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Oxidative stress in the animal model: the possible protective role of milk serum protein

  • Medical Hypothesis
  • Published:
Mediterranean Journal of Nutrition and Metabolism

Abstract

In the field of biology, free radicals which are derived from the incomplete reduction of oxygen take on great importance; they belong to the so called reactive oxygen species, whose production in the organism is an inevitable consequence of various external or internal factors to which it is exposed. Once free radicals are generated they are often capable of giving rise to chain reactions. A lot of biological molecules are susceptible to the attack by free radicals including lipids, proteins, carbohydrates and nucleic acids. Molecular alterations caused by the radical reactions have been frequently studied and are considered as pathogenetically main passages in the development of many diseases and ageing. In order to face a radical attack, living organisms have developed several biological defensive systems against it: the main ones are represented by anti oxidizing molecules and by enzymatic anti oxidizing systems. Among the various defence systems, glutathione stands out as the principal guarantor of homoeostatic intra-cellular oxidation–reduction. One of glutathione’s most important functions is to act as cysteine “tank”; this amino acid is extremely unstable in the extra-cellular environment and it rapidly auto-oxidates. Whey proteins (WP) are particularly rich in cysteine (cys) and in glutamine (glu) and therefore potentially capable of increasing the organism’s antioxidant defences. It is thought that the principal mechanism which allows WPs to exert their properties is through the contribution of cys and glu, which is rich in these proteins and is used intra-cellularly for the synthesis of glutathione. A diet based on milk serum proteins which supplies a superior quantity of cys, allows for a greater synthesis of hepatic glutathione in oxidative stress conditions. The use of ultra-filtrated WP could represent a useful tool in the control of oxidative stress in numerous pathological situations.

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References

  1. Harman D (1992) Free radical theory of ageing. Mutat Res 275:257–266

    CAS  Google Scholar 

  2. Halliwell B (1989) Tell me about free radicals, doctor: a review. J R Soc Med 82:747–752

    CAS  Google Scholar 

  3. Purkayastha S, Milligan JR, Bernhard WA (2006) The role of hydration in the distribution of free radical trapping in directly ionized DNA. Radiat Res 166:1–8

    Article  CAS  Google Scholar 

  4. Sato K, Kadiiska MB, Ghio AJ, Corbett J, Fann YC, Holland SM, Thurman RG, Mason RP (2002) In vivo lipid-derived free radical formation by NADPH oxidase in acute lung injury induced by lipopolysaccharide: a model for ARDS. FASEB J 16:1713–1720

    Article  CAS  Google Scholar 

  5. Cadenas E, Davies KJ (2000) Mitochondrial free radical generation, oxidative stress, and aging. Free Radic Biol Med 29:222–230

    Article  CAS  Google Scholar 

  6. Sanz A, Caro P, Sanchez JG, Barja G (2006) Effect of lipid restriction on mitochondrial free radical production and oxidative DNA damage. Ann NY Acad Sci 1067:200–209

    Article  CAS  Google Scholar 

  7. Kennedy CH, Mason RP (1990) A reexamination of the cytochrome P-450-catalyzed free radical production from a dihydropyridine. Evidence of trace transition metal catalysis. J Biol Chem 265:11425–11428

    CAS  Google Scholar 

  8. Faivre B, Menu P, Labrude P, Vigneron C (1998) Hemoglobin autooxidation/oxidation mechanisms and methemoglobin prevention or reduction processes in the bloodstream. Literature review and outline of autooxidation reaction. Artif Cells Blood Substit Immobil Biotechnol 26:17–26

    Article  CAS  Google Scholar 

  9. Hunt JV, Dean RT, Wolff SP (1988) Hydroxyl radical production and autoxidative glycosylation. Glucose autoxidation as the cause of protein damage in the experimental glycation model of diabetes mellitus and ageing. Biochem J 256:205–212

    CAS  Google Scholar 

  10. Miyata T, Inagi R, Asahi K, Yamada Y, Horie K, Sakai H, Uchida K, Kurokawa K (1998) Generation of protein carbonyls by glycoxidation and lipoxidation reactions with autoxidation products of ascorbic acid and polyunsaturated fatty acids. FEBS Lett 437:24–28

    Article  CAS  Google Scholar 

  11. Sevanian A, Ursini F (2000) Lipid peroxidation in membranes and low-density lipoproteins: similarities and differences. Free Radic Biol Med 29:306–311

    Article  CAS  Google Scholar 

  12. Esterbauer H, Schaur RJ, Zollner H (1991) Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Radic Biol Med 11:81–128

    Article  CAS  Google Scholar 

  13. Gieseg S, Duggan S, Gebicki JM (2000) Peroxidation of proteins before lipids in U937 cells exposed to peroxyl radicals. Biochem J 350(Pt 1):215–218

    Article  CAS  Google Scholar 

  14. Gebicki S, Gebicki JM (1993) Formation of peroxides in amino acids and proteins exposed to oxygen free radicals. Biochem J 289(Pt 3):743–749

    CAS  Google Scholar 

  15. Neuzil J, Gebicki JM, Stocker R (1993) Radical-induced chain oxidation of proteins and its inhibition by chain-breaking antioxidants. Biochem J 293(Pt 3):601–606

    CAS  Google Scholar 

  16. Davies MJ, Fu S, Wang H, Dean RT (1999) Stable markers of oxidant damage to proteins and their application in the study of human disease. Free Radic Biol Med 27:1151–1163

    Article  CAS  Google Scholar 

  17. Lu SC (1999) Regulation of hepatic glutathione synthesis: current concepts and controversies. FASEB J 13:1169–1183

    CAS  Google Scholar 

  18. Meister A, Anderson ME (1983) Glutathione. Annu Rev Biochem 52:711–760

    Article  CAS  Google Scholar 

  19. de la Asuncion JG, Millan A, Pla R, Bruseghini L, Esteras A, Pallardo FV, Sastre J, Vina J (1996) Mitochondrial glutathione oxidation correlates with age-associated oxidative damage to mitochondrial DNA. FASEB J 10:333–338

    Google Scholar 

  20. Griffith OW (1999) Biologic and pharmacologic regulation of mammalian glutathione synthesis. Free Radic Biol Med 27:922–935

    Article  CAS  Google Scholar 

  21. Fernandez-Checa JC (2003) Redox regulation and signaling lipids in mitochondrial apoptosis. Biochem Biophys Res Commun 304:471–479

    Article  CAS  Google Scholar 

  22. Conner EM, Grisham MB (1996) Inflammation, free radicals, and antioxidants. Nutrition 12:274–277

    Article  CAS  Google Scholar 

  23. Vergely C, Maupoil V, Clermont G, Bril A, Rochette L (2003) Identification and quantification of free radicals during myocardial ischemia and reperfusion using electron paramagnetic resonance spectroscopy. Arch Biochem Biophys 420:209–216

    Article  CAS  Google Scholar 

  24. Halliwell B (1989) Free radicals, reactive oxygen species and human disease: a critical evaluation with special reference to atherosclerosis. Br J Exp Pathol 70:737–757

    CAS  Google Scholar 

  25. Nixon RA, Cataldo AM (1994) Free radicals, proteolysis, and the degeneration of neurons in Alzheimer disease: how essential is the beta-amyloid link? Neurobiol Aging 15:463–469 (discussion 473)

    Article  CAS  Google Scholar 

  26. Dreher D, Junod AF (1996) Role of oxygen free radicals in cancer development. Eur J Cancer 32A:30–38

    Article  CAS  Google Scholar 

  27. Oberley LW (1988) Free radicals and diabetes. Free Radic Biol Med 5:113–124

    Article  CAS  Google Scholar 

  28. Odetti P, Pesce C, Traverso N, Menini S, Maineri EP, Cosso L, Valentini S, Patriarca S, Cottalasso D, Marinari UM, Pronzato MA (2003) Comparative trial of N-acetyl-cysteine, taurine, and oxerutin on skin and kidney damage in long-term experimental diabetes. Diabetes 52:499–505

    Article  CAS  Google Scholar 

  29. Wratten ML, Tetta C, Ursini F, Sevanian A (2000) Oxidant stress in hemodialysis: prevention and treatment strategies. Kidney Int Suppl 76:S126–S132

    Article  CAS  Google Scholar 

  30. Muller FL, Lustgarten MS, Jang Y, Richardson A, Van Remmen H (2007) Trends in oxidative aging theories. Free Radic Biol Med 43:477–503

    Article  CAS  Google Scholar 

  31. Miyata T, Taneda S, Kawai R, Ueda Y, Horiuchi S, Hara M, Maeda K, Monnier VM (1996) Identification of pentosidine as a native structure for advanced glycation end products in beta-2-microglobulin-containing amyloid fibrils in patients with dialysis-related amyloidosis. Proc Natl Acad Sci USA 93:2353–2358

    Article  CAS  Google Scholar 

  32. Kristal BS, Yu BP (1992) An emerging hypothesis: synergistic induction of aging by free radicals and Maillard reactions. J Gerontol 47:B107–B114

    CAS  Google Scholar 

  33. Davies KJ (1987) Protein damage and degradation by oxygen radicals. I. general aspects. J Biol Chem 262:9895–9901

    CAS  Google Scholar 

  34. Tomasi A, Albano E, Banni S, Botti B, Corongiu F, Dessi MA, Iannone A, Vannini V, Dianzani MU (1987) Free-radical metabolism of carbon tetrachloride in rat liver mitochondria. A study of the mechanism of activation. Biochem J 246:313–317

    CAS  Google Scholar 

  35. Narkowicz CK, Vial JH, McCartney PW (1993) Hyperbaric oxygen therapy increases free radical levels in the blood of humans. Free Radic Res Commun 19:71–80

    Article  CAS  Google Scholar 

  36. Duthie SJ, Gardner PT, Morrice PC, Wood SG, Pirie L, Bestwick CC, Milne L, Duthie GG (2005) DNA stability and lipid peroxidation in vitamin E-deficient rats in vivo and colon cells in vitro-modulation by the dietary anthocyanin, cyanidin-3-glycoside. Eur J Nutr 44:195–203

    Article  CAS  Google Scholar 

  37. Anderson ME (1998) Glutathione: an overview of biosynthesis and modulation. Chem Biol Interact 111–112:1–14

    Article  Google Scholar 

  38. Witt EH, Reznick AZ, Viguie CA, Starke-Reed P, Packer L (1992) Exercise, oxidative damage and effects of antioxidant manipulation. J Nutr 122:766–773

    CAS  Google Scholar 

  39. Elia D, Stadler K, Horvath V, Jakus J (2006) Effect of soy- and whey protein-isolate supplemented diet on the redox parameters of trained mice. Eur J Nutr 45:259–266

    Article  CAS  Google Scholar 

  40. Bounous G, Molson JH (2003) The antioxidant system. Anticancer Res 23:1411–1415

    CAS  Google Scholar 

  41. Sukkar SG, Cella F, Patriarca S, Furfaro AL, Abate F, Ferrari C, Balbis E, Traverso N, Cottalasso D (2008) Whey protein, as exclusively nitrogen source, controls food intake and promotes glutathione antioxidant protection in Sprague-Dawley rats. Mediterr J Nutr Metab 1:109–116

    Article  Google Scholar 

  42. Balbis E, Patriarca S, Furfaro AL, Millanta S, Sukkar SG, Marinari UM, Pronzato MA, Cottalasso D, Traverso N (2009) Whey proteins influence hepatic glutathione after CCl4 intoxication. Toxicol Ind Health 25:325–328

    Article  CAS  Google Scholar 

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Correspondence to Samir G. Sukkar.

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Traverso, N., Balbis, E., Sukkar, S.G. et al. Oxidative stress in the animal model: the possible protective role of milk serum protein. Mediterr J Nutr Metab 3, 173–178 (2010). https://doi.org/10.1007/s12349-010-0011-1

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  • DOI: https://doi.org/10.1007/s12349-010-0011-1

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