Table of Contents Author Guidelines Submit a Manuscript
Oxidative Medicine and Cellular Longevity
Volume 2018, Article ID 6015351, 17 pages
https://doi.org/10.1155/2018/6015351
Review Article

Biological Activities, Health Benefits, and Therapeutic Properties of Avenanthramides: From Skin Protection to Prevention and Treatment of Cerebrovascular Diseases

1Department of Clinical and Biological Sciences, University of Torino, Orbassano, Torino, Italy
2CCM Italia, Torino, Italy
3Proteomics & Mass Spectrometry Laboratory, ISPAAM, National Research Council, Napoli, Italy
4Plant Genetics and Breeding, Department of Agriculture, Forest and Food Sciences, University of Torino, Grugliasco, Torino, Italy

Correspondence should be addressed to Saverio Francesco Retta; ti.otinu@atter.ocsecnarf

Received 27 April 2018; Accepted 24 July 2018; Published 23 August 2018

Academic Editor: Daria M. Monti

Copyright © 2018 Andrea Perrelli et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. N. B. Halima, R. B. Saad, B. Khemakhem, I. Fendri, and S. Abdelkafi, “Oat (Avena sativa L.): oil and nutriment compounds valorization for potential use in industrial applications,” Journal of Oleo Science, vol. 64, no. 9, pp. 915–932, 2015. View at Publisher · View at Google Scholar · View at Scopus
  2. C. S. Buer, N. Imin, and M. A. Djordjevic, “Flavonoids: new roles for old molecules,” Journal of Integrative Plant Biology, vol. 52, no. 1, pp. 98–111, 2010. View at Publisher · View at Google Scholar · View at Scopus
  3. C. I. Abuajah, A. C. Ogbonna, and C. M. Osuji, “Functional components and medicinal properties of food: a review,” Journal of Food Science and Technology, vol. 52, no. 5, pp. 2522–2529, 2015. View at Publisher · View at Google Scholar · View at Scopus
  4. C. Rice-Evans and N. Miller, “Measurement of the antioxidant status of dietary constituents, low density lipoproteins and plasma,” Prostaglandins, Leukotrienes, and Essential Fatty Acids, vol. 57, no. 4-5, pp. 499–505, 1997. View at Publisher · View at Google Scholar
  5. A. Kozubek and J. H. P. Tyman, “Resorcinolic lipids, the natural non-isoprenoid phenolic amphiphiles and their biological activity,” Chemical Reviews, vol. 99, no. 1, pp. 1–26, 1999. View at Publisher · View at Google Scholar
  6. R. A. Dixon and N. L. Paiva, “Stress-induced phenylpropanoid metabolism,” Plant Cell, vol. 7, no. 7, pp. 1085–1097, 1995. View at Publisher · View at Google Scholar · View at Scopus
  7. D. Treutter, “Significance of flavonoids in plant resistance and enhancement of their biosynthesis,” Plant Biology, vol. 7, no. 6, pp. 581–591, 2005. View at Publisher · View at Google Scholar · View at Scopus
  8. M. N. Clifford, “Chlorogenic acids and other cinnamates—nature, occurrence and dietary burden,” Journal of Science and Food Agriculture, vol. 79, no. 3, pp. 362–372, 1999. View at Publisher · View at Google Scholar
  9. A. W. Boots, G. R. M. M. Haenen, and A. Bast, “Health effects of quercetin: from antioxidant to nutraceutical,” European Journal of Pharmacology, vol. 585, no. 2-3, pp. 325–337, 2008. View at Publisher · View at Google Scholar · View at Scopus
  10. M. Jang, L. Cai, G. O. Udeani et al., “Cancer chemopreventive activity of resveratrol, a natural product derived from grapes,” Science, vol. 275, no. 5297, pp. 218–220, 1997. View at Publisher · View at Google Scholar
  11. P. Mattila, J. M. Pihlava, and J. Hellstrom, “Contents of phenolic acids, alkyl- and alkenylresorcinols, and avenanthramides in commercial grain products,” Journal of Agricultural and Food Chemistry, vol. 53, no. 21, pp. 8290–8295, 2005. View at Publisher · View at Google Scholar · View at Scopus
  12. F. W. Collins, “Oat phenolics—avenanthramides, novel substituted N-cinnamoylanthranilate alkaloids from oat groats and hulls,” Journal of Agricultural and Food Chemistry, vol. 37, no. 1, pp. 60–66, 1989. View at Publisher · View at Google Scholar · View at Scopus
  13. Y. Okazaki, T. Isobe, Y. Iwata et al., “Metabolism of avenanthramide phytoalexins in oats,” The Plant Journal, vol. 39, no. 4, pp. 560–572, 2004. View at Publisher · View at Google Scholar · View at Scopus
  14. F. W. Collins, “Oat Phenolics—avenanthramides, substituted N-cinnamoyl-anthranilate alkaloids from oat bran and oat hulls,” Cereal Foods World, vol. 31, no. 8, pp. 593–593, 1986. View at Google Scholar
  15. C. L. Emmons and D. M. Peterson, “Antioxidant activity and phenolic content of oat as affected by cultivar and location,” Crop Science, vol. 41, no. 6, 2001. View at Publisher · View at Google Scholar
  16. R. Sur, A. Nigam, D. Grote, F. Liebel, and M. D. Southall, “Avenanthramides, polyphenols from oats, exhibit anti-inflammatory and anti-itch activity,” Archives of Dermatological Research, vol. 300, no. 10, pp. 569–574, 2008. View at Publisher · View at Google Scholar · View at Scopus
  17. M. Meydani, “Potential health benefits of avenanthramides of oats,” Nutrition Reviews, vol. 67, no. 12, pp. 731–735, 2009. View at Publisher · View at Google Scholar · View at Scopus
  18. K. Miyazawa, S. Hamano, and A. Ujiie, “Antiproliferative and c-myc mRNA suppressive effect of Tranilast on newborn human vascular smooth muscle cells in culture,” British Journal of Pharmacology, vol. 118, no. 4, pp. 915–922, 1996. View at Publisher · View at Google Scholar · View at Scopus
  19. L. Li Ji, D. Lay, E. Chung, Y. Fu, and D. M. Peterson, “Effects of avenanthramides on oxidant generation and antioxidant enzyme activity in exercised rats,” Nutrition Research, vol. 23, no. 11, pp. 1579–1590, 2003. View at Publisher · View at Google Scholar · View at Scopus
  20. K. Bratt, K. Sunnerheim, S. Bryngelsson et al., “Avenanthramides in oats (Avena sativa L.) and structure-antioxidant activity relationships,” Journal of Agricultural and Food Chemistry, vol. 51, no. 3, pp. 594–600, 2003. View at Publisher · View at Google Scholar · View at Scopus
  21. C.-Y. Oliver Chen, P. E. Milbury, F. William Collins, and J. B. Blumberg, “Avenanthramides are bioavailable and have antioxidant activity in humans after acute consumption of an enriched mixture from oats,” The Journal of Nutrition, vol. 137, no. 6, pp. 1375–1382, 2007. View at Publisher · View at Google Scholar
  22. C. Y. Chen, P. E. Milbury, H. K. Kwak, F. W. Collins, P. Samuel, and J. B. Blumberg, “Avenanthramides and phenolic acids from oats are bioavailable and act synergistically with vitamin C to enhance hamster and human LDL resistance to oxidation,” The Journal of Nutrition, vol. 134, no. 6, pp. 1459–1466, 2004. View at Publisher · View at Google Scholar
  23. Y. F. Chu, M. L. Wise, A. A. Gulvady et al., “In vitro antioxidant capacity and anti-inflammatory activity of seven common oats,” Food Chemistry, vol. 139, no. 1–4, pp. 426–431, 2013. View at Publisher · View at Google Scholar · View at Scopus
  24. A. Fagerlund, K. Sunnerheim, and L. H. Dimberg, “Radical-scavenging and antioxidant activity of avenanthramides,” Food Chemistry, vol. 113, no. 2, pp. 550–556, 2009. View at Publisher · View at Google Scholar · View at Scopus
  25. W. Guo, L. Nie, D. Wu et al., “Avenanthramides inhibit proliferation of human colon cancer cell lines in vitro,” Nutrition and Cancer, vol. 62, no. 8, pp. 1007–1016, 2010. View at Publisher · View at Google Scholar · View at Scopus
  26. W. Guo, M. L. Wise, F. W. Collins, and M. Meydani, “Avenanthramides, polyphenols from oats, inhibit IL-1β-induced NF-κB activation in endothelial cells,” Free Radical Biology & Medicine, vol. 44, no. 3, pp. 415–429, 2008. View at Publisher · View at Google Scholar · View at Scopus
  27. E. S. Kurtz and W. Wallo, “Colloidal oatmeal: history, chemistry and clinical properties,” Journal of Drugs in Dermatology, vol. 6, no. 2, pp. 167–170, 2007. View at Google Scholar
  28. A. M. Lee-Manion, R. K. Price, J. J. Strain, L. H. Dimberg, K. Sunnerheim, and R. W. Welch, “In vitro antioxidant activity and antigenotoxic effects of avenanthramides and related compounds,” Journal of Agricultural and Food Chemistry, vol. 57, no. 22, pp. 10619–10624, 2009. View at Publisher · View at Google Scholar · View at Scopus
  29. L. Liu, L. Zubik, F. W. Collins, M. Marko, and M. Meydani, “The antiatherogenic potential of oat phenolic compounds,” Atherosclerosis, vol. 175, no. 1, pp. 39–49, 2004. View at Publisher · View at Google Scholar · View at Scopus
  30. L. Nie, M. Wise, D. Peterson, and M. Meydani, “Mechanism by which avenanthramide-c, a polyphenol of oats, blocks cell cycle progression in vascular smooth muscle cells,” Free Radical Biology & Medicine, vol. 41, no. 5, pp. 702–708, 2006. View at Publisher · View at Google Scholar · View at Scopus
  31. L. Nie, M. L. Wise, D. M. Peterson, and M. Meydani, “Avenanthramide, a polyphenol from oats, inhibits vascular smooth muscle cell proliferation and enhances nitric oxide production,” Atherosclerosis, vol. 186, no. 2, pp. 260–266, 2006. View at Publisher · View at Google Scholar · View at Scopus
  32. Y. R. Lee, E. M. Noh, H. J. Oh et al., “Dihydroavenanthramide D inhibits human breast cancer cell invasion through suppression of MMP-9 expression,” Biochemical and Biophysical Research Communications, vol. 405, no. 4, pp. 552–557, 2011. View at Publisher · View at Google Scholar · View at Scopus
  33. H. Azuma, K. Banno, and T. Yoshimura, “Pharmacological properties of N-(3,4-dimethoxycinnamoyl) anthranilic acid (N-5), a new anti-atopic agent,” British Journal of Pharmacology, vol. 58, no. 4, pp. 483–488, 1976. View at Publisher · View at Google Scholar · View at Scopus
  34. H. Komatsu, M. Kojima, N. Tsutsumi et al., “Study of the mechanism of inhibitory-action of Tranilast on chemical mediator release,” The Japanese Journal of Pharmacology, vol. 46, no. 1, pp. 43–51, 1988. View at Publisher · View at Google Scholar · View at Scopus
  35. M. Okuda, T. Ishikawa, Y. Saito, T. Shimizu, and S. Baba, “A clinical evaluation of N-5 with perennial-type allergic rhinitis—a test by the multi-clinic, intergroup, double-blind comparative method,” Annals of Allergy, vol. 53, no. 2, pp. 178–185, 1984. View at Google Scholar
  36. A. Eudes, E. E. K. Baidoo, F. Yang et al., “Production of Tranilast [N-(3,4-dimethoxycinnamoyl)-anthranilic acid] and its analogs in yeast Saccharomyces cerevisiae,” Applied Microbiology and Biotechnology, vol. 89, no. 4, pp. 989–1000, 2011. View at Publisher · View at Google Scholar · View at Scopus
  37. S. Darakhshan and A. B. Pour, “Tranilast: a review of its therapeutic applications,” Pharmacological Research, vol. 91, pp. 15–28, 2015. View at Publisher · View at Google Scholar · View at Scopus
  38. M. Spiecker, I. Lorenz, N. Marx, and H. Darius, “Tranilast inhibits cytokine-induced nuclear factor kappaB activation in vascular endothelial cells,” Molecular Pharmacology, vol. 62, no. 4, pp. 856–863, 2002. View at Publisher · View at Google Scholar · View at Scopus
  39. A. Moglia, C. Comino, S. Lanteri et al., “Production of novel antioxidative phenolic amides through heterologous expression of the plant's chlorogenic acid biosynthesis genes in yeast,” Metabolic Engineering, vol. 12, no. 3, pp. 223–232, 2010. View at Publisher · View at Google Scholar · View at Scopus
  40. A. Moglia, L. Goitre, S. Gianoglio et al., “Evaluation of the bioactive properties of avenanthramide analogs produced in recombinant yeast,” BioFactors, vol. 41, no. 1, pp. 15–27, 2015. View at Publisher · View at Google Scholar · View at Scopus
  41. L. Goitre, P. V. DiStefano, A. Moglia et al., “Up-regulation of NADPH oxidase-mediated redox signaling contributes to the loss of barrier function in KRIT1 deficient endothelium,” Scientific Reports, vol. 7, no. 1, p. 8296, 2017. View at Publisher · View at Google Scholar · View at Scopus
  42. L. Lowen, L. Anderson, and R. W. Harrison, “Cereal flours as antioxidants for fishery products,” Industrial & Engineering Chemistry, vol. 29, no. 2, pp. 151–156, 1937. View at Publisher · View at Google Scholar · View at Scopus
  43. F. N. Peters, “Oat flour as an antioxidant,” Industrial & Engineering Chemistry, vol. 29, no. 2, pp. 146–151, 1937. View at Publisher · View at Google Scholar · View at Scopus
  44. H. Lingnert, K. Vallentin, and C. E. Eriksson, “Measurement of antioxidative effect in model system,” Journal of Food Processing and Preservation, vol. 3, no. 2, pp. 87–103, 1979. View at Publisher · View at Google Scholar · View at Scopus
  45. L. H. Dimberg, O. Theander, and H. Lingnert, “Avenanthramides—a group of phenolic antioxidants in oats,” Cereal Chemistry, vol. 70, no. 6, pp. 637–641, 1993. View at Google Scholar
  46. C. L. Emmons, D. M. Peterson, and G. L. Paul, “Antioxidant capacity of oat (Avena sativa L.) extracts. 2. In vitro antioxidant activity and contents of phenolic and tocol antioxidants,” Journal of Agricultural and Food Chemistry, vol. 47, no. 12, pp. 4894–4898, 1999. View at Publisher · View at Google Scholar · View at Scopus
  47. D. M. Peterson, M. J. Hahn, and C. L. Emmons, “Oat avenanthramides exhibit antioxidant activities in vitro,” Food Chemistry, vol. 79, no. 4, pp. 473–478, 2002. View at Publisher · View at Google Scholar · View at Scopus
  48. Y. Ren, X. Yang, X. Niu, S. Liu, and G. Ren, “Chemical characterization of the avenanthramide-rich extract from oat and its effect on D-galactose-induced oxidative stress in mice,” Journal of Agricultural and Food Chemistry, vol. 59, no. 1, pp. 206–211, 2011. View at Publisher · View at Google Scholar · View at Scopus
  49. H. Mori, H. Tanaka, K. Kawada, H. Nagai, and A. Koda, “Suppressive effects of Tranilast on pulmonary fibrosis and activation of alveolar macrophages in mice treated with bleomycin—role of alveolar macrophages in the fibrosis,” The Japanese Journal of Pharmacology, vol. 67, no. 4, pp. 279–289, 1995. View at Publisher · View at Google Scholar · View at Scopus
  50. J. Fu, Y. Zhu, A. Yerke et al., “Oat avenanthramides induce heme oxygenase-1 expression via Nrf2-mediated signaling in HK-2 cells,” Molecular Nutrition & Food Research, vol. 59, no. 12, pp. 2471–2479, 2015. View at Publisher · View at Google Scholar · View at Scopus
  51. Y. Miyachi, S. Imamura, and Y. Niwa, “The effect of Tranilast of the generation of reactive oxygen species,” Journal of Pharmacobio-Dynamics, vol. 10, no. 6, pp. 255–259, 1987. View at Publisher · View at Google Scholar · View at Scopus
  52. T. Lotts, K. Agelopoulos, N. Q. Phan et al., “Dihydroavenanthramide D inhibits mast cell degranulation and exhibits anti-inflammatory effects through the activation of neurokinin-1 receptor,” Experimental Dermatology, vol. 26, no. 8, pp. 739–742, 2017. View at Publisher · View at Google Scholar · View at Scopus
  53. R. Koenig, J. R. Dickman, C. Kang, T. Zhang, Y. F. Chu, and L. L. Ji, “Avenanthramide supplementation attenuates exercise-induced inflammation in postmenopausal women,” Nutrition Journal, vol. 13, no. 1, p. 21, 2014. View at Publisher · View at Google Scholar · View at Scopus
  54. J. Yang, B. Ou, M. L. Wise, and Y. F. Chu, “In vitro total antioxidant capacity and anti-inflammatory activity of three common oat-derived avenanthramides,” Food Chemistry, vol. 160, pp. 338–345, 2014. View at Publisher · View at Google Scholar · View at Scopus
  55. H. O. Pae, S. O. Jeong, B. S. Koo, H. Y. Ha, K. M. Lee, and H. T. Chung, “Tranilast, an orally active anti-allergic drug, up-regulates the anti-inflammatory heme oxygenase-1 expression but down-regulates the pro-inflammatory cyclooxygenase-2 and inducible nitric oxide synthase expression in RAW264.7 macrophages,” Biochemical and Biophysical Research Communications, vol. 371, no. 3, pp. 361–365, 2008. View at Publisher · View at Google Scholar · View at Scopus
  56. H. Inone, H. Ohshima, H. Kono et al., “Suppressive effects of Tranilast on the expression of inducible cyclooxygenase (COX2) in interleukin-1β-stimulated fibroblasts,” Biochemical Pharmacology, vol. 53, no. 12, pp. 1941–1944, 1997. View at Publisher · View at Google Scholar · View at Scopus
  57. J. Hastings and J. Kenealey, “Avenanthramide-C reduces the viability of MDA-MB-231 breast cancer cells through an apoptotic mechanism,” Cancer Cell International, vol. 17, no. 1, p. 93, 2017. View at Publisher · View at Google Scholar · View at Scopus
  58. M. Hiroi, M. Onda, E. Uchida, and T. Aimoto, “Anti-tumor effect of N-[3,4-dimethoxycinnamoyl]-anthranilic acid (Tranilast) on experimental pancreatic cancer,” Journal of Nippon Medical School, vol. 69, no. 3, pp. 224–234, 2002. View at Publisher · View at Google Scholar · View at Scopus
  59. M. Isaji, H. Miyata, Y. Ajisawa, Y. Takehana, and N. Yoshimura, “Tranilast inhibits the proliferation, chemotaxis and tube formation of human microvascular endothelial cells in vitro and angiogenesis in vivo,” British Journal of Pharmacology, vol. 122, no. 6, pp. 1061–6, 1997. View at Publisher · View at Google Scholar · View at Scopus
  60. M. Isaji, H. Miyata, Y. Ajisawa, and N. Yoshimura, “Inhibition by Tranilast of vascular endothelial growth factor (VEGF)/vascular permeability factor (VPF)-induced increase in vascular permeability in rats,” Life Sciences, vol. 63, no. 4, pp. PL71–PL74, 1998. View at Publisher · View at Google Scholar · View at Scopus
  61. M. Isaji, H. Miyata, and Y. Ajisawa, “Tranilast: a new application in the cardiovascular field as an antiproliferative drug,” Cardiovascular Drug Reviews, vol. 16, no. 3, pp. 288–299, 1998. View at Publisher · View at Google Scholar
  62. M. Isaji, N. Aruga, J. Naito, and H. Miyata, “Inhibition by Tranilast of collagen accumulation in hypersensitive granulomatous inflammation in vivo and of morphological changes and functions of fibroblasts in vitro,” Life Sciences, vol. 55, no. 15, pp. PL287–PL292, 1994. View at Publisher · View at Google Scholar · View at Scopus
  63. K. M. Holmstrom and T. Finkel, “Cellular mechanisms and physiological consequences of redox-dependent signalling,” Nature Reviews Molecular Cell Biology, vol. 15, no. 6, pp. 411–421, 2014. View at Publisher · View at Google Scholar · View at Scopus
  64. S. Miwa, Oxidative Stress in Aging: from Model Systems to Human Diseases, S. Miwa, Ed., Human Press, 2008.
  65. S. F. Retta, P. Chiarugi, L. Trabalzini, P. Pinton, and A. M. Belkin, “Reactive oxygen species: friends and foes of signal transduction,” Journal of Signal Transduction, vol. 2012, Article ID 534029, 1 page, 2012. View at Publisher · View at Google Scholar
  66. L. Goitre, B. Pergolizzi, E. Ferro, L. Trabalzini, and S. F. Retta, “Molecular crosstalk between integrins and cadherins: do reactive oxygen species set the talk?” Journal of Signal Transduction, vol. 2012, Article ID 807682, 12 pages, 2012. View at Publisher · View at Google Scholar
  67. C. Espinosa-Diez, V. Miguel, D. Mennerich et al., “Antioxidant responses and cellular adjustments to oxidative stress,” Redox Biology, vol. 6, pp. 183–197, 2015. View at Publisher · View at Google Scholar · View at Scopus
  68. H. H. H. W. Schmidt, R. Stocker, C. Vollbracht et al., “Antioxidants in translational medicine,” Antioxidants & Redox Signaling, vol. 23, no. 14, pp. 1130–1143, 2015. View at Publisher · View at Google Scholar · View at Scopus
  69. V. Lobo, A. Patil, A. Phatak, and N. Chandra, “Free radicals, antioxidants and functional foods: impact on human health,” Pharmacognosy Reviews, vol. 4, no. 8, pp. 118–126, 2010. View at Publisher · View at Google Scholar · View at Scopus
  70. N. Okarter and R. H. Liu, “Health benefits of whole grain phytochemicals,” Critical Reviews in Food Science and Nutrition, vol. 50, no. 3, pp. 193–208, 2010. View at Publisher · View at Google Scholar · View at Scopus
  71. M. Rogosnitzky, R. Danks, and E. Kardash, “Therapeutic potential of Tranilast, an anti-allergy drug, in proliferative disorders,” Anticancer Research, vol. 32, no. 7, pp. 2471–2478, 2012. View at Google Scholar
  72. J. Fan, J. Stanfield, Y. Guo et al., “Effect of trans-2,3-dimethoxycinnamoyl azide on enhancing antitumor activity of romidepsin on human bladder cancer,” Clinical Cancer Research, vol. 14, no. 4, pp. 1200–1207, 2008. View at Publisher · View at Google Scholar · View at Scopus
  73. T. Goto, T. Nemoto, K. Ogura, T. Hozumi, and N. Funata, “Successful treatment of desmoid tumor of the chest wall with Tranilast: a case report,” Journal of Medical Case Reports, vol. 4, no. 1, p. 384, 2010. View at Publisher · View at Google Scholar
  74. K. Izumi, A. Mizokami, Y. Q. Li et al., “Tranilast inhibits hormone refractory prostate cancer cell proliferation and suppresses transforming growth factor beta1-associated osteoblastic changes,” Prostate, vol. 69, no. 11, pp. 1222–1234, 2009. View at Publisher · View at Google Scholar · View at Scopus
  75. K. Nakajima, Y. Okita, and S. Matsuda, “Sensitivity of scirrhous gastric cancer to 5-fluorouracil and the role of cancer cell-stromal fibroblast interaction,” Oncology Reports, vol. 12, no. 1, pp. 85–90, 2004. View at Publisher · View at Google Scholar
  76. N. Noguchi, S. Kawashiri, A. Tanaka, K. Kato, and H. Nakaya, “Effects of fibroblast growth inhibitor on proliferation and metastasis of oral squamous cell carcinoma,” Oral Oncology, vol. 39, no. 3, pp. 240–247, 2003. View at Publisher · View at Google Scholar · View at Scopus
  77. M. Platten, C. Wild-Bode, W. Wick, J. Leitlein, J. Dichgans, and M. Weller, “N-[3,4-dimethoxycinnamoyl]-anthranilic acid (Tranilast) inhibits transforming growth factor-β release and reduces migration and invasiveness of human malignant glioma cells,” International Journal of Cancer, vol. 93, no. 1, pp. 53–61, 2001. View at Publisher · View at Google Scholar · View at Scopus
  78. H. Shime, M. Kariya, A. Orii et al., “Tranilast inhibits the proliferation of uterine leiomyoma cells in vitro through G1 arrest associated with the induction of p21(waf1) and p53,” The Journal of Clinical Endocrinology & Metabolism, vol. 87, no. 12, pp. 5610–5617, 2002. View at Publisher · View at Google Scholar · View at Scopus
  79. V. Subramaniam, O. Ace, G. J. Prud'homme, and S. Jothy, “Tranilast treatment decreases cell growth, migration and inhibits colony formation of human breast cancer cells,” Experimental and Molecular Pathology, vol. 90, no. 1, pp. 116–122, 2011. View at Publisher · View at Google Scholar · View at Scopus
  80. V. Subramaniam, R. Chakrabarti, G. J. Prud’homme, and S. Jothy, “Tranilast inhibits cell proliferation and migration and promotes apoptosis in murine breast cancer,” Anti-Cancer Drugs, vol. 21, no. 4, pp. 351–361, 2010. View at Publisher · View at Google Scholar · View at Scopus
  81. M. Yamamoto, T. Yamauchi, K. Okano, M. Takahashi, S. Watabe, and Y. Yamamoto, “Tranilast, an anti-allergic drug, down-regulates the growth of cultured neurofibroma cells derived from neurofibromatosis type 1,” The Tohoku Journal of Experimental Medicine, vol. 217, no. 3, pp. 193–201, 2009. View at Publisher · View at Google Scholar · View at Scopus
  82. D. McKay, C. O. Chen, F. W. Collins, and J. Blumberg, “Avenanthramide-enriched oats have an anti-inflammatory action: a pilot clinical trial,” The FASEB Journal, vol. 29, 2015. View at Google Scholar
  83. E. S. Scarpa, M. Mari, E. Antonini, F. Palma, and P. Ninfali, “Natural and synthetic avenanthramides activate caspases 2, 8, 3 and downregulate hTERT, MDR1 and COX-2 genes in CaCo-2 and Hep3B cancer cells,” Food & Function, vol. 9, no. 5, pp. 2913–2921, 2018. View at Publisher · View at Google Scholar
  84. S. F. Retta and A. J. Glading, “Oxidative stress and inflammation in cerebral cavernous malformation disease pathogenesis: two sides of the same coin,” The International Journal of Biochemistry & Cell Biology, vol. 81, Part B, pp. 254–270, 2016. View at Publisher · View at Google Scholar · View at Scopus
  85. H. Choquet, L. Pawlikowska, M. T. Lawton, and H. Kim, “Genetics of cerebral cavernous malformations: current status and future prospects,” Journal of Neurosurgical Sciences, vol. 59, no. 3, pp. 211–220, 2015. View at Google Scholar
  86. E. Trapani and S. F. Retta, “Cerebral cavernous malformation (CCM) disease: from monogenic forms to genetic susceptibility factors,” Journal of Neurosurgical Sciences, vol. 59, no. 3, pp. 201–209, 2015. View at Google Scholar
  87. K. D. Flemming, “Clinical management of cavernous malformations,” Current Cardiology Reports, vol. 19, no. 12, p. 122, 2017. View at Publisher · View at Google Scholar · View at Scopus
  88. L. Goitre, E. de Luca, S. Braggion et al., “KRIT1 loss of function causes a ROS-dependent upregulation of c-Jun,” Free Radical Biology & Medicine, vol. 68, pp. 134–147, 2014. View at Publisher · View at Google Scholar · View at Scopus
  89. L. Goitre, F. Balzac, S. Degani et al., “KRIT1 regulates the homeostasis of intracellular reactive oxygen species,” PLoS One, vol. 5, no. 7, article e11786, 2010. View at Publisher · View at Google Scholar · View at Scopus
  90. C. C. Gibson, W. Zhu, C. T. Davis et al., “Strategy for identifying repurposed drugs for the treatment of cerebral cavernous malformation,” Circulation, vol. 131, no. 3, pp. 289–299, 2015. View at Publisher · View at Google Scholar · View at Scopus
  91. S. Marchi, M. Corricelli, E. Trapani et al., “Defective autophagy is a key feature of cerebral cavernous malformations,” EMBO Molecular Medicine, vol. 7, no. 11, pp. 1403–1417, 2015. View at Publisher · View at Google Scholar · View at Scopus
  92. S. Marchi, E. Trapani, M. Corricelli, L. Goitre, P. Pinton, and S. F. Retta, “Beyond multiple mechanisms and a unique drug: defective autophagy as pivotal player in cerebral cavernous malformation pathogenesis and implications for targeted therapies,” Rare Diseases, vol. 4, no. 1, article e1142640, 2016. View at Publisher · View at Google Scholar · View at Scopus
  93. H. Choquet, E. Trapani, L. Goitre et al., “Cytochrome P450 and matrix metalloproteinase genetic modifiers of disease severity in cerebral cavernous malformation type 1,” Free Radical Biology & Medicine, vol. 92, pp. 100–109, 2016. View at Publisher · View at Google Scholar · View at Scopus
  94. C. Antognelli, E. Trapani, S. Delle Monache et al., “KRIT1 loss-of-function induces a chronic Nrf2-mediated adaptive homeostasis that sensitizes cells to oxidative stress: implication for cerebral cavernous malformation disease,” Free Radical Biology & Medicine, vol. 115, pp. 202–218, 2018. View at Publisher · View at Google Scholar · View at Scopus
  95. C. Antognelli, E. Trapani, S. Delle Monache et al., “Data in support of sustained upregulation of adaptive redox homeostasis mechanisms caused by KRIT1 loss-of-function,” Data in Brief, vol. 16, pp. 929–938, 2018. View at Publisher · View at Google Scholar · View at Scopus
  96. S. Sang and Y. Chu, “Whole grain oats, more than just a fiber: role of unique phytochemicals,” Molecular Nutrition & Food Research, vol. 61, no. 7, 2017. View at Publisher · View at Google Scholar · View at Scopus
  97. V. García-Cañas, C. Simó, C. León, and A. Cifuentes, “Advances in nutrigenomics research: novel and future analytical approaches to investigate the biological activity of natural compounds and food functions,” Journal of Pharmaceutical and Biomedical Analysis, vol. 51, no. 2, pp. 290–304, 2010. View at Publisher · View at Google Scholar · View at Scopus
  98. A. Wilmes, A. Limonciel, L. Aschauer et al., “Application of integrated transcriptomic, proteomic and metabolomic profiling for the delineation of mechanisms of drug induced cell stress,” Journal of Proteomics, vol. 79, pp. 180–194, 2013. View at Publisher · View at Google Scholar · View at Scopus
  99. B. Titz, A. Elamin, F. Martin et al., “Proteomics for systems toxicology,” Computational and Structural Biotechnology Journal, vol. 11, no. 18, pp. 73–90, 2014. View at Publisher · View at Google Scholar · View at Scopus
  100. V. García-Cañas, C. Simó, M. Herrero, E. Ibáñez, and A. Cifuentes, “Present and future challenges in food analysis: foodomics,” Analytical Chemistry, vol. 84, no. 23, pp. 10150–10159, 2012. View at Publisher · View at Google Scholar · View at Scopus
  101. M. Kussmann, M. Affolter, K. Nagy, B. Holst, and L. B. Fay, “Mass spectrometry in nutrition: understanding dietary health effects at the molecular level,” Mass Spectrometry Reviews, vol. 26, no. 6, pp. 727–750, 2007. View at Publisher · View at Google Scholar · View at Scopus
  102. L. Badimon, G. Vilahur, and T. Padro, “Systems biology approaches to understand the effects of nutrition and promote health,” British Journal of Clinical Pharmacology, vol. 83, no. 1, pp. 38–45, 2017. View at Publisher · View at Google Scholar · View at Scopus
  103. T. Zheng, Y. Ni, J. Li, B. K. C. Chow, and G. Panagiotou, “Designing dietary recommendations using system level interactomics analysis and network-based inference,” Frontiers in Physiology, vol. 8, p. 753, 2017. View at Publisher · View at Google Scholar · View at Scopus
  104. A. Valdés, K. A. Artemenko, J. Bergquist, V. García-Cañas, and A. Cifuentes, “Comprehensive proteomic study of the antiproliferative activity of a polyphenol-enriched rosemary extract on colon cancer cells using nanoliquid chromatography-orbitrap MS/MS,” Journal of Proteome Research, vol. 15, no. 6, pp. 1971–1985, 2016. View at Publisher · View at Google Scholar · View at Scopus
  105. A. Valdés, V. García-Cañas, L. Rocamora-Reverte, Á. Gómez-Martínez, J. A. Ferragut, and A. Cifuentes, “Effect of rosemary polyphenols on human colon cancer cells: transcriptomic profiling and functional enrichment analysis,” Genes & Nutrition, vol. 8, no. 1, pp. 43–60, 2013. View at Publisher · View at Google Scholar · View at Scopus
  106. A. Valdés, V. García-Cañas, A. Pérez-Sánchez et al., “Shotgun proteomic analysis to study the decrease of xenograft tumor growth after rosemary extract treatment,” Journal of Chromatography A, vol. 1499, pp. 90–100, 2017. View at Publisher · View at Google Scholar · View at Scopus
  107. A. Valdés, V. García-Cañas, C. Simó et al., “Comprehensive foodomics study on the mechanisms operating at various molecular levels in cancer cells in response to individual rosemary polyphenols,” Analytical Chemistry, vol. 86, no. 19, pp. 9807–9815, 2014. View at Publisher · View at Google Scholar · View at Scopus
  108. A. Valdés, V. García-Cañas, K. A. Artemenko, C. Simó, J. Bergquist, and A. Cifuentes, “Nano-liquid chromatography-orbitrap MS-based quantitative proteomics reveals differences between the mechanisms of action of carnosic acid and carnosol in colon cancer cells,” Molecular & Cellular Proteomics, vol. 16, no. 1, pp. 8–22, 2017. View at Publisher · View at Google Scholar · View at Scopus
  109. F. Olivas-Aguirre, J. Rodrigo-García, N. Martínez-Ruiz et al., “Cyanidin-3-O-glucoside: physical-chemistry, foodomics and health effects,” Molecules, vol. 21, no. 9, 2016. View at Publisher · View at Google Scholar · View at Scopus
  110. G. Breikers, S. G. J. van Breda, F. G. Bouwman et al., “Potential protein markers for nutritional health effects on colorectal cancer in the mouse as revealed by proteomics analysis,” Proteomics, vol. 6, no. 9, pp. 2844–2852, 2006. View at Publisher · View at Google Scholar · View at Scopus
  111. D. Fuchs, R. Piller, J. Linseisen, H. Daniel, and U. Wenzel, “The human peripheral blood mononuclear cell proteome responds to a dietary flaxseed-intervention and proteins identified suggest a protective effect in atherosclerosis,” Proteomics, vol. 7, no. 18, pp. 3278–3288, 2007. View at Publisher · View at Google Scholar · View at Scopus
  112. A. Herzog, B. Kindermann, F. Döring, H. Daniel, and U. Wenzel, “Pleiotropic molecular effects of the pro-apoptotic dietary constituent flavone in human colon cancer cells identified by protein and mRNA expression profiling,” Proteomics, vol. 4, no. 8, pp. 2455–2464, 2004. View at Publisher · View at Google Scholar · View at Scopus
  113. M. P. G. Barnett, J. M. Cooney, Y. E. M. Dommels et al., “Modulation of colonic inflammation in mdr1a−/− mice by green tea polyphenols and their effects on the colon transcriptome and proteome,” Journal of Nutritional Biochemistry, vol. 24, no. 10, pp. 1678–1690, 2013. View at Publisher · View at Google Scholar · View at Scopus
  114. B. de Roos, X. Zhang, G. Rodriguez Gutierrez et al., “Anti-platelet effects of olive oil extract: in vitro functional and proteomic studies,” European Journal of Nutrition, vol. 50, no. 7, pp. 553–562, 2011. View at Publisher · View at Google Scholar · View at Scopus
  115. B. de Roos, A. Geelen, K. Ross et al., “Identification of potential serum biomarkers of inflammation and lipid modulation that are altered by fish oil supplementation in healthy volunteers,” Proteomics, vol. 8, no. 10, pp. 1965–1974, 2008. View at Publisher · View at Google Scholar · View at Scopus
  116. B. Khakimov and S. B. Engelsen, “Resveratrol in the foodomics era: 1 : 25,000,” Annals of the New York Academy of Sciences, vol. 1403, no. 1, pp. 48–58, 2017. View at Publisher · View at Google Scholar · View at Scopus
  117. D. S. Rowlands, J. S. Thomson, B. W. Timmons et al., “Transcriptome and translational signaling following endurance exercise in trained skeletal muscle: impact of dietary protein,” Physiological Genomics, vol. 43, no. 17, pp. 1004–1020, 2011. View at Publisher · View at Google Scholar · View at Scopus
  118. F. Raymond, L. Wang, M. Moser et al., “Consequences of exchanging carbohydrates for proteins in the cholesterol metabolism of mice fed a high-fat diet,” PLoS One, vol. 7, no. 11, article e49058, 2012. View at Publisher · View at Google Scholar
  119. H. T. Dieck, F. Doring, D. Fuchs, H.-P. Roth, and H. Daniel, “Transcriptome and proteome analysis identifies the pathways that increase hepatic lipid accumulation in zinc-deficient rats,” The Journal of Nutrition, vol. 135, no. 2, pp. 199–205, 2005. View at Publisher · View at Google Scholar
  120. S. J. Duthie, G. Horgan, B. de Roos et al., “Blood folate status and expression of proteins involved in immune function, inflammation, and coagulation: biochemical and proteomic changes in the plasma of humans in response to long-term synthetic folic acid supplementation,” Journal of Proteome Research, vol. 9, no. 4, pp. 1941–1950, 2010. View at Publisher · View at Google Scholar · View at Scopus
  121. M. G. Mathias, C. A. Coelho-Landell, M. P. Scott-Boyer et al., “Clinical and vitamin response to a short-term multi-micronutrient intervention in Brazilian children and teens: from population data to interindividual responses,” Molecular Nutrition & Food Research, vol. 62, no. 6, article e1700613, 2018. View at Publisher · View at Google Scholar · View at Scopus
  122. X. Z. Li, S. N. Zhang, K. X. Wang, S. M. Liu, and F. Lu, “iTRAQ-based quantitative proteomics study on the neuroprotective effects of extract of Acanthopanax senticosus harm on SH-SY5Y cells overexpressing A53T mutant α-synuclein,” Neurochemistry International, vol. 72, pp. 37–47, 2014. View at Publisher · View at Google Scholar · View at Scopus
  123. A. Manavalan, L. Feng, S. K. Sze, J. M. Hu, and K. Heese, “New insights into the brain protein metabolism of Gastrodia elata-treated rats by quantitative proteomics,” Journal of Proteomics, vol. 75, no. 8, pp. 2468–2479, 2012. View at Publisher · View at Google Scholar · View at Scopus
  124. U. Ramachandran, A. Manavalan, H. Sundaramurthi et al., “Tianma modulates proteins with various neuro-regenerative modalities in differentiated human neuronal SH-SY5Y cells,” Neurochemistry International, vol. 60, no. 8, pp. 827–836, 2012. View at Publisher · View at Google Scholar · View at Scopus
  125. J. L. Sonnenburg and F. Backhed, “Diet-microbiota interactions as moderators of human metabolism,” Nature, vol. 535, no. 7610, pp. 56–64, 2016. View at Publisher · View at Google Scholar · View at Scopus
  126. A. T. Tang, J. P. Choi, J. J. Kotzin et al., “Endothelial TLR4 and the microbiome drive cerebral cavernous malformations,” Nature, vol. 545, no. 7654, pp. 305–310, 2017. View at Publisher · View at Google Scholar · View at Scopus
  127. I. Dalle-Donne, A. Scaloni, D. Giustarini et al., “Proteins as biomarkers of oxidative/nitrosative stress in diseases: the contribution of redox proteomics,” Mass Spectrometry Reviews, vol. 24, no. 1, pp. 55–99, 2005. View at Publisher · View at Google Scholar · View at Scopus
  128. A. Scaloni, E. Codarin, V. di Maso et al., “Modern strategies to identify new molecular targets for the treatment of liver diseases: the promising role of proteomics and redox proteomics investigations,” Proteomics Clinical Applications, vol. 3, no. 2, pp. 242–262, 2009. View at Publisher · View at Google Scholar · View at Scopus
  129. H. Y. Yang and T. H. Lee, “Antioxidant enzymes as redox-based biomarkers: a brief review,” BMB Reports, vol. 48, no. 4, pp. 200–208, 2015. View at Publisher · View at Google Scholar · View at Scopus
  130. A. Bachi, I. Dalle-Donne, and A. Scaloni, “Redox proteomics: chemical principles, methodological approaches and biological/biomedical promises,” Chemical Reviews, vol. 113, no. 1, pp. 596–698, 2013. View at Publisher · View at Google Scholar · View at Scopus
  131. D. A. Butterfield and M. Perluigi, “Redox proteomics: a key tool for new insights into protein modification with relevance to disease,” Antioxidants & Redox Signaling, vol. 26, no. 7, pp. 277–279, 2017. View at Publisher · View at Google Scholar · View at Scopus
  132. T. Vaisar, P. Mayer, E. Nilsson, X. Q. Zhao, R. Knopp, and B. J. Prazen, “HDL in humans with cardiovascular disease exhibits a proteomic signature,” Clinica Chimica Acta, vol. 411, no. 13-14, pp. 972–979, 2010. View at Publisher · View at Google Scholar · View at Scopus
  133. X. Fu, Y. Wang, J. Kao et al., “Specific sequence motifs direct the oxygenation and chlorination of tryptophan by myeloperoxidase,” Biochemistry, vol. 45, no. 12, pp. 3961–3971, 2006. View at Publisher · View at Google Scholar · View at Scopus
  134. A. S. Shah, L. Tan, J. L. Long, and W. S. Davidson, “Proteomic diversity of high density lipoproteins: our emerging understanding of its importance in lipid transport and beyond,” Journal of Lipid Research, vol. 54, no. 10, pp. 2575–2585, 2013. View at Publisher · View at Google Scholar · View at Scopus
  135. T. Koeck, J. A. Corbett, J. W. Crabb, D. J. Stuehr, and K. S. Aulak, “Glucose-modulated tyrosine nitration in beta cells: targets and consequences,” Archives of Biochemistry and Biophysics, vol. 484, no. 2, pp. 221–231, 2009. View at Publisher · View at Google Scholar · View at Scopus
  136. T. Koeck, B. Willard, J. W. Crabb, M. Kinter, D. J. Stuehr, and K. S. Aulak, “Glucose-mediated tyrosine nitration in adipocytes: targets and consequences,” Free Radical Biology & Medicine, vol. 46, no. 7, pp. 884–892, 2009. View at Publisher · View at Google Scholar · View at Scopus
  137. N. Ranjan Singh, P. Rondeau, L. Hoareau, and E. Bourdon, “Identification of preferential protein targets for carbonylation in human mature adipocytes treated with native or glycated albumin,” Free Radical Research, vol. 41, no. 10, pp. 1078–1088, 2009. View at Publisher · View at Google Scholar · View at Scopus
  138. A. Jaleel, G. C. Henderson, B. J. Madden et al., “Identification of de novo synthesized and relatively older proteins accelerated oxidative damage to de novo synthesized apolipoprotein A-1 in type 1 diabetes,” Diabetes, vol. 59, no. 10, pp. 2366–2374, 2010. View at Publisher · View at Google Scholar · View at Scopus
  139. C. H. Shao, G. J. Rozanski, R. Nagai et al., “Carbonylation of myosin heavy chains in rat heart during diabetes,” Biochemical Pharmacology, vol. 80, no. 2, pp. 205–217, 2010. View at Publisher · View at Google Scholar · View at Scopus
  140. Z. Hashim and S. Zarina, “Advanced glycation end products in diabetic and non-diabetic human subjects suffering from cataract,” Age, vol. 33, no. 3, pp. 377–384, 2011. View at Publisher · View at Google Scholar · View at Scopus
  141. K. Horie, T. Miyata, K. Maeda et al., “Immunohistochemical colocalization of glycoxidation products and lipid peroxidation products in diabetic renal glomerular lesions. Implication for glycoxidative stress in the pathogenesis of diabetic nephropathy,” Journal of Clinical Investigation, vol. 100, no. 12, pp. 2995–3004, 1997. View at Publisher · View at Google Scholar · View at Scopus
  142. M. G. Rosca, T. G. Mustata, M. T. Kinter et al., “Glycation of mitochondrial proteins from diabetic rat kidney is associated with excess superoxide formation,” American Journal of Physiology-Renal Physiology, vol. 289, no. 2, pp. F420–F430, 2005. View at Publisher · View at Google Scholar · View at Scopus
  143. C. H. Shao, H. L. Capek, K. P. Patel et al., “Carbonylation contributes to SERCA2a activity loss and diastolic dysfunction in a rat model of type 1 diabetes,” Diabetes, vol. 60, no. 3, pp. 947–959, 2011. View at Publisher · View at Google Scholar · View at Scopus
  144. K. R. Bidasee, Y. Zhang, C. H. Shao et al., “Diabetes increases formation of advanced glycation end products on sarco(endo)plasmic reticulum Ca2+-ATPase,” Diabetes, vol. 53, no. 2, pp. 463–473, 2004. View at Publisher · View at Google Scholar · View at Scopus
  145. R. Sultana, H. F. Poon, J. Cai et al., “Identification of nitrated proteins in Alzheimer's disease brain using a redox proteomics approach,” Neurobiology of Disease, vol. 22, no. 1, pp. 76–87, 2006. View at Publisher · View at Google Scholar · View at Scopus
  146. J. Choi, M. C. Sullards, J. A. Olzmann et al., “Oxidative damage of DJ-1 is linked to sporadic Parkinson and Alzheimer diseases,” Journal of Biological Chemistry, vol. 281, no. 16, pp. 10816–10824, 2006. View at Publisher · View at Google Scholar · View at Scopus
  147. A. Castegna, M. Aksenov, M. Aksenova et al., “Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part I: creatine kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1,” Free Radical Biology & Medicine, vol. 33, no. 4, pp. 562–571, 2002. View at Publisher · View at Google Scholar · View at Scopus
  148. F. Di Domenico, R. Sultana, A. Ferree et al., “Redox proteomics analyses of the influence of co-expression of wild-type or mutated LRRK2 and Tau on C. elegans protein expression and oxidative modification: relevance to Parkinson disease,” Antioxidants & Redox Signaling, vol. 17, no. 11, pp. 1490–1506, 2012. View at Publisher · View at Google Scholar · View at Scopus
  149. M. Perluigi, R. Sultana, G. Cenini et al., “Redox proteomics identification of 4-hydroxynonenal-modified brain proteins in Alzheimer's disease: role of lipid peroxidation in Alzheimer's disease pathogenesis,” Proteomics - Clinical Applications, vol. 3, no. 6, pp. 682–693, 2009. View at Publisher · View at Google Scholar · View at Scopus
  150. D. A. Butterfield, M. Perluigi, T. Reed et al., “Redox proteomics in selected neurodegenerative disorders: from its infancy to future applications,” Antioxidants & Redox Signaling, vol. 17, no. 11, pp. 1610–1655, 2012. View at Publisher · View at Google Scholar · View at Scopus
  151. D. Perez-Sala, E. Cernuda-Morollon, and F. J. Canada, “Molecular basis for the direct inhibition of AP-1 DNA binding by 15-deoxy-Δ12,14-prostaglandin J2,” Journal of Biological Chemistry, vol. 278, no. 51, pp. 51251–51260, 2003. View at Publisher · View at Google Scholar · View at Scopus
  152. K. S. Aulak, M. Miyagi, L. Yan et al., “Proteomic method identifies proteins nitrated in vivo during inflammatory challenge,” Proceedings of the National Academy of Sciences, vol. 98, no. 21, pp. 12056–12061, 2001. View at Publisher · View at Google Scholar · View at Scopus
  153. E. Barreiro, J. Gea, G. Matar, and S. N. A. Hussain, “Expression and carbonylation of creatine kinase in the quadriceps femoris muscles of patients with chronic obstructive pulmonary disease,” American Journal of Respiratory Cell and Molecular Biology, vol. 33, no. 6, pp. 636–642, 2005. View at Publisher · View at Google Scholar · View at Scopus
  154. E. Barreiro, J. Gea, M. di Falco, L. Kriazhev, S. James, and S. N. A. Hussain, “Protein carbonyl formation in the diaphragm,” American Journal of Respiratory Cell and Molecular Biology, vol. 32, no. 1, pp. 9–17, 2005. View at Publisher · View at Google Scholar · View at Scopus
  155. J. Marin-Corral, J. Minguella, A. L. Ramirez-Sarmiento, S. N. A. Hussain, J. Gea, and E. Barreiro, “Oxidised proteins and superoxide anion production in the diaphragm of severe COPD patients,” European Respiratory Journal, vol. 33, no. 6, pp. 1309–1319, 2009. View at Publisher · View at Google Scholar · View at Scopus
  156. R. R. Cocklin, Y. Zhang, K. D. O’Neill et al., “Identity and localization of advanced glycation end products on human beta2-microglobulin using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry,” Analytical Biochemistry, vol. 314, no. 2, pp. 322–325, 2003. View at Publisher · View at Google Scholar · View at Scopus
  157. T. Miyata, S. Taneda, R. Kawai et al., “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,” Proceedings of the National Academy of Sciences, vol. 93, no. 6, pp. 2353–2358, 1996. View at Publisher · View at Google Scholar · View at Scopus
  158. A. K. Padival, J. W. Crabb, and R. H. Nagaraj, “Methylglyoxal modifies heat shock protein 27 in glomerular mesangial cells,” FEBS Letters, vol. 551, no. 1–3, pp. 113–118, 2003. View at Publisher · View at Google Scholar · View at Scopus
  159. L. Cesaratto, C. Vascotto, C. D'Ambrosio et al., “Overoxidation of peroxiredoxins as an immediate and sensitive marker of oxidative stress in HepG2 cells and its application to the redox effects induced by ischemia/reperfusion in human liver,” Free Radical Research, vol. 39, no. 3, pp. 255–268, 2009. View at Publisher · View at Google Scholar · View at Scopus
  160. E. K. Ahmed, A. Rogowska-Wrzesinska, P. Roepstorff, A. L. Bulteau, and B. Friguet, “Protein modification and replicative senescence of WI-38 human embryonic fibroblasts,” Aging Cell, vol. 9, no. 2, pp. 252–272, 2010. View at Publisher · View at Google Scholar · View at Scopus
  161. M. B. Feeney and C. Schoneich, “Tyrosine modifications in aging,” Antioxidants & Redox Signaling, vol. 17, no. 11, pp. 1571–1579, 2012. View at Publisher · View at Google Scholar · View at Scopus
  162. C. Bregere, I. Rebrin, and R. S. Sohal, “Detection and characterization of in vivo nitration and oxidation of tryptophan residues in proteins,” Methods in Enzymology, vol. 441, pp. 339–349, 2008. View at Publisher · View at Google Scholar · View at Scopus
  163. J. P. Rabek, W. H. Boylston III, and J. Papaconstantinou, “Carbonylation of ER chaperone proteins in aged mouse liver,” Biochemical and Biophysical Research Communications, vol. 305, no. 3, pp. 566–572, 2003. View at Publisher · View at Google Scholar · View at Scopus
  164. R. A. Vaishnav, M. L. Getchell, H. F. Poon et al., “Oxidative stress in the aging murine olfactory bulb: redox proteomics and cellular localization,” Journal of Neuroscience Research, vol. 85, no. 2, pp. 373–385, 2007. View at Publisher · View at Google Scholar · View at Scopus
  165. L. Prokai, L. J. Yan, J. L. Vera-Serrano, S. M. Stevens, and M. J. Forster, “Mass spectrometry-based survey of age-associated protein carbonylation in rat brain mitochondria,” Journal of Mass Spectrometry, vol. 42, no. 12, pp. 1583–1589, 2007. View at Publisher · View at Google Scholar · View at Scopus
  166. S. Poggioli, H. Bakala, and B. Friguet, “Age-related increase of protein glycation in peripheral blood lymphocytes is restricted to preferential target proteins,” Experimental Gerontology, vol. 37, no. 10-11, pp. 1207–1215, 2002. View at Publisher · View at Google Scholar · View at Scopus
  167. M. Hamelin, J. Mary, M. Vostry, B. Friguet, and H. Bakala, “Glycation damage targets glutamate dehydrogenase in the rat liver mitochondrial matrix during aging,” FEBS Journal, vol. 274, no. 22, pp. 5949–5961, 2007. View at Publisher · View at Google Scholar · View at Scopus
  168. S. J. Hong, G. Gokulrangan, and C. Schoneich, “Proteomic analysis of age dependent nitration of rat cardiac proteins by solution isoelectric focusing coupled to nanoHPLC tandem mass spectrometry,” Experimental Gerontology, vol. 42, no. 7, pp. 639–651, 2007. View at Publisher · View at Google Scholar · View at Scopus
  169. R. Tyther, B. McDonagh, and D. Sheehan, “Proteomics in investigation of protein nitration in kidney disease: technical challenges and perspectives from the spontaneously hypertensive rat,” Mass Spectrometry Reviews, vol. 30, no. 1, pp. 121–141, 2011. View at Publisher · View at Google Scholar · View at Scopus
  170. R. Tyther, A. Ahmeda, E. Johns, and D. Sheehan, “Proteomic identification of tyrosine nitration targets in kidney of spontaneously hypertensive rats,” Proteomics, vol. 7, no. 24, pp. 4555–4564, 2007. View at Publisher · View at Google Scholar · View at Scopus
  171. R. Tyther, A. Ahmeda, E. Johns, and D. Sheehan, “Protein carbonylation in kidney medulla of the spontaneously hypertensive rat,” Proteomics - Clinical Applications, vol. 3, no. 3, pp. 338–346, 2009. View at Publisher · View at Google Scholar · View at Scopus
  172. C. Vascotto, A. M. Salzano, C. D'Ambrosio et al., “Oxidized transthyretin in amniotic fluid as an early marker of preeclampsia,” Journal of Proteome Research, vol. 6, no. 1, pp. 160–170, 2007. View at Publisher · View at Google Scholar · View at Scopus
  173. G. Boden, C. Homko, C. A. Barrero et al., “Excessive caloric intake acutely causes oxidative stress, GLUT4 carbonylation, and insulin resistance in healthy men,” Science Translational Medicine, vol. 7, no. 304, article 304re7, 2015. View at Publisher · View at Google Scholar · View at Scopus
  174. K. E. Menger, A. M. James, H. M. Cochemé et al., “Fasting, but not aging, dramatically alters the redox status of cysteine residues on proteins in Drosophila melanogaster,” Cell Reports, vol. 13, no. 6, p. 1285, 2015. View at Publisher · View at Google Scholar · View at Scopus
  175. L. Méndez, M. Pazos, E. Molinar-Toribio et al., “Protein carbonylation associated to high-fat, high-sucrose diet and its metabolic effects,” The Journal of Nutritional Biochemistry, vol. 25, no. 12, pp. 1243–1253, 2014. View at Publisher · View at Google Scholar · View at Scopus
  176. N. Morales-Prieto, J. Ruiz-Laguna, and N. Abril, “Dietary Se supplementation partially restores the REDOX proteomic map of M. spretus liver exposed to p,p'-DDE,” Food and Chemical Toxicology, vol. 114, pp. 292–301, 2018. View at Publisher · View at Google Scholar · View at Scopus
  177. W. O. Opii, G. Joshi, E. Head et al., “Proteomic identification of brain proteins in the canine model of human aging following a long-term treatment with antioxidants and a program of behavioral enrichment: relevance to Alzheimer's disease,” Neurobiology of Aging, vol. 29, no. 1, pp. 51–70, 2008. View at Publisher · View at Google Scholar · View at Scopus
  178. S. K. Suh, B. L. Hood, B. J. Kim, T. P. Conrads, T. D. Veenstra, and B. J. Song, “Identification of oxidized mitochondrial proteins in alcohol-exposed human hepatoma cells and mouse liver,” Proteomics, vol. 4, no. 11, pp. 3401–3412, 2004. View at Publisher · View at Google Scholar · View at Scopus
  179. V. B. Patel, C. H. Spencer, T. A. Young, M. O. Lively, and C. C. Cunningham, “Effects of 4-hydroxynonenal on mitochondrial 3-hydroxy-3-methylglutaryl (HMG-CoA) synthase,” Free Radical Biology & Medicine, vol. 43, no. 11, pp. 1499–1507, 2007. View at Publisher · View at Google Scholar · View at Scopus
  180. A. Venkatraman, A. Landar, A. J. Davis et al., “Oxidative modification of hepatic mitochondria protein thiols: effect of chronic alcohol consumption,” American Journal of Physiology-Gastrointestinal and Liver Physiology, vol. 286, no. 4, pp. G521–G527, 2004. View at Publisher · View at Google Scholar
  181. Y. Li, Z. Luo, X. Wu et al., “Proteomic analyses of cysteine redox in high-fat-fed and fasted mouse livers: implications for liver metabolic homeostasis,” Journal of Proteome Research, vol. 17, no. 1, pp. 129–140, 2018. View at Publisher · View at Google Scholar · View at Scopus
  182. D. L. Carbone, J. A. Doorn, Z. Kiebler, and D. R. Petersen, “Cysteine modification by lipid peroxidation products inhibits protein disulfide isomerase,” Chemical Research in Toxicology, vol. 18, no. 8, pp. 1324–1331, 2005. View at Publisher · View at Google Scholar · View at Scopus
  183. B. J. Song, K. H. Moon, N. U. Olsson, and N. Salem Jr., “Prevention of alcoholic fatty liver and mitochondrial dysfunction in the rat by long-chain polyunsaturated fatty acids,” Journal of Hepatology, vol. 49, no. 2, pp. 262–273, 2008. View at Publisher · View at Google Scholar · View at Scopus
  184. K. H. Moon, B. L. Hood, B. J. Kim et al., “Inactivation of oxidized and S-nitrosylated mitochondrial proteins in alcoholic fatty liver of rats,” Hepatology, vol. 44, no. 5, pp. 1218–1230, 2006. View at Publisher · View at Google Scholar · View at Scopus
  185. M. Dodson, M. Redmann, N. S. Rajasekaran, V. Darley-Usmar, and J. Zhang, “KEAP1-NRF2 signalling and autophagy in protection against oxidative and reductive proteotoxicity,” Biochemical Journal, vol. 469, no. 3, pp. 347–355, 2015. View at Publisher · View at Google Scholar · View at Scopus
  186. J. Johansen, A. K. Harris, D. J. Rychly, and A. Ergul, “Oxidative stress and the use of antioxidants in diabetes: linking basic science to clinical practice,” Cardiovascular Diabetology, vol. 4, no. 1, p. 5, 2005. View at Publisher · View at Google Scholar · View at Scopus