Polyphenol compounds and PKC signaling

Biochimica et Biophysica Acta - General Subjects

Volumn 1860, Issue 10, 2016, Pages 2107-2121

  Das, Joydip ^a   Ramani, Rashmi ^a   Suraju, M Olufemi ^a  

^a UNIVERSITY OF HOUSTON   (United States)

Author keywords

Antioxidant; Cancer; Polyphenol; Protein kinase C; Signal transduction

Indexed keywords

ACTEOSIDE; ANTINEOPLASTIC AGENT; APIGENIN; CAFFEIC ACID; CALCIUM CHANNEL; CALCIUM ION; CHLOROGENIC ACID; CURCUMIN; ELLAGIC ACID; EPIGALLOCATECHIN GALLATE; HYDROXYTYROSOL; ISOPROTEIN; MIYABENOL C; MYRICETIN; POLYPHENOL DERIVATIVE; PROTEIN KINASE C; PROTEIN SERINE THREONINE KINASE; PROTOCATECHUIC ACID; QUERCETIN; RESVERATROL; RHAMNETIN; ROSMARINIC ACID; ROTTLERIN; TANNIN; THEAFLAVIN 3,3 DIGALLATE; UNCLASSIFIED DRUG; UNINDEXED DRUG; VANICOSIDE A1; VANICOSIDE B2; VERBACOSIDE; VINIFERIN; POLYPHENOL; STILBENE DERIVATIVE;

ANTIDIABETIC ACTIVITY; ANTINEOPLASTIC ACTIVITY; ANTIOXIDANT ACTIVITY; BINDING SITE; COLON CANCER; CONTROLLED STUDY; DRUG BIOAVAILABILITY; DRUG MECHANISM; DRUG STRUCTURE; HUMAN; IC50; PRIORITY JOURNAL; PROPHYLAXIS; PROTEIN PHOSPHORYLATION; PROTEIN TARGETING; REVIEW; ANTAGONISTS AND INHIBITORS; DRUG EFFECTS; ENZYMOLOGY; GENETICS; METABOLISM; NEOPLASMS; PATHOLOGY; SIGNAL TRANSDUCTION;

CURCUMIN; HUMANS; NEOPLASMS; POLYPHENOLS; PROTEIN KINASE C; SIGNAL TRANSDUCTION; STILBENES;

EID: 84978280528     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2016.06.022     Document Type: Review

References (276)

1. [1] Manach, C., Scalbert, A., Morand, C., Remesy, C., Jimenez, L., Polyphenols: food sources and bioavailability. Am. J. Clin. Nutr. 79 (2004), 727–747.
2. [2] Hearon, W.M., Macgregor, W.S., The naturally occurring lignans. Chem. Rev. 55 (1955), 957–1068.
3. [3] Robbins, R.J., Phenolic acids in foods: an overview of analytical methodology. J. Agric. Food Chem. 51 (2003), 2866–2887.
4. [4] Shen, T., Wang, X.N., Lou, H.X., Natural stilbenes: an overview. Nat. Prod. Rep. 26 (2009), 916–935.
5. [5] Perron, N.R., Brumaghim, J.L., A review of the antioxidant mechanisms of polyphenol compounds related to iron binding. Cell Biochem. Biophys. 53 (2009), 75–100.
6. [6] Pasinetti, G.M., Ho, L., Role of grape seed polyphenols in Alzheimer's disease neuropathology. Nutr. Diet. Suppl. 2010 (2010), 97–103.
7. [7] Rojanathammanee, L., Puig, K.L., Combs, C.K., Pomegranate polyphenols and extract inhibit nuclear factor of activated T-cell activity and microglial activation in vitro and in a transgenic mouse model of Alzheimer disease. J. Nutr. 143 (2013), 597–605.
8. [8] Maher, P., Dargusch, R., Bodai, L., Gerard, P.E., Purcell, J.M., Marsh, J.L., ERK activation by the polyphenols fisetin and resveratrol provides neuroprotection in multiple models of Huntington's disease. Hum. Mol. Genet. 20 (2011), 261–270.
9. [9] Anandhan, A., Tamilselvam, K., Radhiga, T., Rao, S., Essa, M.M., Manivasagam, T., Theaflavin, a black tea polyphenol, protects nigral dopaminergic neurons against chronic MPTP/probenecid induced Parkinson's disease. Brain Res. 1433 (2012), 104–113.
10. [10] Vauzour, D., Ravaioli, G., Vafeiadou, K., Rodriguez-Mateos, A., Angeloni, C., Spencer, J.P.E., Peroxynitrite induced formation of the neurotoxins 5-S-cysteinyl-dopamine and DHBT-1: implications for Parkinson's disease and protection by polyphenols. Arch. Biochem. Biophys. 476 (2008), 145–151.
11. [11] Duchnowicz, P., Bors, M., Podsedek, A., Koter-Michalak, M., Broncel, M., Effect of polyphenols extracts from Brassica vegetables on erythrocyte membranes (in vitro study). Environ. Toxicol. Pharmacol. 34 (2012), 783–790.
12. [12] Sathyapalan, T., Beckett, S., Rigby, A.S., Mellor, D.D., Atkin, S.L., High cocoa polyphenol rich chocolate may reduce the burden of the symptoms in chronic fatigue syndrome. Nutr. J., 9, 2010, 55, 10.1186/1475-2891-9-55.
13. [13] Gupta, A., Vij, G., Sharma, S., Tirkey, N., Rishi, P., Chopra, K., Curcumin, a polyphenolic antioxidant, attenuates chronic fatigue syndrome in murine water immersion stress model. Immunobiol. 214 (2009), 33–39.
14. [14] Sabu, M.C., Smitha, K., Ramadasan, K., Anti-diabetic activity of green tea polyphenols and their role in reducing oxidative stress in experimental diabetes. J. Ethnopharmacol. 83 (2002), 109–116.
15. [15] Wang, L.M., Wang, Y.J., Cui, M., Luo, W.J., Wang, X.J., Barber, P.A., Chen, Z.Y., A dietary polyphenol resveratrol acts to provide neuroprotection in recurrent stroke models by regulating AMPK and SIRT1 signaling, thereby reducing energy requirements during ischemia. Eur. J. Neurosci. 37 (2013), 1669–1681.
16. [16] Negishi, H., Xu, J.W., Ikeda, K., Njelekela, M., Nara, Y., Yamori, Y., Black and green tea polyphenols attenuate blood pressure increases in stroke-prone spontaneously hypertensive rats. J. Nutr. 134 (2004), 38–42.
17. [17] Sarkar, F.H., Li, Y.W., Mechanisms of cancer chemoprevention by soy isoflavone genistein. Cancer Metast. Rev. 21 (2002), 265–280.
18. [18] Knekt, P., Jarvinen, R., Seppanen, R., Heliovaara, M., Teppo, L., Pukkala, E., Aromaa, A., Dietary flavonoids and the risk of lung cancer and other malignant neoplasms. Am. J. Epidemiol. 146 (1997), 223–230.
19. [19] Aviram, M., Dornfeld, L., Pomegranate juice consumption inhibits serum angiotensin converting enzyme activity and reduces systolic blood pressure. Atherosclerosis 158 (2001), 195–198.
20. [20] Zern, T.L., Fernandez, M.L., Cardioprotective effects of dietary polyphenols. J. Nutr. 135 (2005), 2291–2294.
21. [21] Banji, D., Banji, O.J.F., Abbagoni, S., Hayath, M.S., Kambam, S., Chiluka, V.L., Amelioration of behavioral aberrations and oxidative markers by green tea extract in valproate induced autism in animals. Brain Res. 1410 (2011), 141–151.
22. [22] Dvorakova, M., Jezova, D., Blazicek, P., Trebaticka, J., Skodacek, I., Suba, J., Waczulikova, I., Rohdewald, P., Durackova, Z., Urinary catecholamines in children with attention deficit hyperactivity disorder (ADHD): modulation by a polyphenolic extract from pine bark (Pycnogenol((R))). Nutr. Neurosci. 10 (2007), 151–157.
23. [23] Jalel, A., Soumaya, G.S., Hamdaoui, M.H., Vitiligo treatment with vitamins, minerals and polyphenol supplementation. Indian J. Dermatol. 54 (2009), 357–360.
24. [24] Khodja, N.I., Chataigneau, T., Auger, C., Schini-Kerth, V.B., Grape-derived polyphenols improve aging-related endothelial dysfunction in rat mesenteric artery: role of oxidative stress and the angiotensin system. PloS one, 7, 2012.
25. [25] Mandel, S.A., Amit, T., Weinreb, O., Youdim, M.B.H., Understanding the broad-spectrum neuroprotective action profile of green tea polyphenols in aging and neurodegenerative diseases. J. Alzheimers Dis. 25 (2011), 187–208.
26. [26] Du, W.X., Olsen, C.W., Avena-Bustillos, R.J., Friedman, M., McHugh, T.H., Physical and antibacterial properties of edible films formulated with apple skin polyphenols. J. Food Sci. 76 (2011), M149–M155.
27. [27] Daglia, M., Polyphenols as antimicrobial agents. Curr. Opin. Biotech. 23 (2012), 174–181.
28. [28] Francisco, V., Figueirinha, A., Costa, G., Lopes, M.C., Garcia-Rodriguez, C., Cruz, M.T., Batista, M.T., Anti-inflammatory properties of polyphenols from Cymbopogon citratus by inhibition of NF-kappa B pathway. Planta Med. 77 (2011), 1419–1420.
29. [29] Scholz, E.P., Zitron, E., Katus, H.A., Karle, C.A., Cardiovascular ion channels as a molecular target of flavonoids. Cardiovasc. Ther. 28 (2010), e46–e52.
30. [30] Lu, J.M., Lin, P.H., Yao, Q., Chen, C., Chemical and molecular mechanisms of antioxidants: experimental approaches and model systems. J. Cell. Mol. Med. 14 (2010), 840–860.
31. [31] Chun, O.K., Kim, D.O., Lee, C.Y., Superoxide radical scavenging activity of the major polyphenols in fresh plums. J. Agric. Food Chem. 51 (2003), 8067–8072.
32. [32] Forman, H.J., Torres, M., Fukuto, J., Redox signaling. Mol. Cell. Biochem. 234 (2002), 49–62.
33. [33] Valko, M., Leibfritz, D., Moncol, J., Cronin, M.T., Mazur, M., Telser, J., Free radicals and antioxidants in normal physiological functions and human disease. Int. J. Biochem. Cell Biol. 39 (2007), 44–84.
34. [34] Ahmed, K.A., Sawa, T., Ihara, H., Kasamatsu, S., Yoshitake, J., Rahaman, M.M., Okamoto, T., Fujii, S., Akaike, T., Regulation by mitochondrial superoxide and NADPH oxidase of cellular formation of nitrated cyclic GMP: potential implications for ROS signalling. Biochem. J. 441 (2012), 719–730.
35. [35] Frohlich, D.A., McCabe, M.T., Arnold, R.S., Day, M.L., The role of Nrf2 in increased reactive oxygen species and DNA damage in prostate tumorigenesis. Oncogene 27 (2008), 4353–4362.
36. [36] Gray, S.P., Di Marco, E., Okabe, J., Szyndralewiez, C., Heitz, F., Montezano, A.C., de Haan, J.B., Koulis, C., El-Osta, A., Andrews, K.L., Chin-Dusting, J.P.F., Touyz, R.M., Wingler, K., Cooper, M.E., Schmidt, H.H.H.W., Jandeleit-Dahm, K.A., NADPH oxidase 1 plays a key role in diabetes mellitus-accelerated atherosclerosis. Circulation, 127, 2013, 1888.
37. [37] Mohsenzadegan, M., Mirshafiey, A., The immunopathogenic role of reactive oxygen species in Alzheimer disease. Iran. J. Allergy Asthm. 11 (2012), 203–216.
38. [38] Cassarino, D.S., Fall, C.P., Swerdlow, R.H., Smith, T.S., Halvorsen, E.M., Miller, S.W., Parks, J.P., Parker, W.D. Jr., Bennett, J.P. Jr., Elevated reactive oxygen species and antioxidant enzyme activities in animal and cellular models of Parkinson's disease. Biochim. Biophys. Acta 1362 (1997), 77–86.
39. [39] Lin, H.C., Tsai, S.H., Chen, C.S., Chang, Y.C., Lee, C.M., Lai, Z.Y., Lin, C.M., Structure-activity relationship of coumarin derivatives on xanthine oxidase-inhibiting and free radical-scavenging activities. Biochem. Pharmacol. 75 (2008), 1416–1425.
40. [40] Farines, V., Monje, M.C., Telo, J.P., Hnawia, E., Sauvain, M., Nepveu, F., Polyphenols as superoxide dismutase modulators and ligands for estrogen receptors. Anal. Chim. Acta 513 (2004), 103–111.
41. [41] Li, Y.B., Cao, Z.X., Zhu, H., Upregulation of endogenous antioxidants and phase 2 enzymes by the red wine polyphenol, resveratrol in cultured aortic smooth muscle cells leads to cytoprotection against oxidative and electrophilic stress. Pharmacol. Res. 53 (2006), 6–15.
42. [42] Azzi, A., Davies, K.J.A., Kelly, F., Free radical biology - terminology and critical thinking. FEBS Lett. 558 (2004), 3–6.
43. [43] Halliwell, B., Rafter, J., Jenner, A., Health promotion by flavonoids, tocopherols, tocotrienols, and other phenols: direct or indirect effects? Antioxidant or not?. Am. J. Clin. Nutr. 81 (2005), 268S–276S.
44. [44] Azzi, A., Boscoboinik, D., Hensey, C., The protein kinase C family. Eur. J. Biochem. 208 (1992), 547–557.
45. [45] Takai, Y., Kishimoto, A., Inoue, M., Nishizuka, Y., Studies on a cyclic nucleotide-independent protein kinase and its proenzyme in mammalian tissues. I. Purification and characterization of an active enzyme from bovine cerebellum. J. Biol. Chem. 252 (1977), 7603–7609.
46. [46] Inoue, M., Kishimoto, A., Takai, Y., Nishizuka, Y., Studies on a cyclic nucleotide-independent protein kinase and its proenzyme in mammalian tissues. II. Proenzyme and its activation by calcium-dependent protease from rat brain. J. Biol. Chem. 252 (1977), 7610–7616.
47. [47] Musashi, M., Ota, S., Shiroshita, N., The role of protein kinase C isoforms in cell proliferation and apoptosis. Int. J. Hematol. 72 (2000), 12–19.
48. [48] Nishizuka, Y., Intracellular signaling by hydrolysis of phospholipids and activation of protein-kinase-C. Science 258 (1992), 607–614.
49. [49] Nogues, X., Protein kinase C, learning and memory: a circular determinism between physiology and behaviour. Prog. Neuro-Psychoph. 21 (1997), 507–529.
50. [50] Wu-Zhang, A.X., Newton, A.C., Protein kinase C pharmacology: refining the toolbox. Biochem. J. 452 (2013), 195–209.
51. [51] Newton, A.C., Regulation of the structure, function, and localization of protein kinase C. FASEB J., 11, 1997, A1298.
52. [52] Tobias, I.S., Kaulich, M., Kim, P.K., Simon, N., Jacinto, E., Dowdy, S.F., King, C.C., Newton, A.C., Protein kinase Czeta exhibits constitutive phosphorylation and phosphatidylinositol-3,4,5-triphosphate-independent regulation. Biochem. J. 473 (2016), 509–523.
53. [53] Cohen, S., Braiman, A., Shubinsky, G., Isakov, N., Protein kinase C-theta in platelet activation. FEBS Lett. 585 (2011), 3208–3215.
54. [54] Duquesnes, N., Lezoualc'h, F., Crozatier, B., PKC-delta and PKC-epsilon: foes of the same family or strangers?. J. Mol. Cell. Cardiol. 51 (2011), 665–673.
55. [55] Goldberg, M., Steinberg, S.F., Tissue-specific developmental regulation of protein kinase C isoforms. Biochem. Pharmacol. 51 (1996), 1089–1093.
56. [56] Koivunen, J., Aaltonen, V., Peltonen, J., Protein kinase C (PKC) family in cancer progression. Cancer Lett. 235 (2006), 1–10.
57. [57] Griner, E.M., Kazanietz, M.G., Protein kinase C and other diacylglycerol effectors in cancer. Nature Rev. Cancer 7 (2007), 281–294.
58. [58] Simonis, G., Braun, M.U., Kirrstetter, M., Schon, S.P., Strasser, R.H., Mechanisms of myocardial remodeling: ramiprilat blocks the expressional upregulation of protein kinase C-epsilon in the surviving myocardium early after infarction. J. Cardiovasc. Pharmacol. 41 (2003), 780–787.
59. 2 +-sensitive isoforms in the failing human heart. Circulation 99 (1999), 384–391.
60. [60] Palaniyandi, S.S., Sun, L., Ferreira, J.C., Mochly-Rosen, D., Protein kinase C in heart failure: a therapeutic target?. Cardiovasc. Res. 82 (2009), 229–239.
61. [61] Ferreira, J.C., Brum, P.C., Mochly-Rosen, D., betaIIPKC and epsilonPKC isozymes as potential pharmacological targets in cardiac hypertrophy and heart failure. J. Mol. Cell. Cardiol. 51 (2011), 479–484.
62. [62] Bright, R., Mochly-Rosen, D., The role of protein kinase C in cerebral ischemic and reperfusion injury. Stroke 36 (2005), 2781–2790.
63. [63] Dempsey, E.C., Cool, C.D., Littler, C.M., Lung disease and PKCs. Pharmacol. Res. 55 (2007), 545–559.
64. [64] Li, J., Gobe, G., Protein kinase C activation and its role in kidney disease. Nephrol. (Carlton) 11 (2006), 428–434.
65. [65] Ishii, H., Jirousek, M.R., Koya, D., Takagi, C., Xia, P., Clermont, A., Bursell, S.E., Kern, T.S., Ballas, L.M., Heath, W.F., Stramm, L.E., Feener, E.P., King, G.L., Amelioration of vascular dysfunctions in diabetic rats by an oral PKC beta inhibitor. Science 272 (1996), 728–731.
66. [66] Maioli, E., Valacchi, G., Rottlerin: bases for a possible usage in psoriasis. Current Drug Metabol. 11 (2010), 425–430.
67. [67] DiazGranados, N., Zarate, C.A. Jr., A review of the preclinical and clinical evidence for protein kinase C as a target for drug development for bipolar disorder. Curr. Psychiatry Rep. 10 (2008), 510–519.
68. [68] Zhang, D., Anantharam, V., Kanthasamy, A., Kanthasamy, A.G., Neuroprotective effect of protein kinase C delta inhibitor rottlerin in cell culture and animal models of Parkinson's disease. J. Pharmacol. Exp. Ther. 322 (2007), 913–922.
69. [69] Burguillos, M.A., Deierborg, T., Kavanagh, E., Persson, A., Hajji, N., Garcia-Quintanilla, A., Cano, J., Brundin, P., Englund, E., Venero, J.L., Joseph, B., Caspase signalling controls microglia activation and neurotoxicity. Nature 472 (2011), 319–324.
70. [70] Sun, M.K., Alkon, D.L., Pharmacology of protein kinase C activators: cognition-enhancing and antidementic therapeutics. Pharmacol. Ther. 127 (2010), 66–77.
71. [71] Alkon, D.L., Sun, M.K., Nelson, T.J., PKC signaling deficits: a mechanistic hypothesis for the origins of Alzheimer's disease. Trends Pharmacol. Sci. 28 (2007), 51–60.
72. [72] Garrido, J.L., Godoy, J.A., Alvarez, A., Bronfman, M., Inestrosa, N.C., Protein kinase C inhibits amyloid beta peptide neurotoxicity by acting on members of the Wnt pathway. FASEB J. 16 (2002), 1982–1984.
73. [73] Sweitzer, S.M., Wong, S.M., Peters, M.C., Mochly-Rosen, D., Yeomans, D.C., Kendig, J.J., Protein kinase C epsilon and gamma: involvement in formalin-induced nociception in neonatal rats. J. Pharmacol. Exp. Ther. 309 (2004), 616–625.
74. [74] Mochly-Rosen, D., Das, K., Grimes, K.V., Protein kinase C, an elusive therapeutic target?. Nat. Rev. Drug Discov. 11 (2012), 937–957.
75. [75] Steinberg, S.F., Structural basis of protein kinase C isoform function. Physiol. Rev. 88 (2008), 1341–1378.
76. [76] Colon-Gonzalez, F., Kazanietz, M.G., C1 domains exposed: from diacylglycerol binding to protein-protein interactions. Biochim. Biophys. Acta 1761 (2006), 827–837.
77. [77] Yamasaki, T., Takahashi, A., Pan, J.Z., Yamaguchi, N., Yokoyama, K.K., Phosphorylation of activation transcription factor-2 at serine 121 by protein kinase C controls c-Jun-mediated activation of transcription. J. Biol. Chem. 284 (2009), 8567–8581.
78. [78] Kazanietz, M.G., Krausz, K.W., Blumberg, P.M., Differential irreversible insertion of protein kinase C into phospholipid vesicles by phorbol esters and related activators. J. Biol. Chem. 267 (1992), 20878–20886.
79. [79] Sharkey, N.A., Leach, K.L., Blumberg, P.M., Competitive inhibition by diacylglycerol of specific phorbol ester binding. Proc. Natl. Acad. Sci. U. S. A. 81 (1984), 607–610.
80. [80] Farah, C.A., Sossin, W.S., The role of C2 domains in PKC signaling. Adv Eexp Med Biol. 740 (2012), 663–683.
81. [81] Hanks, S.K., Hunter, T., Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J. 9 (1995), 576–596.
82. [82] Zhang, G., Kazanietz, M.G., Blumberg, P.M., Hurley, J.H., Crystal structure of the cys2 activator-binding domain of protein kinase C delta in complex with phorbol ester. Cell 81 (1995), 917–924.
83. [83] Verdaguer, N., Corbalan-Garcia, S., Ochoa, W.F., Fita, I., Gomez-Fernandez, J.C., Ca(2 +) bridges the C2 membrane-binding domain of protein kinase Calpha directly to phosphatidylserine. EMBO J. 18 (1999), 6329–6338.
84. [84] Grodsky, N., Li, Y., Bouzida, D., Love, R., Jensen, J., Nodes, B., Nonomiya, J., Grant, S., Structure of the catalytic domain of human protein kinase C beta II complexed with a bisindolylmaleimide inhibitor. Biochemistry 45 (2006), 13970–13981.
85. [85] Leonard, T.A., Rozycki, B., Saidi, L.F., Hummer, G., Hurley, J.H., Crystal structure and allosteric activation of protein kinase C betaII. Cell 144 (2011), 55–66.
86. [86] Ananthanarayanan, B., Stahelin, R.V., Digman, M.A., Cho, W., Activation mechanisms of conventional protein kinase C isoforms are determined by the ligand affinity and conformational flexibility of their C1 domains. J. Biol. Chem. 278 (2003), 46886–46894.
87. [87] Das, J., Rahman, G.M., C1 domains: structure and ligand-binding properties. Chem. Rev. 114 (2014), 12108–12131.
88. [88] House, C., Kemp, B.E., Protein kinase C contains a pseudosubstrate prototope in its regulatory domain. Science 238 (1987), 1726–1728.
89. [89] Orr, J.W., Newton, A.C., Intrapeptide regulation of protein kinase C. J. Biol. Chem. 269 (1994), 8383–8387.
90. [90] Kirwan, A.F., Bibby, A.C., Mvilongo, T., Riedel, H., Burke, T., Millis, S.Z., Parissenti, A.M., Inhibition of protein kinase C catalytic activity by additional regions within the human protein kinase Calpha-regulatory domain lying outside of the pseudosubstrate sequence. Biochem. J. 373 (2003), 571–581.
91. [91] Huang, H.C., Nguyen, T., Pickett, C.B., Regulation of the antioxidant response element by protein kinase C-mediated phosphorylation of NF-E2-related factor 2. Proc. Natl. Acad. Sci. U. S. A. 97 (2000), 12475–12480.
92. [92] Huang, H.C., Nguyen, T., Pickett, C.B., Phosphorylation of Nrf2 at Ser-40 by protein kinase C regulates antioxidant response element-mediated transcription. J. Biol. Chem. 277 (2002), 42769–42774.
93. [93] Bloom, D.A., Jaiswal, A.K., Phosphorylation of Nrf2 at Ser40 by protein kinase C in response to antioxidants leads to the release of Nrf2 from INrf2, but is not required for Nrf2 stabilization/accumulation in the nucleus and transcriptional activation of antioxidant response element-mediated NAD(P)H:quinone oxidoreductase-1 gene expression. J. Biol. Chem. 278 (2003), 44675–44682.
94. [94] Antal, C.E., Newton, A.C., Tuning the signalling output of protein kinase C. Biochem. Soc. Trans. 42 (2014), 1477–1483.
95. [95] Mishra, S., Vinayak, M., Anti-carcinogenic action of ellagic acid mediated via modulation of oxidative stress regulated genes in Dalton lymphoma bearing mice. Leuk. Lymphoma 52 (2011), 2155–2161.
96. [96] Varadkar, P., Dubey, P., Krishna, M., Verma, N., Modulation of radiation-induced protein kinase C activity by phenolics. J. Radiol. Prot. 21 (2001), 361–370.
97. [97] Goel, A., Aggarwal, B.B., Curcumin, the golden spice from Indian saffron, is a chemosensitizer and radiosensitizer for tumors and chemoprotector and radioprotector for normal organs. Nutr. Cancer 62 (2010), 919–930.
98. [98] Epstein, J., Sanderson, I.R., Macdonald, T.T., Curcumin as a therapeutic agent: the evidence from in vitro, animal and human studies. Br. J. Nutr. 103 (2010), 1545–1557.
99. [99] Singh, S., From exotic spice to modern drug?. Cell 130 (2007), 765–768.
100. [100] Ataie, A., Sabetkasaei, M., Haghparast, A., Moghaddam, A.H., Ataee, R., Moghaddam, S.N., Curcumin exerts neuroprotective effects against homocysteine intracerebroventricular injection-induced cognitive impairment and oxidative stress in rat brain. J. Med. Food 13 (2010), 821–826.
101. [101] Cemil, B., Topuz, K., Demircan, M.N., Kurt, G., Tun, K., Kutlay, M., Ipcioglu, O., Kucukodaci, Z., Curcumin improves early functional results after experimental spinal cord injury. Acta Neurochir. 152 (2010), 1583–1590.
102. [102] Morimoto, T., Sunagawa, Y., Fujita, M., Hasegawa, K., Novel heart failure therapy targeting transcriptional pathway in cardiomyocytes by a natural compound, curcumin. Circ. J. 74 (2010), 1059–1066.
103. [103] Lin, J.K., Molecular targets of curcumin. Adv. Exp. Med. Biol. 595 (2007), 227–243.
104. [104] Johnson, J.J., Mukhtar, H., Curcumin for chemoprevention of colon cancer. Cancer Lett. 255 (2007), 170–181.
105. [105] Soetikno, V., Watanabe, K., Sari, F.R., Harima, M., Thandavarayan, R.A., Veeraveedu, P.T., Arozal, W., Sukumaran, V., Lakshmanan, A.P., Arumugam, S., Suzuki, K., Curcumin attenuates diabetic nephropathy by inhibiting PKC-alpha and PKC-beta1 activity in streptozotocin-induced type I diabetic rats. Mol. Nutr. Food Res. 55 (2011), 1655–1665.
106. [106] Soetikno, V., Sari, F.R., Sukumaran, V., Lakshmanan, A.P., Mito, S., Harima, M., Thandavarayan, R.A., Suzuki, K., Nagata, M., Takagi, R., Watanabe, K., Curcumin prevents diabetic cardiomyopathy in streptozotocin-induced diabetic rats: possible involvement of PKC-MAPK signaling pathway. Eur. J. Pharmaceut. Sci. 47 (2012), 604–614.
107. [107] Rushworth, S.A., Ogborne, R.M., Charalambos, C.A., O'Connell, M.A., Role of protein kinase C delta in curcumin-induced antioxidant response element-mediated gene expression in human monocytes. Biochem. Biophys. Res. Commun. 341 (2006), 1007–1016.
108. [108] Liu, J.Y., Lin, S.J., Lin, J.K., Inhibitory effects of curcumin on protein kinase C activity induced by 12-O-tetradecanoyl-phorbol-13-acetate in NIH 3T3 cells. Carcinogenesis 14 (1993), 857–861.
109. [109] Reddy, S., Aggarwal, B.B., Curcumin is a non-competitive and selective inhibitor of phosphorylase kinase. FEBS Lett. 341 (1994), 19–22.
110. [110] Lin, J.K., Chen, Y.C., Huang, Y.T., Lin-Shiau, S.Y., Suppression of protein kinase C and nuclear oncogene expression as possible molecular mechanisms of cancer chemoprevention by apigenin and curcumin. J. Cell. Biochem. Suppl. 28-29 (1997), 39–48.
111. [111] Rungseesantivanon, S., Thenchaisri, N., Ruangvejvorachai, P., Patumraj, S., Curcumin supplementation could improve diabetes-induced endothelial dysfunction associated with decreased vascular superoxide production and PKC inhibition. BMC Complement. Altern. Med., 10, 2010, 57.
112. [112] Garg, R., Ramchandani, A.G., Maru, G.B., Curcumin decreases 12-O-tetradecanoylphorbol-13-acetate-induced protein kinase C translocation to modulate downstream targets in mouse skin. Carcinogenesis 29 (2008), 1249–1257.
113. [113] Liao, K.K., Wu, M.J., Chen, P.Y., Huang, S.W., Chiu, S.J., Ho, C.T., Yen, J.H., Curcuminoids promote neurite outgrowth in PC12 cells through MAPK/ERK- and PKC-dependent pathways. J. Agric. Food Chem. 60 (2012), 433–443.
114. [114] Mahmmoud, Y.A., Modulation of protein kinase C by curcumin; inhibition and activation switched by calcium ions. Br. J. Pharmacol. 150 (2007), 200–208.
115. [115] Perez-Lara, A., Corbalan-Garcia, S., Gomez-Fernandez, J.C., Curcumin modulates PKCalpha activity by a membrane-dependent effect. Arch. Biochem. Biophys. 513 (2011), 36–41.
116. [116] Pany, S., Majhi, A., Das, J., Selective modulation of protein kinase C alpha over protein kinase C epsilon by curcumin and its derivatives in CHO-K1 cells. Biochemistry 55 (2016), 2135–2143.
117. [117] Majhi, A., Rahman, G.M., Panchal, S., Das, J., Binding of curcumin and its long chain derivatives to the activator binding domain of novel protein kinase C. Bioorg. Med. Chem. 18 (2010), 1591–1598.
118. [118] Das, J., Pany, S., Panchal, S., Majhi, A., Rahman, G.M., Binding of isoxazole and pyrazole derivatives of curcumin with the activator binding domain of novel protein kinase C. Bioorg. Med. Chem. 19 (2011), 6196–6202.
119. [119] Pervaiz, S., Resveratrol: from grapevines to mammalian biology. FASEB J. 17 (2003), 1975–1985.
120. [120] Wang, Y., Catana, F., Yang, Y., Roderick, R., van Breemen, R.B., An LC-MS method for analyzing total resveratrol in grape juice, cranberry juice, and in wine. J. Agric. Food Chem. 50 (2002), 431–435.
121. [121] Wu, J.M., Hsieh, T.C., Resveratrol: a cardioprotective substance. Ann. N. Y. Acad. Sci. 1215 (2011), 16–21.
122. [122] Petrovski, G., Gurusamy, N., Das, D.K., Resveratrol in cardiovascular health and disease. Ann. N. Y. Acad. Sci. 1215 (2011), 22–33.
123. [123] Szekeres, T., Saiko, P., Fritzer-Szekeres, M., Djavan, B., Jager, W., Chemopreventive effects of resveratrol and resveratrol derivatives. Ann. N. Y. Acad. Sci. 1215 (2011), 89–95.
124. [124] Gupta, S.C., Kannappan, R., Reuter, S., Kim, J.H., Aggarwal, B.B., Chemosensitization of tumors by resveratrol. Ann. N. Y. Acad. Sci. 1215 (2011), 150–160.
125. [125] Shukla, Y., Singh, R., Resveratrol and cellular mechanisms of cancer prevention. Ann. N. Y. Acad. Sci. 1215 (2011), 1–8.
126. [126] Richard, T., Pawlus, A.D., Iglesias, M.L., Pedrot, E., Waffo-Teguo, P., Merillon, J.M., Monti, J.P., Neuroprotective properties of resveratrol and derivatives. Ann. N. Y. Acad. Sci. 1215 (2011), 103–108.
127. [127] Kundu, J.K., Surh, Y.J., Cancer chemopreventive and therapeutic potential of resveratrol: mechanistic perspectives. Cancer Lett. 269 (2008), 243–261.
128. [128] Subbaramaiah, K., Chung, W.J., Michaluart, P., Telang, N., Tanabe, T., Inoue, H., Jang, M., Pezzuto, J.M., Dannenberg, A.J., Resveratrol inhibits cyclooxygenase-2 transcription and activity in phorbol ester-treated human mammary epithelial cells. J. Biol. Chem. 273 (1998), 21875–21882.
129. [129] Woo, J.H., Lim, J.H., Kim, Y.H., Suh, S.I., Min, D.S., Chang, J.S., Lee, Y.H., Park, J.W., Kwon, T.K., Resveratrol inhibits phorbol myristate acetate-induced matrix metalloproteinase-9 expression by inhibiting JNK and PKC delta signal transduction. Oncogene 23 (2004), 1845–1853.
130. [130] Fang, J.Y., Li, Z.H., Li, Q., Huang, W.S., Kang, L., Wang, J.P., Resveratrol affects protein kinase C activity and promotes apoptosis in human colon carcinoma cells. Asian Pac. J. Cancer Prev. 13 (2012), 6017–6022.
131. [131] Schwedhelm, E., Maas, R., Troost, R., Boger, R.H., Clinical pharmacokinetics of antioxidants and their impact on systemic oxidative stress. Clin. Pharmacokinet. 42 (2003), 437–459.
132. [132] Patel, K.R., Scott, E., Brown, V.A., Gescher, A.J., Steward, W.P., Brown, K., Clinical trials of resveratrol. Ann. N. Y. Acad. Sci. 1215 (2011), 161–169.
133. [133] Menard, C., Bastianetto, S., Quirion, R., Neuroprotective effects of resveratrol and epigallocatechin gallate polyphenols are mediated by the activation of protein kinase C gamma. Front. Cell. Neurosci., 7, 2013, 281.
134. [134] Drabikova, K., Perecko, T., Nosal, R., Harmatha, J., Smidrkal, J., Jancinova, V., Polyphenol derivatives - potential regulators of neutrophil activity. Interdisciplinary Toxicol. 5 (2012), 65–70.
135. [135] Atten, M.J., Godoy-Romero, E., Attar, B.M., Milson, T., Zopel, M., Holian, O., Resveratrol regulates cellular PKC alpha and delta to inhibit growth and induce apoptosis in gastric cancer cells. Investig. New Drugs 23 (2005), 111–119.
136. [136] Stewart, J.R., O'Brian, C.A., Resveratrol antagonizes EGFR-dependent Erk1/2 activation in human androgen-independent prostate cancer cells with associated isozyme-selective PKC alpha inhibition. Investig. New Drugs 22 (2004), 107–117.
137. [137] Stewart, J.R., Ward, N.E., Ioannides, C.G., O'Brian, C.A., Resveratrol preferentially inhibits protein kinase C-catalyzed phosphorylation of a cofactor-independent, arginine-rich protein substrate by a novel mechanism. Biochemistry 38 (1999), 13244–13251.
138. [138] Patel, R., Apostolatos, A., Carter, G., Ajmo, J., Gali, M., Cooper, D.R., You, M., Bisht, K.S., Patel, N.A., Protein kinase C delta (PKCdelta) splice variants modulate apoptosis pathway in 3T3L1 cells during adipogenesis: identification of PKCdeltaII inhibitor. J. Biol. Chem. 288 (2013), 26834–26846.
139. [139] Slater, S.J., Seiz, J.L., Cook, A.C., Stagliano, B.A., Buzas, C.J., Inhibition of protein kinase C by resveratrol. Biochim. Biophys. Acta 1637 (2003), 59–69.
140. [140] Das, J., Pany, S., Majhi, A., Chemical modifications of resveratrol for improved protein kinase C alpha activity. Bioorg. Med. Chem. 19 (2011), 5321–5333.
141. [141] Pany, S., Majhi, A., Das, J., PKC activation by resveratrol derivatives with unsaturated aliphatic chain. PLoS One, 7, 2012, e52888.
142. [142] Singh, B.N., Shankar, S., Srivastava, R.K., Green tea catechin, epigallocatechin-3-gallate (EGCG): mechanisms, perspectives and clinical applications. Biochem. Pharmacol. 82 (2011), 1807–1821.
143. [143] Chowdhury, A., Sarkar, J., Chakraborti, T., Pramanik, P.K., Chakraborti, S., Protective role of epigallocatechin-3-gallate in health and disease: a perspective. Biomed. Pharmacother. 78 (2016), 50–59.
144. [144] Reznichenko, L., Amit, T., Zheng, H., Avramovich-Tirosh, Y., Youdim, M.B.H., Weinreb, O., Mandel, S., Reduction of iron-regulated amyloid precursor protein and beta-amyloid peptide by (−)-epigallocatechin-3-gallate in cell cultures: implications for iron chelation in Alzheimer's disease. J. Neurochem. 97 (2006), 527–536.
145. [145] Morinobu, A., Biao, W., Tanaka, S., Horiuchi, M., Jun, L., Tsuji, G., Sakai, Y., Kurosaka, M., Kumagai, S., (−)-epigallocatechin-3-gallate suppresses osteoclast differentiation and ameliorates experimental arthritis in mice. Arthritis Rheum. 58 (2008), 2012–2018.
146. [146] Tammela, P., Ekokoski, E., Garcia-Horsman, A., Talman, V., Finel, M., Tuominen, R., Vuorela, P., Screening of natural compounds and their derivatives as potential protein kinase C inhibitors. Drug Develop. Res. 63 (2004), 76–87.
147. [147] Kitano, K., Nam, K.Y., Kimura, S., Fujiki, H., Imanishi, Y., Sealing effects of (−)-epigallocatechin gallate on protein kinase C and protein phosphatase 2A. Biophys. Chem. 65 (1997), 157–164.
148. [148] Wang, S.I., Mukhtar, H., Gene expression profile in human prostate LNCaP cancer cells by (−) epigallocatechin-3-gallate. Cancer Lett. 182 (2002), 43–51.
149. [149] Levites, Y., Amit, T., Mandel, S., Youdim, M.B., Neuroprotection and neurorescue against Abeta toxicity and PKC-dependent release of nonamyloidogenic soluble precursor protein by green tea polyphenol (−)-epigallocatechin-3-gallate. FASEB J. 17 (2003), 952–954.
150. [150] Kalfon, L., Youdim, M.B., Mandel, S.A., Green tea polyphenol (−)-epigallocatechin-3-gallate promotes the rapid protein kinase C- and proteasome-mediated degradation of Bad: implications for neuroprotection. J. Neurochem. 100 (2007), 992–1002.
151. [151] Levites, Y., Amit, T., Youdim, M.B., Mandel, S., Involvement of protein kinase C activation and cell survival/cell cycle genes in green tea polyphenol (−)-epigallocatechin 3-gallate neuroprotective action. J. Biol. Chem. 277 (2002), 30574–30580.
152. [152] Park, S.J., Jeong, J.M., Jeong, H.S., Park, J.S., Kim, N.H., Effects of epigallocatechin-3-gallate on the expression of TGF-beta1, PKC alpha/betaII, and NF-kappaB in high-glucose-stimulated glomerular epithelial cells. Chonnam. Med. J. 47 (2011), 116–121.
153. [153] Adhikary, G., Chew, Y.C., Reece, E.A., Eckert, R.L., PKC-delta and -eta, MEKK-1, MEK-6, MEK-3, and p38-delta are essential mediators of the response of normal human epidermal keratinocytes to differentiating agents. J. Invest. Dermatol. 130 (2010), 2017–2030.
154. [154] Li, R., Peng, N., Li, X.P., Le, W.D., (−)-Epigallocatechin gallate regulates dopamine transporter internalization via protein kinase C-dependent pathway. Brain Res. 1097 (2006), 85–89.
155. +-dependent glutamate release via activation of protein kinase C in rat cerebral cortex. Synapse 61 (2007), 889–902.
156. [156] Yang, J., Han, Y., Chen, C., Sun, H., He, D., Guo, J., Jiang, B., Zhou, L., Zeng, C., EGCG attenuates high glucose-induced endothelial cell inflammation by suppression of PKC and NF-kappaB signaling in human umbilical vein endothelial cells. Life Sci. 92 (2013), 589–597.
157. [157] Yang, J., Han, Y., Sun, H., Chen, C., He, D., Guo, J., Yu, C., Jiang, B., Zhou, L., Zeng, C., (−)-Epigallocatechin gallate suppresses proliferation of vascular smooth muscle cells induced by high glucose by inhibition of PKC and ERK1/2 signalings. J. Agric. Food Chem. 59 (2011), 11483–11490.
158. [158] Bode, A.M., Dong, Z., Epigallocatechin 3-gallate and green tea catechins: united they work, divided they fail. Cancer Prev. Res. (Phila.) 2 (2009), 514–517.
159. [159] Tachibana, H., Koga, K., Fujimura, Y., Yamada, K., A receptor for green tea polyphenol EGCG. Nat. Struct. Mol. Biol. 11 (2004), 380–381.
160. [160] Gundimeda, U., McNeill, T.H., Elhiani, A.A., Schiffman, J.E., Hinton, D.R., Gopalakrishna, R., Green tea polyphenols precondition against cell death induced by oxygen-glucose deprivation via stimulation of laminin receptor, generation of reactive oxygen species, and activation of protein kinase Cepsilon. J. Biol. Chem. 287 (2012), 34694–34708.
161. [161] Tsukamoto, S., Hirotsu, K., Kumazoe, M., Goto, Y., Sugihara, K., Suda, T., Tsurudome, Y., Suzuki, T., Yamashita, S., Kim, Y., Huang, Y., Yamada, K., Tachibana, H., Green tea polyphenol EGCG induces lipid-raft clustering and apoptotic cell death by activating protein kinase Cdelta and acid sphingomyelinase through a 67 kDa laminin receptor in multiple myeloma cells. Biochem. J. 443 (2012), 525–534.
162. [162] Han, X.Z., Shen, T., Lou, H.X., Dietary polyphenols and their biological significance. Int. J. Mol. Sci. 8 (2007), 950–988.
163. [163] Bastianetto, S., Zheng, W.H., Quirion, R., Neuroprotective abilities of resveratrol and other red wine constituents against nitric oxide-related toxicity in cultured hippocampal neurons. Br. J. Pharmacol. 131 (2000), 711–720.
164. [164] Crozier, A., Lean, M.E.J., McDonald, M.S., Black, C., Quantitative analysis of the flavonoid content of commercial tomatoes, onions, lettuce, and celery. J. Agric. Food Chem. 45 (1997), 590–595.
165. [165] Kelly, G.S., Quercetin. Monograph. Altern. Med. Rev. 16 (2011), 172–194.
166. [166] Ferriola, P.C., Cody, V., Middleton, E. Jr., Protein kinase C inhibition by plant flavonoids. Kinetic mechanisms and structure-activity relationships. Biochem. Pharmacol. 38 (1989), 1617–1624.
167. [167] End, D.W., Look, R.A., Shaffer, N.L., Balles, E.A., Persico, F.J., Non-selective inhibition of mammalian protein kinases by flavinoids in vitro. Res. Commun. Chem. Pathol. Pharmacol. 56 (1987), 75–86.
168. [168] Picq, M., Dubois, M., Munari-Silem, Y., Prigent, A.F., Pacheco, H., Flavonoid modulation of protein kinase C activation. Life Sci. 44 (1989), 1563–1571.
169. [169] Lin, C.W., Hou, W.C., Shen, S.C., Juan, S.H., Ko, C.H., Wang, L.M., Chen, Y.C., Quercetin inhibition of tumor invasion via suppressing PKC delta/ERK/AP-1-dependent matrix metalloproteinase-9 activation in breast carcinoma cells. Carcinogenesis 29 (2008), 1807–1815.
170. [170] Kang, T.B., Liang, N.C., Effect of quercetin on activities of protein kinase C and tyrosine protein kinase from HL-60 cells. Acta Pharmacol. Sin. 18 (1997), 374–376.
171. [171] Zhang, X.M., Huang, S.P., Xu, Q., Quercetin inhibits the invasion of murine melanoma B16-BL6 cells by decreasing pro-MMP-9 via the PKC pathway. Cancer Chemother. Pharmacol. 53 (2004), 82–88.
172. [172] Maurya, A.K., Vinayak, M., Anticarcinogenic action of quercetin by downregulation of phosphatidylinositol 3-kinase (PI3K) and protein kinase C (PKC) via induction of p53 in hepatocellular carcinoma (HepG2) cell line. Mol. Biol. Rep. 42 (2015), 1419–1429.
173. [173] Maurya, A.K., Vinayak, M., Modulation of PKC signaling and induction of apoptosis through suppression of reactive oxygen species and tumor necrosis factor receptor 1 (TNFR1): key role of quercetin in cancer prevention. Tumour Biol. 36 (2015), 8913–8924.
174. [174] Dok-Go, H., Lee, K.H., Kim, H.J., Lee, E.H., Lee, J., Song, Y.S., Lee, Y.H., Jin, C., Lee, Y.S., Cho, J., Neuroprotective effects of antioxidative flavonoids, quercetin, (+)-dihydroquercetin and quercetin 3-methyl ether, isolated from Opuntia ficus-indica var. saboten. Brain Res. 965 (2003), 130–136.
175. [175] Russo, M., Palumbo, R., Mupo, A., Tosto, M., Iacomino, G., Scognamiglio, A., Tedesco, I., Galano, G., Russo, G.L., Flavonoid quercetin sensitizes a CD95-resistant cell line to apoptosis by activating protein kinase C alpha. Oncogene 22 (2003), 3330–3342.
176. [176] Kandere-Grzybowska, K., Kempuraj, D., Cao, J., Cetrulo, C.L., Theoharides, T.C., Regulation of IL-1-induced selective IL-6 release from human mast cells and inhibition by quercetin. Br. J. Pharmacol. 148 (2006), 208–215.
177. [177] Pignatelli, P., Di Santo, S., Buchetti, B., Sanguigni, V., Brunelli, A., Violi, F., Polyphenols enhance platelet nitric oxide by inhibiting protein kinase C-dependent NADPH oxidase activation: effect on platelet recruitment. FASEB J. 20 (2006), 1082–1089.
178. [178] Larrosa, M., Garcia-Conesa, M.T., Espin, J.C., Tomas-Barberan, F.A., Ellagitannins, ellagic acid and vascular health. Mol. Asp. Med. 31 (2010), 513–539.
179. [179] Xiao, H.T., Tsang, S.W., Qin, H.Y., Choi, F.F., Yang, Z.J., Han, Q.B., Chen, H.B., Xu, H.X., Sheng, H., Lu, A.P., Bian, Z.X., A bioactivity-guided study on the anti-diarrheal activity of Polygonum chinense Linn. J. Ethnopharmacol. 149 (2013), 499–505.
180. [180] Rani, P.U., Kesavan, R., Ganugula, R., T, A., Kumar, P.U., Reddy, G.B., Dixit, M., Ellagic acid inhibits PDGF-BB-induced vascular smooth muscle cell proliferation and prevents atheroma formation in streptozotocin-induced diabetic rats. J. Nutr. Biochem. 24 (2013), 1830–1839.
181. [181] Chung, Y.C., Lu, L.C., Tsai, M.H., Chen, Y.J., Chen, Y.Y., Yao, S.P., Hsu, C.P., The inhibitory effect of ellagic acid on cell growth of ovarian carcinoma cells. Evid. Based Complement. Alternat. Med., 2013, 2013, 306705.
182. [182] Qiu, Z., Zhou, B., Jin, L., Yu, H., Liu, L., Liu, Y., Qin, C., Xie, S., Zhu, F., In vitro antioxidant and antiproliferative effects of ellagic acid and its colonic metabolite, urolithins, on human bladder cancer T24 cells. Food Chem. Toxicol. 59C (2013), 428–437.
183. [183] Mo, J., Panichayupakaranant, P., Kaewnopparat, N., Songkro, S., Reanmongkol, W., Topical anti-inflammatory potential of standardized pomegranate rind extract and ellagic acid in contact dermatitis. Phytother. Res. 28 (2014), 629–632.
184. [184] Chang, Y., Chen, W.F., Lin, K.H., Hsieh, C.Y., Chou, D.S., Lin, L.J., Sheu, J.R., Chang, C.C., Novel bioactivity of ellagic acid in inhibiting human platelet activation. Evid. Based Complement. Alternat. Med., 2013, 2013, 595128.
185. [185] Mishra, S., Vinayak, M., Ellagic acid checks lymphoma promotion via regulation of PKC signaling pathway. Mol. Biol. Rep. 40 (2013), 1417–1428.
186. [186] Mishra, S., Vinayak, M., Ellagic acid inhibits PKC signaling by improving antioxidant defense system in murine T cell lymphoma. Mol. Biol. Rep. 41 (2014), 4187–4197.
187. [187] Mishra, S., Vinayak, M., Role of ellagic acid in regulation of apoptosis by modulating novel and atypical PKC in lymphoma bearing mice. BMC Complement. Altern. Med., 15, 2015, 281.
188. [188] Gamaro, G.D., Suyenaga, E., Borsoi, M., Lermen, J., Pereira, P., Ardenghi, P., Effect of rosmarinic and caffeic acids on inflammatory and nociception process in rats. ISRN Pharmacol., 2011, 2011, 451682.
189. [189] Takeda, H., Tsuji, M., Inazu, M., Egashira, T., Matsumiya, T., Rosmarinic acid and caffeic acid produce antidepressive-like effect in the forced swimming test in mice. Eur. J. Pharmacol. 449 (2002), 261–267.
190. [190] Nardini, M., Scaccini, C., Packer, L., Virgili, F., In vitro inhibition of the activity of phosphorylase kinase, protein kinase C and protein kinase A by caffeic acid and a procyanidin-rich pine bark (Pinus marittima) extract. Biochim. Biophys. Acta 1474 (2000), 219–225.
191. [191] Chen, J., Wei, J.H., Cai, S.F., Miao, W.S., Pan, L.W., [Study on chemical constituents of Cardiospermum halicacabum]. Zhong Yao Cai. 36 (2013), 228–230.
192. [192] Yan, X.X., Liang, Z.F., Wang, M.Y., Wang, J.R., Wang, Z.N., [Study on the chemical constituents in the fruit of Harrisonia perforata]. Zhong Yao Cai 36 (2013), 223–225.
193. [193] Vitaglione, P., Donnarumma, G., Napolitano, A., Galvano, F., Gallo, A., Scalfi, L., Fogliano, V., Protocatechuic acid is the major human metabolite of cyanidin-glucosides. J. Nutr. 137 (2007), 2043–2048.
194. [194] Kim, Y.S., Seo, H.W., Lee, M.H., Kim, D.K., Jeon, H., Cha, D.S., Protocatechuic acid extends lifespan and increases stress resistance in Caenorhabditis elegans. Arch. Pharm. Res. 37 (2014), 245–252.
195. [195] Muley, M.M., Thakare, V.N., Patil, R.R., Bafna, P.A., Naik, S.R., Amelioration of cognitive, motor and endogenous defense functions with silymarin, piracetam and protocatechuic acid in the cerebral global ischemic rat model. Life Sci. 93 (2013), 51–57.
196. [196] Lin, C.Y., Huang, C.S., Huang, C.Y., Yin, M.C., Anticoagulatory, antiinflammatory, and antioxidative effects of protocatechuic acid in diabetic mice. J. Agric. Food Chem. 57 (2009), 6661–6667.
197. [197] Szaefer, H., Kaczmarek, J., Rybczynska, M., Baer-Dubowska, W., The effect of plant phenols on the expression and activity of phorbol ester-induced PKC in mouse epidermis. Toxicol. 230 (2007), 1–10.
198. [198] Lin, C.Y., Tsai, S.J., Huang, C.S., Yin, M.C., Antiglycative effects of protocatechuic acid in the kidneys of diabetic mice. J. Agric. Food Chem. 59 (2011), 5117–5124.
199. [199] Alasalvar, C., Pelvan, E., Ozdemir, K.S., Kocadagli, T., Mogol, B.A., Pasli, A.A., Ozcan, N., Ozcelik, B., Gokmen, V., Compositional, nutritional, and functional characteristics of instant teas produced from low- and high-quality black teas. J. Agric. Food Chem., 2013.
200. [200] Lee, J.H., Park, J.H., Cho, H.S., Joo, S.W., Cho, M.H., Lee, J., Anti-biofilm activities of quercetin and tannic acid against Staphylococcus aureus. Biofouling 29 (2013), 491–499.
201. [201] Sajid, Z.I., Anwar, F., Shabir, G., Rasul, G., Alkharfy, K.M., Gilani, A.H., Antioxidant, antimicrobial properties and phenolics of different solvent extracts from bark, leaves and seeds of Pongamia pinnata (L.) Pierre. Molecules 17 (2012), 3917–3932.
202. [202] Sieniawska, E., Activities of tannins–from in vitro studies to clinical trials. Nat. Prod. Commun. 10 (2015), 1877–1884.
203. [203] Chung, K.T., Wei, C.I., Johnson, M.G., Are tannins a double-edged sword in biology and health?. Trends Food Sci. Tech. 9 (1998), 168–175.
204. [204] Kuo, M.L., Wu, W.S., Lee, K.C., Lin, J.K., Effects of tannic-acid on 12-O-tetradecanoylphorbol-13-acetate-induced protein-kinase-C activation in Nih 3t3 cells. Biochem. Pharmacol. 46 (1993), 1327–1332.
205. [205] Yang, E.B., Wei, L., Zhang, K., Chen, Y.Z., Chen, W.N., Tannic acid, a potent inhibitor of epidermal growth factor receptor tyrosine kinase. J. Biochem. 139 (2006), 495–502.
206. [206] Cloutier, M.M., Guernsey, L., Tannin inhibition of protein kinase C in airway epithelium. Lung 173 (1995), 307–319.
207. [207] Kashiwada, Y., Nonaka, G.-I., Nishioka, I., Ballas, L.M., Jiang, J.B., Janzen, W.P., Lee, K.-H., Tannins as selective inhibitors of protein kinase C. Bioorg. Med. Chem. Lett. 2 (1992), 239–244.
208. [208] Mubarak, A., Hodgson, J.M., Considine, M.J., Croft, K.D., Matthews, V.B., Supplementation of a high-fat diet with chlorogenic acid is associated with insulin resistance and hepatic lipid accumulation in mice. J. Agric. Food Chem. 61 (2013), 4371–4378.
209. [209] Jurikova, T., Sochor, J., Rop, O., Mlcek, J., Balla, S., Szekeres, L., Adam, V., Kizek, R., Polyphenolic profile and biological activity of Chinese hawthorn (Crataegus pinnatifida BUNGE) fruits. Molecules 17 (2012), 14490–14509.
210. [210] Marcason, W., What is green coffee extract?. J. Acad. Nutr. Diet., 113, 2013, 364.
211. [211] Zhao, Y., Wang, J., Ballevre, O., Luo, H., Zhang, W., Antihypertensive effects and mechanisms of chlorogenic acids. Hypertens. Res. 35 (2012), 370–374.
212. [212] Kawai, M., Hirano, T., Higa, S., Arimitsu, J., Maruta, M., Kuwahara, Y., Ohkawara, T., Hagihara, K., Yamadori, T., Shima, Y., Ogata, A., Kawase, I., Tanaka, T., Flavonoids and related compounds as anti-allergic substances. Allergol. Int. 56 (2007), 113–123.
213. [213] Vargo, M.A., Voss, O.H., Poustka, F., Cardounel, A.J., Grotewold, E., Doseff, A.I., Apigenin-induced-apoptosis is mediated by the activation of PKC delta and caspases in leukemia cells. Biochem. Pharmacol. 72 (2006), 681–692.
214. [214] Huang, Y.T., Kuo, M.L., Liu, J.Y., Huang, S.Y., Lin, J.K., Inhibitions of protein kinase C and proto-oncogene expressions in NIH 3T3 cells by apigenin. Eur. J. Cancer 32A (1996), 146–151.
215. [215] Balasubramanian, S., Zhu, L., Eckert, R.L., Apigenin inhibition of involucrin gene expression is associated with a specific reduction in phosphorylation of protein kinase Cdelta Tyr311. J. Biol. Chem. 281 (2006), 36162–36172.
216. [216] Lin, J.K., Chen, P.C., Ho, C.T., Lin-Shiau, S.Y., Inhibition of xanthine oxidase and suppression of intracellular reactive oxygen species in HL-60 cells by theaflavin-3,3′-digallate, (−)-epigallocatechin-3-gallate, and propyl gallate. J. Agric. Food Chem. 48 (2000), 2736–2743.
217. [217] Isaacs, C.E., Xu, W.M., Theaflavin-3,3′-digallate and lactic acid combinations reduce herpes simplex virus infectivity. Antimicrob. Agents Chemother. 57 (2013), 3806–3814.
218. [218] Schuck, A.G., Ausubel, M.B., Zuckerbraun, H.L., Babich, H., Theaflavin-3,3′-digallate, a component of black tea: an inducer of oxidative stress and apoptosis. Toxicol. in Vitro 22 (2008), 598–609.
219. [219] Chen, Y.C., Liang, Y.C., Lin-Shiau, S.Y., Ho, C.T., Lin, J.K., Inhibition of TPA-induced protein kinase C and transcription activator protein-1 binding activities by theaflavin-3,3′-digallate from black tea in NIH3T3 cells. J. Agric. Food Chem. 47 (1999), 1416–1421.
220. [220] Filho, A.G., Morel, A.F., Adolpho, L., Ilha, V., Giralt, E., Tarrago, T., Dalcol, I.I., Inhibitory effect of verbascoside isolated from Buddleja brasiliensis Jacq. ex Spreng on prolyl oligopeptidase activity. Phytother. Res. 26 (2012), 1472–1475.
221. [221] Gvazava, L.N., Kikoladze, V.S., Verbascoside from Verbascum phlomoides. Chem. Nat. Compd. 43 (2007), 710–711.
222. [222] Xie, J., Tan, F., Zhu, J., Yue, C., Li, Q., Separation, purification and quantification of verbascoside from Penstemon barbatus (Cav.) Roth. Food Chem. 135 (2012), 2536–2541.
223. [223] Damtoft, S., Franzyk, H., Jensen, S.R., Nielsen, B.J., Iridoids and verbascosides in Retzia. Phytochemistry 34 (1993), 239–243.
224. [224] Brandao, G.C., Kroon, E.G., Souza, D.E., Filho, J.D., Oliveira, A.B., Chemistry and antiviral activity of Arrabidaea pulchra (Bignoniaceae). Molecules 18 (2013), 9919–9932.
225. [225] Speranza, L., Franceschelli, S., Pesce, M., Reale, M., Menghini, L., Vinciguerra, I., De Lutiis, M.A., Felaco, M., Grilli, A., Antiinflammatory effects in THP-1 cells treated with verbascoside. Phytother. Res. 24 (2010), 1398–1404.
226. [226] Zhao, X.H., Yue, H.L., Li, P., Zeng, X., Zhang, G., Evaluation of the Antitumor Activity by Cdte Qds with Verbascoside. Nano, 8, 2013, 10.1142/S1793292013500318.
227. [227] Hausmann, M., Obermeier, F., Paper, D.H., Balan, K., Dunger, N., Menzel, K., Falk, W., Schoelmerich, J., Herfarth, H., Rogler, G., In vivo treatment with the herbal phenylethanoid acteoside ameliorates intestinal inflammation in dextran sulphate sodium-induced colitis. Clin. Exp. Immunol. 148 (2007), 373–381.
228. [228] Esposito, E., Dal Toso, R., Pressi, G., Bramanti, P., Meli, R., Cuzzocrea, S., Protective effect of verbascoside in activated C6 glioma cells: possible molecular mechanisms. N-S Arch. Pharmacol. 381 (2010), 93–105.
229. [229] Ahmad, M., Rizwani, G.H., Aftab, K., Ahmad, V.U., Gilani, A.H., Ahmad, S.P., Acteoside - a new antihypertensive drug. Phytother. Res. 9 (1995), 525–527.
230. [230] Herbert, J.M., Maffrand, J.P., Taoubi, K., Augereau, J.M., Fouraste, I., Gleye, J., Verbascoside isolated from Lantana camara, an inhibitor of protein kinase C. J. Nat. Prod. 54 (1991), 1595–1600.
231. [231] He, C.N., Peng, Y., Xu, L.J., Liu, Z.A., Gu, J., Zhong, A.G., Xiao, P.G., Three new oligostilbenes from the seeds of Paeonia suffruticosa. Chem. Pharm. Bull. (Tokyo) 58 (2010), 843–847.
232. [232] Yuk, H.J., Ryu, H.W., Jeong, S.H., Curtis-Long, M.J., Kim, H.J., Wang, Y., Song, Y.H., Park, K.H., Profiling of neuraminidase inhibitory polyphenols from the seeds of Paeonia lactiflora. Food Chem. Toxicol. 55 (2013), 144–149.
233. [233] Liu, W.B., Hu, L., Hu, Q., Chen, N.N., Yang, Q.S., Wang, F.F., New resveratrol oligomer derivatives from the roots of Rheum lhasaense. Molecules 18 (2013), 7093–7102.
234. [234] Wang, P., Xu, J., Wang, Q., Feng, S.X., Chen, T., Zhang, C.L., Phenylpropanoids and diphenylethene compounds from roots and rhizomes of Smilax scobinicaulis. Zhongguo Zhong Yao Za Zhi 38 (2013), 1531–1535.
235. [235] Pawlus, A.D., Sahli, R., Bisson, J., Riviere, C., Delaunay, J.C., Richard, T., Gomes, E., Bordenave, L., Waffo-Teguo, P., Merillon, J.M., Stilbenoid profiles of canes from Vitis and Muscadinia species. J. Agric. Food Chem. 61 (2013), 501–511.
236. [236] Yan, T., Wang, T., Wei, W., Jiang, N., Qin, Y.H., Tan, R.X., Ge, H.M., Polyphenolic acetylcholinesterase inhibitors from Hopea chinensis. Planta Med. 78 (2012), 1015–1019.
237. [237] Schnee, S., Queiroz, E.F., Voinesco, F., Marcourt, L., Dubuis, P.H., Wolfender, J.L., Gindro, K., Vitis vinifera canes, a new source of antifungal compounds against Plasmopara viticola, Erysiphe necator, and Botrytis cinerea. J. Agric. Food Chem. 61 (2013), 5459–5467.
238. [238] Gonzalez-Sarrias, A., Gromek, S., Niesen, D., Seeram, N.P., Henry, G.E., Resveratrol oligomers isolated from Carex species inhibit growth of human colon tumorigenic cells mediated by cell cycle arrest. J. Agric. Food Chem. 59 (2011), 8632–8638.
239. [239] Yim, N., Ha do, T., Trung, T.N., Kim, J.P., Lee, S., Na, M., Jung, H., Kim, H.S., Kim, Y.H., Bae, K., The antimicrobial activity of compounds from the leaf and stem of Vitis amurensis against two oral pathogens. Bioorg. Med. Chem. Lett. 20 (2010), 1165–1168.
240. [240] Morikawa, T., Chaipech, S., Matsuda, H., Hamao, M., Umeda, Y., Sato, H., Tamura, H., Kon'i, H., Ninomiya, K., Yoshikawa, M., Pongpiriyadacha, Y., Hayakawa, T., Muraoka, O., Antidiabetogenic oligostilbenoids and 3-ethyl-4-phenyl-3,4-dihydroisocoumarins from the bark of Shorea roxburghii. Bioorg. Med. Chem. 20 (2012), 832–840.
241. [241] Kim, J.Y., Jeong, H.Y., Lee, H.K., Kim, S., Hwang, B.Y., Bae, K., Seong, Y.H., Neuroprotection of the leaf and stem of Vitis amurensis and their active compounds against ischemic brain damage in rats and excitotoxicity in cultured neurons. Phytomedicine 19 (2012), 150–159.
242. [242] Zghonda, N., Yoshida, S., Ezaki, S., Otake, Y., Murakami, C., Mliki, A., Ghorbel, A., Miyazaki, H., ε-Viniferin is more effective than its monomer resveratrol in improving the functions of vascular endothelial cells and the heart. Biosci. Biotechnol. Biochem. 76 (2012), 954–960.
243. [243] Zhou, J., Xie, G., Yan, X., SpringerLink (online service), encyclopedia of traditional Chinese medicines - molecular structures, pharmacological activities, natural sources and applications. Isolated Compounds A–C, Vol. 1, 2011, Springer-Verlag Berlin Heidelberg, Berlin, Heidelberg.
244. [244] Kulanthaivel, P., Janzen, W.P., Ballas, L.M., Jiang, J.B., Hu, C.Q., Darges, J.W., Seldin, J.C., Cofield, D.J., Adams, L.M., Naturally-occurring protein-kinase-C inhibitors 0.2. Isolation of oligomeric stilbenes from Caragana-Sinica. Planta Med. 61 (1995), 41–44.
245. [245] Aggarwal, B.B., Kunnumakkara, A.B., ebrary Inc., Molecular targets and therapeutic uses of spices modern uses for ancient medicine. World Scientific, Singapore; Hackensack, NJ, 2009.
246. [246] Azevedo, M.F., Lima, C.F., Fernandes-Ferreira, M., Almeida, M.J., Wilson, J.M., Pereira-Wilson, C., Rosmarinic acid, major phenolic constituent of Greek sage herbal tea, modulates rat intestinal SGLT1 levels with effects on blood glucose. Mol. Nutr. Food Res. 55:Suppl. 1 (2011), S15–S25.
247. [247] Feng, L., Jia, X., Zhu, M.M., Chen, Y., Shi, F., Antioxidant activities of total phenols of Prunella vulgaris L. in vitro and in tumor-bearing mice. Molecules 15 (2010), 9145–9156.
248. [248] Petersen, M., Simmonds, M.S., Rosmarinic acid. Phytochemistry 62 (2003), 121–125.
249. [249] Chaher, N., Arraki, K., Dillinseger, E., Temsamani, H., Bernillon, S., Pedrot, E., Delaunay, J.C., Merillon, J.M., Monti, J.P., Izard, J.C., Atmani, D., Richard, T., Bioactive stilbenes from Vitis vinifera grapevine shoots extracts. J. Sci. Food Agric. 94 (2014), 951–954.
250. [250] Jin, Q., Han, X.H., Hong, S.S., Lee, C., Choe, S., Lee, D., Kim, Y., Hong, J.T., Lee, M.K., Hwang, B.Y., Antioxidative oligostilbenes from Caragana sinica. Bioorg. Med. Chem. Lett. 22 (2012), 973–976.
251. [251] Tanaka, T., Ito, T., Iinuma, M., Ohyama, M., Ichise, M., Tateishi, Y., Stilbene oligomers in roots of Sophora davidii. Phytochemistry 53 (2000), 1009–1014.
252. [252] Lambert, C., Bisson, J., Waffo-Teguo, P., Papastamoulis, Y., Richard, T., Corio-Costet, M.F., Merillon, J.M., Cluzet, S., Phenolics and their antifungal role in grapevine wood decay: focus on the Botryosphaeriaceae Family. J. Agric. Food Chem. 60 (2012), 11859–11868.
253. [253] Barjot, C., Tournaire, M., Castagnino, C., Vigor, C., Vercauteren, J., Rossi, J.F., Evaluation of antitumor effects of two vine stalk oligomers of resveratrol on a panel of lymphoid and myeloid cell lines: comparison with resveratrol. Life Sci. 81 (2007), 1565–1574.
254. [254] Xu, G., Zhang, L.P., Chen, L.F., Hu, C.Q., Inhibition of protein kinase C by stilbenoids. Yao Xue Xue Bao 29 (1994), 818–822.
255. [255] Clements, R.T., Cordeiro, B., Feng, J., Bianchi, C., Sellke, F.W., Rottlerin increases cardiac contractile performance and coronary perfusion through BKCa ++ channel activation after cold cardioplegic arrest in isolated hearts. Circulation 124 (2011), S55–S61.
256. [256] Davies, S.P., Reddy, H., Caivano, M., Cohen, P., Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem. J. 351 (2000), 95–105.
257. [257] Liao, Y.F., Hung, Y.C., Chang, W.H., Tsay, G.J., Hour, T.C., Hung, H.C., Liu, G.Y., The PKC delta inhibitor, rottlerin, induces apoptosis of haematopoietic cell lines through mitochondrial membrane depolarization and caspases' cascade. Life Sci. 77 (2005), 707–719.
258. [258] Soltoff, S.P., Rottlerin: an inappropriate and ineffective inhibitor of PKCdelta. Trends Pharmacol. Sci. 28 (2007), 453–458.
259. [259] Kern, M., Pahlke, G., Balavenkatraman, K.K., Bohmer, F.D., Marko, D., Apple polyphenols affect protein kinase C activity and the onset of apoptosis in human colon carcinoma cells. J. Agric. Food Chem. 55 (2007), 4999–5006.
260. [260] Zimmermann, M.L., Sneden, A.T., Vanicosides A and B, protein kinase C inhibitors from Polygonum pensylvanicum. J. Nat. Prod. 57 (1994), 236–242.
261. [261] Mizumaki, Y., Kurimoto, M., Hirashima, Y., Nishijima, M., Kamiyama, H., Nagai, S., Takaku, A., Sugihara, K., Shimizu, M., Endo, S., Lipophilic fraction of Panax ginseng induces neuronal differentiation of PC12 cells and promotes neuronal survival of rat cortical neurons by protein kinase C dependent manner. Brain Res. 950 (2002), 254–260.
262. [262] Scoditti, E., Nestola, A., Massaro, M., Calabriso, N., Storelli, C., De Caterina, R., Carluccio, M.A., Hydroxytyrosol suppresses MMP-9 and COX-2 activity and expression in activated human monocytes via PKCalpha and PKCbeta1 inhibition. Atherosclerosis 232 (2014), 17–24.
263. [263] Kumar, G., Dange, P., Kailaje, V., Vaidya, M.M., Ramchandani, A.G., Maru, G.B., Polymeric black tea polyphenols modulate the localization and activity of 12-O-tetradecanoylphorbol-13-acetate-mediated kinases in mouse skin: mechanisms of their anti-tumor-promoting action. Free Rad. Biol. Med. 53 (2012), 1358–1370.
264. [264] Liu, X., Wang, Z., Wang, P., Yu, B., Liu, Y., Xue, Y., Green tea polyphenols alleviate early BBB damage during experimental focal cerebral ischemia through regulating tight junctions and PKCalpha signaling. BMC Complement. Altern. Med., 13, 2013, 187.
265. [265] Newman, D.J., Cragg, G.M., Natural products as sources of new drugs over the last 25 years. J. Nat. Prod. 70 (2007), 461–477.
266. [266] Tuorkey, M.J., Curcumin a potent cancer preventive agent: mechanisms of cancer cell killing. Interv. Med. Appl. Sci. 6 (2014), 139–146.
267. [267] Varoni, E.M., Lo Faro, A.F., Sharifi-Rad, J., Iriti, M., Anticancer molecular mechanisms of resveratrol. Front. Nutr., 3, 2016, 8.
268. [268] Kulkarni, S.S., Canto, C., The molecular targets of resveratrol. Biochim. Biophys. Acta 1852 (2015), 1114–1123.
269. [269] Singh, B.N., Shankar, S., Srivastava, R.K., Green tea catechin, epigallocatechin-3-gallate (EGCG): mechanisms, perspectives and clinical applications. Biochem. Pharmacol. 82 (2011), 1807–1821.
270. [270] Prasad, S., Tyagi, A.K., Aggarwal, B.B., Recent developments in delivery, bioavailability, absorption and metabolism of curcumin: the golden pigment from golden spice. Cancer Res. Treat. 46 (2014), 2–18.
271. [271] Gambini, J., Ingles, M., Olaso, G., Lopez-Grueso, R., Bonet-Costa, V., Gimeno-Mallench, L., Mas-Bargues, C., Abdelaziz, K.M., Gomez-Cabrera, M.C., Vina, J., Borras, C., Properties of resveratrol: in vitro and in vivo studies about metabolism, bioavailability, and biological effects in animal models and humans. Oxidative Med. Cell. Longev., 2015, 2015, 837042.
272. [272] Walle, T., Bioavailability of resveratrol. Ann. N. Y. Acad. Sci. 1215 (2011), 9–15.
273. [273] Mereles, D., Hunstein, W., Epigallocatechin-3-gallate (EGCG) for clinical trials: more pitfalls than promises?. Int. J. Mol. Sci. 12 (2011), 5592–5603.
274. [274] Wang, J., Bi, W., Cheng, A., Freire, D., Vempati, P., Zhao, W., Gong, B., Janle, E.M., Chen, T.Y., Ferruzzi, M.G., Schmeidler, J., Ho, L., Pasinetti, G.M., Targeting multiple pathogenic mechanisms with polyphenols for the treatment of Alzheimer's disease-experimental approach and therapeutic implications. Front. Aging Neurosci., 6, 2014, 42.
275. [275] Pandareesh, M.D., Mythri, R.B., Srinivas Bharath, M.M., Bioavailability of dietary polyphenols: factors contributing to their clinical application in CNS diseases. Neurochem. Int. 89 (2015), 198–208.
276. [276] Aras, A., Khokhar, A.R., Qureshi, M.Z., Silva, M.F., Sobczak-Kupiec, A., Pineda, E.A., Hechenleitner, A.A., Farooqi, A.A., Targeting cancer with nano-bullets: curcumin, EGCG, resveratrol and quercetin on flying carpets. Asian Pac. J. Cancer Prev. 15 (2014), 3865–3871.