbonyls as a marker of protein oxidation and describes their detection by immunoblotting and ELISA; the Conclusion also discusses both methods. The paper mentions methionine sulfoxides as oxidation products but does not describe their immunochemical analysis, and the passages found do not address 3-nitrotyrosine. Thus it supports the sentence for protein carbonyls, not for all three biomarkers. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

Flagged first, then by citations

Research works printed but not linked: 86

  1. [1]Breusing N. Grune T. Biomarkers of protein oxidation from a chemical, biological and medical point of view Exp. Gerontol. 45 10 2010 733 737 20403419 20403419
  2. [2]Naskalski J.W. Bartosz G. Oxidative modifications of protein structures Adv. Clin. Chem. 35 2000 161 253 11040960 11040960
  3. [3]Stadtman E.R. Protein oxidation and aging Respirology 40 12 2006 1250 1258 17090414
  4. [4]Hoehn A. Jung T. Grune T. Pathophysiological importance of aggregated damaged proteins Biol. Med. 71 2014 70 89 24632383
  5. [5]Davies M.J. The oxidative environment and protein damage Biochim. Biophys. Acta 1703 2 2005 93 109 15680218
  6. [6]Hawkins C.L. Davies M.J. Generation and propagation of radical reactions on proteins Biochim. Biophys. Acta 1504 2–3 2001 196 219 11245785 11245785
  7. [7]Morin B. Bubb W.A. Davies M.J. Dean R.T. Fu S. 3-Hydroxylysine, a potential marker for studying radical-induced protein oxidation Chem. Res. Toxicol. 11 11 1998 1265 1273 9815186 9815186
  8. [8]Fu S.L. Dean R.T. Structural characterization of the products of hydroxyl-radical damage to leucine and their detection on proteins Biochem. J. 324 1 1997 41 48 9164839 9164839 PMC1218399
  9. [9]Fu S. Hick L.A. Sheil M.M. Dean R.T. Structural identification of valine hydroperoxides and hydroxides on radical-damaged amino acid, peptide, and protein molecules Free Radic. Biol. Med. 19 3 1995 281 292 7557542 7557542
  10. [10]Pietzsch J. Measurement of 5-hydroxy-2-aminovaleric acid as a specific marker of iron-mediated oxidation of proline and arginine side-chain residues of low-density lipoprotein apolipoprotein B-100 Biochem. Biophys. Res. Commun. 270 3 2000 852 857 10772915 10772915
  11. [11]Grune T. Reinheckel T. Davies K.J. Degradation of oxidized proteins in K562 human hematopoietic cells by proteasome J. Biol. Chem. 271 26 1996 15504 15509 8663134 8663134
  12. [12]Grune T. Reinheckel T. Joshi M. Davies K.J. Proteolysis in cultured liver epithelial cells during oxidative stress. role of the multicatalytic proteinase complex, proteasome J. Biol. Chem. 270 5 1995 2344 2351 7836468 7836468
  13. [13]Davies M.J. Fu S. Wang H. Dean R.T. Stable markers of oxidant damage to proteins and their application in the study of human disease Biol. Med. 27 11–12 1999 1151 1163 10641706
  14. [14]Kim G. Weiss S.J. Levine R.L. Methionine oxidation and reduction in proteins Biochim. Biophys. Acta 1840 2 2014 901 905 23648414 PMC3766491
  15. [15]Hanschmann E.M. Godoy J.R. Berndt C. Hudemann C. Lillig C.H. Thioredoxins, glutaredoxins, and peroxiredoxins – molecular mechanisms and health significance: from cofactors to antioxidants to redox signaling Antioxid. Redox Signal. 19 13 2013 1539 1605 23397885 23397885 PMC3797455
  16. [16]Headlam H.A. Davies M.J. Markers of protein oxidation: different oxidants give rise to variable yields of bound and released carbonyl products Free Radic. Biol. Med. 36 9 2004 1175 1184 15082071 15082071
  17. [17]Levine R.L. Garland D. Oliver C.N. Amici A. Climent I. Lenz A.G. Ahn B.W. Shaltiel S. Stadtman E.R. Determination of carbonyl content in oxidatively modified proteins Methods Enzymol. 186 1990 464 478 1978225 1978225
  18. [18]Levine R.L. Williams J.A. Stadtman E.R. Shacter E. Carbonyl assays for determination of oxidatively modified proteins Methods Enzymol. 233 1994 346 357 8015469 8015469
  19. [19]Shacter E. Williams J.A. Lim M. Levine R.L. Differential susceptibility of plasma proteins to oxidative modification: examination by western blot immunoassay Free Radic. Biol. Med. 17 5 1994 429 437 7835749 7835749
  20. [20]Buss H. Chan T.P. Sluis K.B. Domigan N.M. Winterbourn C.C. Protein carbonyl measurement by a sensitive ELISA method Free Radic. Biol. Med. 23 3 1997 361 366 9214571 9214571
  21. [21]Tammen H. Schulte I. Hess R. Menzel C. Kellmann M. Mohring T. Schulz-Knappe P. Peptidomic analysis of human blood specimens: comparison between plasma specimens and serum by differential peptide display Proteomics 5 13 2005 3414 3422 16038021 16038021
  22. [22]Keller R.J. Halmes N.C. Hinson J.A. Pumford N.R. Immunochemical detection of oxidized proteins Chem. Res. Toxicol. 6 4 1993 430 433 8374038 8374038
  23. [23]Rogowska-Wrzesinska A. Wojdyla K. Nedić O. Baron C.P. Griffiths H.R. Analysis of protein carbonylation – pitfalls and promise in commonly used methods Respirology 48 10 2014 1145 1162 25072785 25072785
  24. [24]Robinson C.E. Keshavarzian A. Pasco D.S. Frommel T.O. Winship D.H. Holmes E.W. Determination of protein carbonyl groups by immunoblotting Anal. Biochem. 266 1 1999 48 57 9887212 9887212
  25. [25]Alamdari D.H. Kostidou E. Paletas K. Sarigianni M. Konstas A.G. Karapiperidou A. Koliakos G. High sensitivity enzyme-linked immunosorbent assay (ELISA) method for measuring protein carbonyl in samples with low amounts of protein Free Radic. Biol. Med. 39 10 2005 1362 1367 16257645 16257645
  26. [26]Nakamura A. Goto S. Analysis of protein carbonyls with 2,4-dinitrophenyl hydrazine and its antibodies by immunoblot in two-dimensional gel electrophoresis J. Biochem. 119 4 1996 768 774 8743580 8743580
  27. [27]Mahapatra S.K. Chakraborty S.P. Das S. Roy S. Methanol extract of Ocimum gratissimum protects murine peritoneal macrophages from nicotine toxicity by decreasing free radical generation, lipid and protein damage and enhances antioxidant protection Oxid. Med. Cell Longev. 2 4 2009 222 230 20716908 20716908 PMC2763260
  28. [28]Chakraborty S.P. Pramanik P. Roy S. Staphylococcus aureus infection induced oxidative imbalance in neutrophils: possible protective role of nanoconjugated vancomycin ISRN Pharmacol. 2012 2012 435214 22530141 22530141 PMC3317220
  29. [29]Pesez M. 4-Dinitrophenylhydrazine, a suitable reagent for the colorimetric determination of carbonyl compounds J. Pharm. Pharmacol. 11 1959 475 476 14432131 14432131
  30. [30]Dalle-Donne I. Rossi R. Giustarini D. Milzani A. Colombo R. Protein carbonyl groups as biomarkers of oxidative stress Clin. Chim. Acta 329 1–2 2003 23 38 12589963 12589963
  31. [31]Augustyniak E. Adam A. Wojdyla K. Rogowska-Wrzesinska A. Willetts R. Korkmaz A. Atalay M. Weber D. Grune T. Borsa C. Gradinaru D. Chand Bollineni R. Fedorova M. Griffiths H.R. Validation of protein carbonyl measurement: a multi-centre study Redox Biol. 4 2015 149 157 25560243 25560243 PMC4309846
  32. [32]Ahmad A. Shameem M. Husain Q. Relation of oxidant–antioxidant imbalance with disease progression in patients with asthma Ann. Thorac. Med. 7 4 2012 226 232 23189100 23189100 PMC3506103
  33. [33]Al-Shobaili H.A. Al Robaee A.A. Alzolibani A. Khan M.I. Rasheed Z. Hydroxyl radical modification of immunoglobulin G generated cross-reactive antibodies: its potential role in systemic lupus erythematosus Clin. Med. Insights Arthritis Musculoskelet. Disord. 4 2011 11 19 21487454 21487454 PMC3072208
  34. [34]Chevion S. Moran D.S. Heled Y. Shani Y. Regev G. Abbou B. Berenshtein E. Stadtman E.R. Epstein Y. Plasma antioxidant status and cell injury after severe physical exercise Proc. Natl. Acad. Sci. U. S. A. 100 9 2003 5119 5123 12702774 12702774 PMC154308
  35. [35]Renke J. Popadiuk S. Korzon M. Bugajczyk B. Wozniak M. Protein carbonyl groups’ content as a useful clinical marker of antioxidant barrier impairment in plasma of children with juvenile chronic arthritis Free Radic. Biol. Med. 29 2 2000 101 104 10980398 10980398
  36. [36]Estrada J.C. Torres Y. Benguría A. Dopazo A. Roche E. Carrera-Quintanar L. Pérez R.A. Enríquez J.A. Torres R. Ramírez J.C. Samper E. Bernad A. Human mesenchymal stem cell-replicative senescence and oxidative stress are closely linked to aneuploidy J. Cell Death 4 2013 e691 23807220 PMC3702285 23807220
  37. [38]Khan M.A. Oubrahim H. Stadtman E.R. Inhibition of apoptosis in acute promyelocytic leukemia cells leads to increases in levels of oxidized protein and LMP2 immunoproteasome Proc. Natl. Acad. Sci. U. S. A. 101 32 2004 11560 11565 15284441 15284441 PMC511020
  38. [39]Falone S. D’Alessandro A. Mirabilio A. Petruccelli G. Cacchio M. Di I.C. Di L.S. Amicarelli F. Long term running biphasically improves methylglyoxal-related metabolism, redox homeostasis and neurotrophic support within adult mouse brain cortex PLOS One 7 2 2012 e31401 22347470 22347470 PMC3275619
  39. [40]Shan X. Chi L. Ke Y. Luo C. Qian S. Gozal D. Liu R. Manganese superoxide dismutase protects mouse cortical neurons from chronic intermittent hypoxia-mediated oxidative damage Neurobiol. Dis. 28 2 2007 206 215 17719231 17719231 PMC2100412
  40. [41]Wang G. Wang J. Ma H. Khan M.F. Increased nitration and carbonylation of proteins in MRL+/+ mice exposed to trichloroethene: potential role of protein oxidation in autoimmunity Toxicol. Appl. Pharmacol. 237 2 2009 188 195 19332086 19332086 PMC2734328
  41. [42]Abdul Hamid Z. Budin S.B. Wen Jie N. Hamid A. Husain K. Mohamed J. Nephroprotective effects of Zingiber Zerumbet Smith ethyl acetate extract against paracetamol-induced nephrotoxicity and oxidative stress in rats J. Zhejiang Univ. Sci. B 13 3 2012 176 185 22374609 22374609 PMC3296068
  42. [43]Yan L.J. Sohal R.S. Analysis of oxidative modification of proteins Curr. Protoc. Protein Sci. Chapter 14: Unit 14.4 2001 18429124
  43. [44]Paixão J. Dinis T.C. Almeida L.M. Protective role of malvidin-3-glucoside on peroxynitrite-induced damage in endothelial cells by counteracting reactive species formation and apoptotic mitochondrial pathway Oxid. Med. Cell Longev. 2012 2012 428538 22792413 22792413 PMC3388314
  44. [45]Lardinois O.M. Maltby D.A. Medzihradszky K.F. de Montellano P.R. Tomer K.B. Mason R.P. Deterding L.J. Spin scavenging analysis of myoglobin protein-centered radicals using stable nitroxide radicals: characterization of oxoammonium cation-induced modifications Chem. Res. Toxicol. 22 6 2009 1034 1049 19449826 19449826 PMC2862229
  45. [46]Silva M. Bonomo L. de F. Oliveira R. de P. Geraldo de Lima W. Silva M.E. Pedrosa M.L. Effects of the interaction of diabetes and iron supplementation on hepatic and pancreatic tissues, oxidative stress markers, and liver peroxisome proliferator-activated receptor-alpha expression J. Clin. Biochem. Nutr. 49 2 2011 102 108 21980225 21980225 PMC3171682
  46. [47]Conrad C.C. Talent J.M. Malakowsky C.A. Gracy R.W. Post-electrophoretic identification of oxidized proteins Biol. Proced. Online 2 2000 39 45 12734585 12734585 PMC140127
  47. [48]Barth B.M. Gustafson S.J. Kuhn T.B. Neutral sphingomyelinase activation precedes NADPH oxidase-dependent damage in neurons exposed to the proinflammatory cytokine tumor necrosis factor-alpha J. Neurosci. Res. 90 1 2012 229 242 21932365 21932365 PMC3218197
  48. [49]Barth B.M. Stewart-Smeets S. Kuhn T.B. Proinflammatory cytokines provoke oxidative damage to actin in neuronal cells mediated by Rac1 and NADPH oxidase Neuroscientist 41 2 2009 274 285 19344766 PMC2693287 19344766
  49. [50]Lillig C.H. Lönn M.E. Enoksson M. Fernandes A.P. Holmgren A. Short interfering RNA-mediated silencing of glutaredoxin 2 increases the sensitivity of HeLa cells toward doxorubicin and phenylarsine oxide Proc. Natl. Acad. Sci. U. S. A. 101 36 2004 13227 13232 15328416 15328416 PMC516552
  50. [51]Sultana R. Perluigi M. Newman S.F. Pierce W.M. Cini C. Coccia R. Butterfield D.A. Redox proteomic analysis of carbonylated brain proteins in mild cognitive impairment and early Alzheimer’s disease Antioxid. Redox Signal. 12 3 2010 327 336 19686046 19686046 PMC2821142
  51. [52]Nagai K. Betsuyaku T. Kondo T. Nasuhara Y. Nishimura M. Long term smoking with age builds up excessive oxidative stress in bronchoalveolar lavage fluid Thorax 61 6 2006 496 502 16537669 16537669 PMC2111210
  52. [53]Talent J.M. Kong Y. Gracy R.W. A double stain for total and oxidized proteins from two-dimensional fingerprints Anal. Biochem. 263 1 1998 31 38 9750139 9750139
  53. [54]Simonin M.A. Gegout-Pottie P. Minn A. Gillet P. Netter P. Terlain B. Proteoglycan and collagen biochemical variations during fluoroquinolone-induced chondrotoxicity in mice Antimicrob. Agents Chemother. 43 12 1999 2915 2921 10582882 10582882 PMC89587
  54. [55]Simonin M.A. Gegout-Pottie P. Minn A. Gillet P. Netter P. Terlain B. Pefloxacin-induced Achilles tendon toxicity in rodents: biochemical changes in proteoglycan synthesis and oxidative damage to collagen Antimicrob. Agents Chemother. 44 4 2000 867 872 10722483 10722483 PMC89784
  55. [56]Yan L.J. Christians E.S. Liu L. Xiao X. Sohal R.S. Benjamin I.J. Mouse heat shock transcription factor 1 deficiency alters cardiac redox homeostasis and increases mitochondrial oxidative damage EMBO J. 21 19 2002 5164 5172 12356732 12356732 PMC129050
  56. [57]Dickey J.S. Gonzalez Y. Aryal B. Mog S. Nakamura A.J. Redon C.E. Baxa U. Rosen E. Cheng G. Zielonka J. Parekh P. Mason K.P. Joseph J. Kalyanaraman B. Bonner W. Herman E. Shacter E. Rao V.A. Mito-tempol and dexrazoxane exhibit cardioprotective and chemotherapeutic effects through specific protein oxidation and autophagy in a syngeneic breast tumor preclinical model PLOS One 8 8 2013 e70575 23940596 23940596 PMC3734284
  57. [58]Johnson W.T. Newman S.M. Jr. Copper deficiency: a potential model for determining the role of mitochondria in cardiac aging J. Am. Aging Assoc. 26 1–2 2003 19 28 23604915 23604915 PMC3456815
  58. [59]Wu K.L. Berger T. Trichloroethylene metabolism in the rat ovary reduces oocyte fertilizability Chem. Biol. Interact. 170 1 2007 20 30 17673192 17673192 PMC2085368
  59. [60]Wondrak G.T. Cervantes-Laurean D. Jacobson E.L. Jacobson M.K. Histone carbonylation in vivo and in vitro Biochem. J. 351 3 2000 769 777 11042133 11042133 PMC1221418
  60. [61]Wehr N.B. Levine R.L. Quantitation of protein carbonylation by dot blot Anal. Biochem. 423 2 2012 241 245 22326366 22326366 PMC3314425
  61. [62]Buss H. Chan T.P. Sluis K.B. Domigan N.M. Winterbourn C.C. Protein carbonyl measurement by a sensitive ELISA method (vol 23, pg 361, 1997) Biol. Med. 24 1998 1352 9214571
  62. [63]Andresen M. Regueira T. Bruhn A. Perez D. Strobel P. Dougnac A. Marshall G. Leighton F. Lipoperoxidation and protein oxidative damage exhibit different kinetics during septic shock Mediators Inflamm. 2008 2008 168652 18566692 18566692 PMC2430274
  63. [64]Dietrich-Muszalska A. Malinowska J. Olas B. Głowacki R. Bald E. Wachowicz B. Rabe-Jabłońska J. The oxidative stress may be induced by the elevated homocysteine in schizophrenic patients Neurochem. Res. 37 5 2012 1057 1062 22270909 22270909 PMC3321271
  64. [65]Grass D.S. Ross J.M. Family F. Barbour J. James Simpson H. Coulibaly D. Hernandez J. Chen Y. Slavkovich V. Li Y. Graziano J. Santella R.M. Brandt-Rauf P. Chillrud S.N. Airborne particulate metals in the New York City subway: a pilot study to assess the potential for health impacts Environ. Res. 110 1 2010 1 11 19926083 19926083 PMC3155846
  65. [66]Liu Z.M. Li L.Q. Peng M.H. Liu T.W. Qin Z. Guo Y. Xiao K.Y. Ye X.P. Mo X.S. Qin X. Li S. Yan L.N. Shen H.M. Wang L. Wang Q. Wang K.B. Liang R.X. Wei Z.L. Ong C.N. Santella R.M. Peng T. Hepatitis B virus infection contributes to oxidative stress in a population exposed to aflatoxin b1 and high-risk for hepatocellular carcinoma Cancer Lett. 263 2 2008 212 222 18280645 18280645 PMC2676441
  66. [67]Mesia-Vela S. Yeh C.C. Austin J.H. Dounel M. Powell C.A. Reeves A. Santella R.M. Stevenson L. Yankelevitz D. Barr R.G. Plasma carbonyls do not correlate with lung function or computed tomography measures of lung density in older smokers Biomarkers 13 4 2008 422 434 18484356 18484356 PMC2692958
  67. [68]Yeh C.C. Barr R.G. Powell C.A. Mesia-Vela S. Wang Y. Hamade N.K. Austin J.H. Santella R.M. No effect of cigarette smoking dose on oxidized plasma proteins Environ. Res. 106 2 2008 219 225 17996865 17996865 PMC2268894
  68. [69]Zipprich J. Terry M.B. Liao Y. Agrawal M. Gurvich I. Senie R. Santella R.M. Plasma protein carbonyls and breast cancer risk in sisters discordant for breast cancer from the New York site of the Breast Cancer Family Registry Cancer Res. 69 7 2009 2966 2972 19339271 19339271 PMC2666943
  69. [70]Venojärvi M. Aunola S. Puhke R. Marniemi J. Hämäläinen H. Halonen J.P. Lindström J. Rastas M. Hällsten K. Nuutila P. Hänninen O. Atalay M. Exercise training with dietary counselling increases mitochondrial chaperone expression in middle-aged subjects with impaired glucose tolerance Disorders 8 2008 3 18371210 PMC2330145 18371210
  70. [71]Marangon K. Devaraj S. Jialal I. Measurement of protein carbonyls in plasma of smokers and in oxidized LDL by an ELISA Clin. Chem. 45 4 1999 577 578 10102923 10102923
  71. [72]Olas B. Nowak P. Kolodziejczyk J. Ponczek M. Wachowicz B. Protective effects of resveratrol against oxidative/nitrative modifications of plasma proteins and lipids exposed to peroxynitrite J. Nutr. Biochem. 17 2 2006 96 102 16111878 16111878
  72. [73]Olsson M.G. Centlow M. Rutardóttir S. Stenfors I. Larsson J. Hosseini-Maaf B. Olsson M.L. Hansson S.R. Akerström B. Increased levels of cell-free hemoglobin, oxidation markers, and the antioxidative heme scavenger alpha(1)-microglobulin in preeclampsia Free Radic. Biol. Med. 48 2 2010 284 291 19879940 19879940
  73. [74]Rossner P. Jr. Terry M.B. Gammon M.D. Agrawal M. Zhang F.F. Ferris J.S. Teitelbaum S.L. Eng S.M. Gaudet M.M. Neugut A.I. Santella R.M. Plasma protein carbonyl levels and breast cancer risk J. Cell. Mol. Med. 11 5 2007 1138 1148 17979889 17979889 PMC4401280
  74. [75]Grune T. Catalgol B. Licht A. Ermak G. Pickering A.M. Ngo J.K. Davies K.J. HSP70 mediates dissociation and reassociation of the 26S proteasome during adaptation to oxidative stress Free Radic. Biol. Med. 51 7 2011 1355 1364 21767633 21767633 PMC3172204
  75. [76]Hackett T.L. Scarci M. Zheng L. Tan W. Treasure T. Warner J.A. Oxidative modification of albumin in the parenchymal lung tissue of current smokers with chronic obstructive pulmonary disease Respir. Res. 11 2010 180 21176186 21176186 PMC3019185
  76. [77]Sitte N. Merker K. Grune T. Proteasome-dependent degradation of oxidized proteins in MRC-5 fibroblasts FEBS Lett. 440 3 1998 399 402 9872410 9872410
  77. [78]Wang L. Muxin G. Nishida H. Shirakawa C. Sato S. Konishi T. Psychological stress-induced oxidative stress as a model of sub-healthy condition and the effect of TCM Evid. Based Complement. Alternat. Med. 4 2 2007 195 202 17549236 17549236 PMC1876613
  78. [79]Bayram B. Ozcelik B. Grimm S. Roeder T. Schrader C. Ernst I.M. Wagner A.E. Grune T. Frank J. Rimbach G. A diet rich in olive oil phenolics reduces oxidative stress in the heart of SAMP8 mice by induction of Nrf2-dependent gene expression Rejuvenation Res. 15 1 2012 71 81 22236145 22236145 PMC3283438
  79. [80]Efimenko A. Starostina E. Kalinina N. Stolzing A. Angiogenic properties of aged adipose derived mesenchymal stem cells after hypoxic conditioning J. Transl. Med. 9 2011 10 21244679 21244679 PMC3033332
  80. [81]Ganfornina M.D. Do Carmo S. Lora J.M. Torres-Schumann S. Vogel M. Allhorn M. González C. Bastiani M.J. Rassart E. Sanchez D. Apolipoprotein D is involved in the mechanisms regulating protection from oxidative stress Aging Cell 7 4 2008 506 515 18419796 18419796 PMC2574913
  81. [82]Kotarsky H. Keller M. Davoudi M. Levéen P. Karikoski R. Enot D.P. Fellman V. Metabolite profiles reveal energy failure and impaired beta-oxidation in liver of mice with complex III deficiency due to a BCS1L mutation PLOS One 7 7 2012 e41156 22829922 22829922 PMC3400604
  82. [83]Lu L. Oveson B.C. Jo Y.J. Lauer T.W. Usui S. Komeima K. Xie B. Campochiaro P.A. Increased expression of glutathione peroxidase 4 strongly protects retina from oxidative damage Antioxid. Redox Signal. 11 4 2009 715 724 18823256 18823256 PMC2787833
  83. [84]Paromov V. Qui M. Yang H. Smith M. Stone W.L. The influence of N-acetyl-L-cysteine on oxidative stress and nitric oxide synthesis in stimulated macrophages treated with a mustard gas analogue BMC Cell Biol. 9 2008 33 18570648 18570648 PMC2446388
  84. [85]Poppek D. Keck S. Ermak G. Jung T. Stolzing A. Ullrich O. Davies K.J. Grune T. Phosphorylation inhibits turnover of the Tau protein by the proteasome: influence of RCAN1 and oxidative stress Biochem. J. 400 3 2006 511 520 16939415 16939415 PMC1698600
  85. [86]van Ampting M.T. Schonewille A.J. Vink C. Brummer R.J. van der Meer R. Bovee-Oudenhoven I.M. Intestinal barrier function in response to abundant or depleted mucosal glutathione in Salmonella-infected rats BMC Physiol. 9 2009 6 19374741 19374741 PMC2678068
  86. [87]Voss P. Horakova L. Jakstadt M. Kiekebusch D. Grune T. Ferritin oxidation and proteasomal degradation: protection by antioxidants Respirology 40 7 2006 673 683 16983994 16983994

Cited by

Sorted by citations

Authors
Weber, D., Davies, M. J., & Grune, T.
Affiliations
  • German Institute of Human Nutrition (DE)
  • University of Copenhagen (DK)
Corresponding author
Weber, Daniela
ORCID
Venue
Redox Biology
Publisher
Elsevier BV
Published
2015-08
Volume
5
Pages
367-380
ISSN
2213-2317 (ISSN-L)
DOI
10.1016/j.redox.2015.06.005
PMC
PMC4506980
OpenAlex
W565056258
Cited by
295
References
1
Citations by year
2026: 12 · 2025: 28 · 2024: 20 · 2023: 22 · 2022: 32 · 2021: 53 · 2020: 31 · 2019: 38 · 2018: 31 · 2017: 23 · 2016: 5
FWCI
1.91
Type
journal article
Language
en
Open access
Licence
Locations
  • Redox Biology (publishedVersion, cc-by-nc-nd)
  • PubMed Central (publishedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
  • Research at the University of Copenhagen (University of Copenhagen) (publishedVersion, cc-by-nc-nd)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
  • Informationszentrum Lebenswissenschaften (ZB MED) (submittedVersion, cc-by-nc-nd)
Funders
the EU COST (CM1001)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
  • Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
Keywords
protein carbonyls, protein oxidation, sample preparation, derivatization, 2,4-dinitrophenylhydrazine, plasma, cell extracts, tissue homogenates, isolated proteins, reactive oxygen species, spectrophotometric assay, HPLC, Western blot, ELISA, protein stabilization
MeSH terms
Animals, Chromatography, High Pressure Liquid, Enzyme-Linked Immunosorbent Assay, Humans, Oxidation-Reduction, Peptides, Phenylhydrazines, Proteins, Spectrophotometry, Immunoblotting, Biomarkers, Protein Carbonylation

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review