Curcumin, mitochondrial biogenesis, and mitophagy: Exploring recent data and indicating future needs

Biotechnology Advances

Volumn 34, Issue 5, 2016, Pages 813-826

  de Oliveira, Marcos Roberto ^a   Jardim, Fernanda Rafaela ^b   Setzer, William N ^c   Nabavi, Seyed Mohammad ^d   Nabavi, Seyed Fazel ^d  

^a FEDERAL UNIVERSITY OF MATO GROSSO   (Brazil)

^b Postmortem Toxicology Sector   (Brazil)

^c University of Alabama in Huntsville   (United States)

^d BAQIYATALLAH UNIVERSITY OF MEDICAL SCIENCES   (Iran)

Author keywords

Curcumin; Mitochondria; Mitochondrial biogenesis; Mitophagy

Indexed keywords

BIOCHEMISTRY; BIOSYNTHESIS; CELL DEATH; NEURODEGENERATIVE DISEASES; POLYPHENOLIC COMPOUNDS;

CELLULAR FUNCTION; CELLULAR STRESS RESPONSE; CURCUMIN; GROWING BODIES; MITOCHONDRIAL BIOGENESIS; MITOCHONDRIAL DYSFUNCTION; MITOPHAGY; SCIENTIFIC EVIDENCE;

MITOCHONDRIA;

APOPTOSIS; BIOAVAILABILITY; DISEASE TREATMENT; METABOLISM; MITOCHONDRION; NERVOUS SYSTEM DISORDER; PHENOLIC COMPOUND; SECONDARY METABOLITE;

CURCUMA LONGA;

CURCUMIN;

ANIMAL; CELL LINE; CHEMISTRY; DRUG EFFECTS; HUMAN; METABOLISM; MITOCHONDRION; MITOPHAGY; MOUSE; ORGANELLE BIOGENESIS; PHYSIOLOGY;

ANIMALS; CELL LINE; CURCUMIN; HUMANS; MICE; MITOCHONDRIA; MITOCHONDRIAL DEGRADATION; ORGANELLE BIOGENESIS;

EID: 84966539976     PISSN: 07349750     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biotechadv.2016.04.004     Document Type: Review

References (239)

1. Adams, B.K., Cai, J., Armstrong, J., Herold, M., Lu, Y.J., Sun, A., EF24, a novel synthetic curcumin analog, induces apoptosis in cancer cells via a redox-dependent mechanism. Anti-Cancer Drugs 16 (2005), 263–275.
2. Aggarwal, B., Bhatt, I., Ichikawa, H., Ahn, K., Sethi, G., Sandur, S., Curcumin—Biological and Medicinal Properties. Turmeric: The Genus Curcuma. 45, 2007, CRC Press, New York, 297–368.
3. Agnihotri, N., Mishra, P., Scavenging mechanism of curcumin toward the hydroxyl radical: a theoretical study of reactions producing ferulic acid and vanillin. J. Phys. Chem. A 115 (2011), 14221–14232.
4. Ahmed, T., Pathak, R., Mustafa, M., Kar, R., Tripathi, A.K., Ahmed, R.S., Ameliorating effect of N-acetylcysteine and curcumin on pesticide-induced oxidative DNA damage in human peripheral blood mononuclear cells. Environ. Monit. Assess. 179 (2011), 293–299.
5. Ak, T., Gülçin, İ., Antioxidant and radical scavenging properties of curcumin. Chem. Biol. Interact. 174 (2008), 27–37.
6. Alam, S., Panda, J.J., Chauhan, V.S., Novel dipeptide nanoparticles for effective curcumin delivery. Int. J. Nanomedicine 7 (2012), 4207–4222.
7. Amorati, R., Menichetti, S., Mileo, E., Pedulli, G.F., Viglianisi, C., Hydrogen‐atom transfer reactions from ortho‐alkoxy‐substituted phenols: an experimental approach. Chemistry 15 (2009), 4402–4410.
8. Anand, P., Thomas, S.G., Kunnumakkara, A.B., Sundaram, C., Harikumar, K.B., Sung, B., Biological activities of curcumin and its analogues (Congeners) made by man and mother nature. Biochem. Pharmacol. 76 (2008), 1590–1611.
9. Anderson, R., Prolla, T., PGC-1alpha in aging and anti-aging interventions. Biochim. Biophys. Acta 1790 (2009), 1059–1066.
10. Andreux, P.A., Houtkooper, R.H., Auwerx, J., Pharmacological approaches to restore mitochondrial function. Nat. Rev. Drug Discov. 12 (2013), 465–483.
11. Angelo, L.S., Kurzrock, R., Turmeric and green tea: a recipe for the treatment of B-chronic lymphocytic leukemia. Clin. Cancer Res. 15 (2009), 1123–1125.
12. Arun, N., Nalini, N., Efficacy of turmeric on blood sugar and polyol pathway in diabetic albino rats. Plant Foods Hum. Nutr. 57 (2002), 41–52.
13. Babu, P.S., Srinivasan, K., Influence of dietary curcumin and cholesterol on the progression of experimentally induced diabetes in albino rat. Mol. Cell. Biochem. 152 (1995), 13–21.
14. Bakhshi, J., Weinstein, L., Poksay, K.S., Nishinaga, B., Bredesen, D.E., Rao, R.V., Coupling endoplasmic reticulum stress to the cell death program in mouse melanoma cells: effect of curcumin. Apoptosis 13 (2008), 904–914.
15. Balasubramanian, K., Molecular orbital basis for yellow curry spice curcumin's prevention of Alzheimer's disease. J. Agric. Food Chem. 54 (2006), 3512–3520.
16. Ballinger, S.W., Mitochondrial dysfunction in cardiovascular disease. Free Radic. Biol. Med. 38 (2005), 1278–1295.
17. Banji, O.J., Banji, D., Ch, K., Curcumin and hesperidin improve cognition by suppressing mitochondrial dysfunction and apoptosis induced by D-galactose in rat brain. Food Chem. Toxicol. 74 (2014), 51–59.
18. Barik, A., Mishra, B., Shen, L., Mohan, H., Kadam, R., Dutta, S., Evaluation of a new copper (II)–curcumin complex as superoxide dismutase mimic and its free radical reactions. Free Radic. Biol. Med. 39 (2005), 811–822.
19. Basnet, P., Skalko-Basnet, N., Curcumin: an anti-inflammatory molecule from a curry spice on the path to cancer treatment. Molecules 16 (2011), 4567–4598.
20. Baum, L., Lam, C.W.K., Cheung, S.K.K., Kwok, T., Lui, V., Tsoh, J., Six-month randomized, placebo-controlled, double-blind, pilot clinical trial of curcumin in patients with Alzheimer disease. J. Clin. Psychopharmacol. 28 (2008), 110–113.
21. Benassi, R., Ferrari, E., Lazzari, S., Spagnolo, F., Saladini, M., Theoretical study on curcumin: a comparison of calculated spectroscopic properties with NMR, UV–vis and IR experimental data. J. Mol. Struct. 892 (2008), 168–176.
22. Bernabé-Pineda, M., Ramı́rez-Silva, M.T., Romero-Romo, M.A., González-Vergara, E., Rojas-Hernández, A., Spectrophotometric and electrochemical determination of the formation constants of the complexes Curcumin–Fe (III)–water and Curcumin–Fe (II)–water. Spectrochim. Acta A Mol. Biomol. Spectrosc. 60 (2004), 1105–1113.
23. Bhullar, K.S., Jha, A., Rupasinghe, H.V., Novel carbocyclic curcumin analog CUR3d modulates genes involved in multiple apoptosis pathways in human hepatocellular carcinoma cells. Chem. Biol. Interact. 242 (2015), 107–122.
24. Bisht, S., Feldmann, G., Soni, S., Ravi, R., Karikar, C., Maitra, A., Polymeric nanoparticle-encapsulated curcumin (“nanocurcumin”): a novel strategy for human cancer therapy. J. Nanobiotechnol. 5 (2007), 1–18.
25. Boengler, K., Heusch, G., Schulz, R., Nuclear-encoded mitochondrial proteins and their role in cardioprotection. Biochim. Biophys. Acta (BBA)-Mol. Cell Res. 1813 (2011), 1286–1294.
26. Borsari, M., Ferrari, E., Grandi, R., Saladini, M., Curcuminoids as potential new iron-chelating agents: spectroscopic, polarographic and potentiometric study on their Fe (III) complexing ability. Inorg. Chim. Acta 328 (2002), 61–68.
27. Bruzell, E.M., Morisbak, E., Tønnesen, H.H., Studies on curcumin and curcuminoids. XXIX. Photoinduced cytotoxicity of curcumin in selected aqueous preparations. Photochem. Photobiol. Sci. 4 (2005), 523–530.
28. Burgos‐Morón, E., Calderón‐Montaño, J.M., Salvador, J., Robles, A., López‐Lázaro, M., The dark side of curcumin. Int. J. Cancer 126 (2010), 1771–1775.
29. Cadenas, E., Mitochondrial free radical production and cell signaling. Mol. Asp. Med. 25 (2004), 17–26.
30. Cantó, C., Gerhart-Hines, Z., Feige, J.N., Lagouge, M., Noriega, L., Milne, J.C., Elliott, P.J., Puigserver, P., Auwerx, J., AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity. Nature 458 (2009), 1056–1060.
31. Canugovi, C., Maynard, S., Bayne, A.C., Sykora, P., Tian, J., de Souza-Pinto, N.C., Croteau, D.L., Bohr, V.A., The mitochondrial transcription factor A functions in mitochondrial base excision repair. DNA Repair (Amst) 9 (2010), 1080–1089.
32. Chai, H., Yan, S., Lin, P., Lumsden, A.B., Yao, Q., Chen, C., Curcumin blocks HIV protease inhibitor ritonavir-induced vascular dysfunction in porcine coronary arteries. J. Am. Coll. Surg. 200 (2005), 820–830.
33. Chan, W.H., Wu, C.C., Yu, J.S., Curcumin inhibits UV irradiation‐induced oxidative stress and apoptotic biochemical changes in human epidermoid carcinoma A431 cells. J. Cell. Biochem. 90 (2003), 327–338.
34. Chattopadhyay, I., Biswas, K., Bandyopadhyay, U., Banerjee, R.K., Turmeric and curcumin: Biological actions and medicinal applications. Curr. Sci. 87 (2004), 44–53.
35. Chen, H.W., Huang, H.C., Effect of curcumin on cell cycle progression and apoptosis in vascular smooth muscle cells. Br. J. Pharmacol. 124 (1998), 1029–1040.
36. Chen, Q., Vazquez, E.J., Moghaddas, S., Hoppel, C.L., Lesnefsky, E.J., Production of reactive oxygen species by mitochondria central role of complex III. J. Biol. Chem. 278 (2003), 36027–36031.
37. Chen, D.Y., Shien, J.H., Tiley, L., Chiou, S.S., Wang, S.Y., Chang, T.J., Curcumin inhibits influenza virus infection and haemagglutination activity. Food Chem. 119 (2010), 1346–1351.
38. Chen, S.D., Yang, D.I., Lin, T.K., Shaw, F.Z., Liou, C.W., Chuang, Y.C., Roles of oxidative stress, apoptosis, PGC-1α and mitochondrial biogenesis in cerebral ischemia. Int. J. Mol. Sci. 12 (2011), 7199–7215.
39. Chin, L.S., Li, L., Ubiquitin phosphorylation in Parkinson's disease: Implications for pathogenesis and treatment. Transl. Neurodegener., 5, 2016, 1.
40. Civenni, G., Iodice, M., Nabavi, S.F., Habtemariam, S., Nabavi, S.M., Catapano, C., Gallic acid and methyl-3-O-methyl gallate: a comparative study on their effects on prostate cancer stem cells. RSC Adv., 5, 2015 (63800-62806).
41. Conteas, C.N., Panossian, A.M., Tran, T.T., Singh, H.M., Treatment of HIV-associated diarrhea with curcumin. Dig. Dis. Sci. 54 (2009), 2188–2191.
42. Contreras, L., Drago, I., Zampese, E., Pozzan, T., 2010. Mitochondria: the calcium connection. Biochim. Biophys. Acta Bioenerg. 1797, 607–718.
43. Cooper, G.M., Hausman, R.E., The Cells, Mitochondria. 2000, ASM Press, Wahington DC.
44. Coste, A., Louet, J.F., Lagouge, M., Lerin, C., Antal, M.C., Meziane, H., Schoonjans, K., Puigserver, P., O'Malley, B.W., Auwerx, J., The genetic ablation of SRC-3 protects against obesity and improves insulin sensitivity by reducing the acetylation of PGC-1{alpha}. Proc. Natl. Acad. Sci. U. S. A. 105 (2008), 17187–17192.
45. Dahl, T.A., McGowan, W.M., Shand, M.A., Srinivasan, V.S., Photokilling of bacteria by the natural dye curcumin. Arch. Microbiol. 151 (1989), 183–185.
46. Dahll, T.A., Bilski, P., Reszka, K.J., Chignell, C.F., Photocytotoxicity of curcumin. Photochem. Photobiol. 59 (1994), 290–294.
47. Dance-Barnes, S.T., Kock, N.D., Moore, J.E., Lin, E.Y., Mosley, L.J., D'Agostino, R.B., Lung tumor promotion by curcumin. Carcinogenesis 30 (2009), 1016–1023.
48. de Oliveira, M.R., Nabavi, S.F., Habtemariam, S., Orhan, I.E., Daglia, M., Nabavi, S.M., The effects of baicalein and baicalin on mitochondrial function and dynamics: a review. Pharmacol. Res. 100 (2015), 296–308.
49. de Oliveira, M.R., Nabavi, S.M., Braidy, N., Setzer, W.N., Ahmed, T., Nabavi, S.F., Quercetin and the mitochondria: a mechanistic view. Biotechnol. Adv., 2015, 10.1016/j.biotechadv.2015.12.014.
50. de Oliveira, M.R., Nabavi, S.F., Daglia, M., Rastrelli, L., Nabavi, S.M., Epigallocatechin gallate and mitochondria—a story of life and death. Pharmacol. Res. 104 (2016), 70–85.
51. de Oliveira, M.R., Nabavi, S.F., Manayi, A., Daglia, M., Hajheydari, Z., Nabavi, S.M., Resveratrol and the mitochondria: From triggering the intrinsic apoptotic pathway to inducing mitochondrial biogenesis, a mechanistic view. Biochim. Biophys. Acta Gen. Subj. 1860 (2016), 727–745.
52. Deas, E., Wood, N.W., Plun-Favreau, H., Mitophagy and Parkinson's disease: the PINK1-parkin link. Biochim. Biophys. Acta 1813 (2011), 623–633.
53. Desagher, S., Martinou, J.C., Mitochondria as the central control point of apoptosis. Trends Cell Biol. 10 (2000), 369–377.
54. Di Lorenzo, A., Nabavi, S.F., Sureda, A., Moghaddam, A.H., Khanjani, S., Arcidiaco, P., Antidepressive‐like effects and antioxidant activity of green tea and GABA green tea in a mouse model of post‐stroke depression. Mol. Nutr. Food Res., 2015, 10.1002/mnfr.201500567.
55. Di Mauro, S., Schon, E.A., Mitochondrial disorders in the nervous system. Annu. Rev. Neurosci. 31 (2008), 91–123.
56. Dorn, G.W. 2nd, Vega, R.B., Kelly, D.P., Mitochondrial biogenesis and dynamics in the developing and diseased heart. Genes Dev. 29 (2015), 1981–1991.
57. Durcan, T.M., Fon, E.A., The three ‘P's of mitophagy: PARKIN, PINK1, and post-translational modifications. Genes Dev. 29 (2015), 989–999.
58. Duvoix, A., Blasius, R., Delhalle, S., Schnekenburger, M., Morceau, F., Henry, E., Chemopreventive and therapeutic effects of curcumin. Cancer Lett. 223 (2005), 181–190.
59. Egan, M.E., Pearson, M., Weiner, S.A., Rajendran, V., Rubin, D., Glöckner-Pagel, J., Curcumin, a major constituent of turmeric, corrects cystic fibrosis defects. Science 304 (2004), 600–602.
60. Ekstrand, M.I., Falkenberg, M., Rantanen, A., Park, C.B., Gaspari, M., Hultenby, K., Rustin, P., Gustafsson, C.M., Larsson, N.G., Mitochondrial transcription factor A regulates mtDNA copy number in mammals. Hum. Mol. Genet. 13 (2004), 935–944.
61. El-Agamy, D.S., Comparative effects of curcumin and resveratrol on aflatoxin B1-induced liver injury in rats. Arch. Toxicol. 84 (2010), 389–396.
62. Fato, R., Bergamini, C., Leoni, S., Lenaz, G., Mitochondrial production of reactive oxygen species: role of complex I and quinone analogues. Biofactors 32 (2008), 31–39.
63. Feng, J.Y., Liu, Z.Q., Phenolic and enolic hydroxyl groups in curcumin: which plays the major role in scavenging radicals?. J. Agric. Food Chem. 57 (2009), 11041–11046.
64. Fisher, R.P., Clayton, D.A., Purification and characterization of human mitochondrial transcription factor 1. Mol. Cell. Biol. 8 (1988), 3496–3509.
65. Gali-Muhtasib, H., Hmadi, R., Kareh, M., Tohme, R., Darwiche, N., Cell death mechanisms of plant-derived anticancer drugs: beyond apoptosis. Apoptosis 20 (2015), 1531–1562.
66. Ganiger, S., Malleshappa, H., Krishnappa, H., Rajashekhar, G., Rao, V.R., Sullivan, F., A two generation reproductive toxicity study with curcumin, turmeric yellow, in Wistar rats. Food Chem. Toxicol. 45 (2007), 64–69.
67. Gao, M., Liu, L., Zhang, P., Yu, G., Li, Y., Neuroprotective effect of curcumin involved in increasing the protein levels of UCP2 and inhibiting oxidative stress induced by chronic cerebral ischemia in vitro. Mol. Neurodegener., 7, 2012, S26.
68. Gerhart-Hines, Z., Rodgers, J.T., Bare, O., Lerin, C., Kim, S.H., Mostoslavsky, R., Alt, F.W., Wu, Z., Puigserver, P., Metabolic control of muscle mitochondrial function and fatty acid oxidation through SIRT1/PGC-1alpha. EMBO J. 26 (2007), 1913–1923.
69. Gordon, O.N., Schneider, C., Vanillin and ferulic acid are not the major degradation products of curcumin. Trends Mol. Med. 18 (2012), 361–363.
70. Green, D.R., Galluzzi, L., Kroemer, G., Mitochondria and the autophagy–inflammation–cell death axis in organismal aging. Science 333 (2011), 1109–1112.
71. Gunaydın, M., Guzel, A., Guzel, A., Alacam, H., Salis, O., Murat, N., The effect of curcumin on lung injuries in a rat model induced by aspirating gastrointestinal decontamination agents. J. Pediatr. Surg. 47 (2012), 1669–1676.
72. Gupta, S.C., Kismali, G., Aggarwal, B.B., Curcumin, a component of turmeric: from farm to pharmacy. Biofactors 39 (2013), 2–13.
73. Gurd, B.J., 2011. Deacetylation of PGC-1α by SIRT1: importance for skeletal muscle function and exercise-induced mitochondrial biogenesis. Appl. Physiol. Nutr. Metab. 36, 589–597.
74. Hamidie, R.D.R., Yamada, T., Ishizawa, R., Saito, Y., Masuda, K., Curcumin treatment enhances the effect of exercise on mitochondrial biogenesis in skeletal muscle by increasing cAMP levels. Metabolism 64 (2015), 1334–1347.
75. Handschin, C., Spiegelman, B.M., Peroxisome proliferator-activated receptor gamma coactivator 1 coactivators, energy homeostasis, and metabolism. Endocr. Rev. 27 (2006), 728–735.
76. Hassaninasab, A., Hashimoto, Y., Tomita-Yokotani, K., Kobayashi, M., Discovery of the curcumin metabolic pathway involving a unique enzyme in an intestinal microorganism. Proc. Natl. Acad. Sci. 108 (2011), 6615–6620.
77. He, X., Li, Q., Liu, X., Wu, G., Zhai, G., Curcumin-loaded lipid cubic liquid crystalline nanoparticles: preparation, optimization, physicochemical properties and oral absorption. J. Nanosci. Nanotechnol. 15 (2015), 5559–5565.
78. Hoehle, S.I., Pfeiffer, E., Metzler, M., Glucuronidation of curcuminoids by human microsomal and recombinant UDP‐glucuronosyltransferases. Mol. Nutr. Food Res. 51 (2007), 932–938.
79. Holder, G.M., Plummer, J.L., Ryan, A.J., The metabolism and excretion of curcumin (1, 7-bis-(4-hydroxy-3-methoxyphenyl)-1, 6-heptadiene-3, 5-dione) in the rat. Xenobiotica 8 (1978), 761–768.
80. Holt, P.R., Katz, S., Kirshoff, R., Curcumin therapy in inflammatory bowel disease: a pilot study. Dig. Dis. Sci. 50 (2005), 2191–2193.
81. Hong, J., Bose, M., Ju, J., Ryu, J.H., Chen, X., Sang, S., Modulation of arachidonic acid metabolism by curcumin and related β-diketone derivatives: effects on cytosolic phospholipase A2, cyclooxygenases and 5-lipoxygenase. Carcinogenesis 25 (2004), 1671–1679.
82. Hosseinzadehdehkordi, M., Adelinik, A., Tashakor, A., Dual effect of curcumin targets reactive oxygen species, adenosine triphosphate contents and intermediate steps of mitochondria-mediated apoptosis in lung cancer cell lines. Eur. J. Pharmacol. 769 (2015), 203–210.
83. Hroudová, J., Singh, N., Fišar, Z., Mitochondrial dysfunctions in neurodegenerative diseases: relevance to Alzheimer's disease. Biomed. Res. Int., 2014, 2014, 175062.
84. Huang, M.T., Wang, Z., Georgiadis, C., Laskin, J., Conney, A., Inhibitory effects of curcumin on tumor initiation by benzo [a] pyrene and 7, 12-dimethylbenz [a] anthracene. Carcinogenesis 13 (1992), 2183–2186.
85. Im Kim, H., Huang, H., Cheepala, S., Huang, S., Chung, J., Curcumin inhibition of integrin (α6β4)-dependent breast cancer cell motility and invasion. Cancer Prev. Res. 1 (2008), 385–391.
86. Ireson, C.R., Jones, D.J., Orr, S., Coughtrie, M.W., Boocock, D.J., Williams, M.L., Metabolism of the cancer chemopreventive agent curcumin in human and rat intestine. Cancer Epidemiol. Biomark. Prev. 11 (2002), 105–111.
87. Irwin, M.H., Moos, W.H., Faller, D.V., Steliou, K., Pinkert, C.A., Epigenetic treatment of neurodegenerative disorders: Alzheimer and Parkinson diseases. Drug Dev. Res., 2016, 10.1002/ddr.21294.
88. Itoh, K., Nakamura, K., Iijima, M., Sesaki, H., Mitochondrial dynamics in neurodegeneration. Trends Cell Biol. 23 (2013), 64–71.
89. Jang, D.J., Kim, S.T., Oh, E., Lee, K., Enhanced oral bioavailability and antiasthmatic efficacy of curcumin using redispersible dry emulsion. Biomed. Mater. Eng. 24 (2013), 917–930.
90. Jiao, Y., Wilkinson, J., Pietsch, E.C., Buss, J.L., Wang, W., Planalp, R., Iron chelation in the biological activity of curcumin. Free Radic. Biol. Med. 40 (2006), 1152–1160.
91. Johnson, J.J., Mukhtar, H., Curcumin for chemoprevention of colon cancer. Cancer Lett. 255 (2007), 170–181.
92. Jovanovic, S.V., Steenken, S., Boone, C.W., Simic, M.G., H-atom transfer is a preferred antioxidant mechanism of curcumin. J. Am. Chem. Soc. 121 (1999), 9677–9681.
93. Kamalakkannan, N., Rukkumani, R., Varma, P.S., Viswanathan, P., Rajasekharan, K.N., Menon, V.P., Comparative effects of curcumin and an analogue of curcumin in carbon tetrachloride‐induced hepatotoxicity in rats. Basic Clin. Pharmacol. Toxicol. 97 (2005), 15–21.
94. Kang, Q., Chen, A., Curcumin suppresses expression of low‐density lipoprotein (LDL) receptor, leading to the inhibition of LDL‐induced activation of hepatic stellate cells. Br. J. Pharmacol. 157 (2009), 1354–1367.
95. Kasahara, A., Scorrano, L., Mitochondria: from cell death executioners to regulators of cell differentiation. Trends Cell Biol. 24 (2014), 761–770.
96. Katsuyama, Y., Kita, T., Funa, N., Horinouchi, S., Curcuminoid biosynthesis by two type III polyketide synthases in the herb Curcuma longa. J. Biol. Chem. 284 (2009), 11160–11170.
97. Katsuyama, Y., Kita, T., Horinouchi, S., Identification and characterization of multiple curcumin synthases from the herb Curcuma longa. FEBS Lett. 583 (2009), 2799–2803.
98. Kennedy, D.O., Wightman, E.L., Herbal extracts and phytochemicals: plant secondary metabolites and the enhancement of human brain function. Adv. Nutr. 2 (2011), 32–50.
99. Khanna, D., Sethi, G., Ahn, K.S., Pandey, M.K., Kunnumakkara, A.B., Sung, B., Natural products as a gold mine for arthritis treatment. Curr. Opin. Pharmacol. 7 (2007), 344–351.
100. Khurana, A., Ho, C.T., High performance liquid chromatographic analysis of curcuminoids and their photo-oxidative decomposition compounds in Curcuma longa L. J. Liq. Chromatogr. 11 (1988), 2295–2304.
101. Kim, K., Kim, K.H., Kim, H.Y., Cho, H.K., Sakamoto, N., Cheong, J., Curcumin inhibits hepatitis C virus replication via suppressing the Akt-SREBP-1 pathway. FEBS Lett. 584 (2010), 707–712.
102. Kita, T., Imai, S., Sawada, H., Kumagai, H., Seto, H., The biosynthetic pathway of curcuminoid in turmeric (Curcuma longa) as revealed by 13C-labeled precursors. Biosci. Biotechnol. Biochem. 72 (2008), 1789–1798.
103. Koshiba, T., Mitochondrial-mediated antiviral immunity. Biochim. Biophys. Acta (BBA)-Mol. Cell Res. 1833 (2013), 225–232.
104. Kowluru, R.A., Kanwar, M., Effects of curcumin on retinal oxidative stress and inflammation in diabetes. Nutr. Metab., 4, 2007, 1.
105. Kuhad, A., Chopra, K., Curcumin attenuates diabetic encephalopathy in rats: behavioral and biochemical evidences. Eur. J. Pharmacol. 576 (2007), 34–42.
106. Kunnumakkara, A.B., Guha, S., Krishnan, S., Diagaradjane, P., Gelovani, J., Aggarwal, B.B., Curcumin potentiates antitumor activity of gemcitabine in an orthotopic model of pancreatic cancer through suppression of proliferation, angiogenesis, and inhibition of nuclear factor-κB–regulated gene products. Cancer Res. 67 (2007), 3853–3861.
107. Kunnumakkara, A.B., Anand, P., Aggarwal, B.B., Curcumin inhibits proliferation, invasion, angiogenesis and metastasis of different cancers through interaction with multiple cell signaling proteins. Cancer Lett. 269 (2008), 199–225.
108. Kurd, S.K., Smith, N., VanVoorhees, A., Troxel, A.B., Badmaev, V., Seykora, J.T., Oral curcumin in the treatment of moderate to severe psoriasis vulgaris: a prospective clinical trial. J. Am. Acad. Dermatol. 58 (2008), 625–631.
109. Kutluay, S.B., Doroghazi, J., Roemer, M.E., Triezenberg, S.J., Curcumin inhibits herpes simplex virus immediate-early gene expression by a mechanism independent of p300/CBP histone acetyltransferase activity. Virology 373 (2008), 239–247.
110. Lane, N., Mitochondrial disease: powerhouse of disease. Nature 440 (2006), 600–602.
111. Lee, K.S., Lee, B.S., Semnani, S., Avanesian, A., Um, C.Y., Jeon, H.J., Curcumin extends life span, improves health span, and modulates the expression of age-associated aging genes in Drosophila melanogaster. Rejuvenation Res. 13 (2010), 561–570.
112. Lim, G.P., Chu, T., Yang, F., Beech, W., Frautschy, S.A., Cole, G.M., The curry spice curcumin reduces oxidative damage and amyloid pathology in an Alzheimer transgenic mouse. J. Neurosci. 21 (2001), 8370–8377.
113. Lim, D., Fedrizzi, L., Tartari, M., Zuccato, C., Cattaneo, E., Brini, M., Calcium homeostasis and mitochondrial dysfunction in striatal neurons of Huntington disease. J. Biol. Chem. 283 (2008), 5780–5789.
114. Limtrakul, P., Lipigorngoson, S., Namwong, O., Apisariyakul, A., Dunn, F., Inhibitory effect of dietary curcumin on skin carcinogenesis in mice. Cancer Lett. 116 (1997), 197–203.
115. Lin, J., Puigserver, P., Donovan, J., Tarr, P., Spiegelman, B.M., Peroxisome proliferator-activated receptor gamma coactivator 1beta (PGC-1beta), a novel PGC-1-related transcription coactivator associated with host cell factor.J. Biol. Chem. 277 (2002), 1645–1648.
116. Litwinienko, G., Ingold, K., Abnormal solvent effects on hydrogen atom abstraction. 2. Resolution of the curcumin antioxidant controversy. The role of sequential proton loss electron transfer. J. Organomet. Chem. 69 (2004), 5888–5896.
117. Liu, Q., Loo, W.T., Sze, S., Tong, Y., Curcumin inhibits cell proliferation of MDA-MB-231 and BT-483 breast cancer cells mediated by down-regulation of NFκB, cyclinD and MMP-1 transcription. Phytomedicine 16 (2009), 916–922.
118. Liu, K., Chen, H.L., Huang, H., Jing, H., Dong, G.H., Wu, H.W., Curcumin attenuates cardiopulmonary bypass-induced lung oxidative damage in rats. J. Cardiovasc. Pharmacol. Ther. 17 (2012), 395–402.
119. Liu, L., Zhang, W., Wang, L., Li, Y., Tan, B., Lu, X., Curcumin prevents cerebral ischemia reperfusion injury via increase of mitochondrial biogenesis. Neurochem. Res. 39 (2014), 1322–1331.
120. Lobo, R., Prabhu, K.S., Shirwaikar, A., Shirwaikar, A., Curcuma zedoaria Rosc.(white turmeric): a review of its chemical, pharmacological and ethnomedicinal properties. J. Pharm. Pharmacol. 61 (2009), 13–21.
121. Lone, J., Choi, J.H., Kim, S.W., Yun, J.W., Curcumin induces brown fat-like phenotype in 3T3-L1 and primary white adipocytes. J. Nutr. Biochem. 27 (2016), 193–202.
122. Lowell, B.B., Shulman, G.I., Mitochondrial dysfunction and type 2 diabetes. Science 307 (2005), 384–387.
123. Ma, Q., Role of nrf2 in oxidative stress and toxicity. Annu. Rev. Pharmacol. Toxicol. 53 (2013), 401–426.
124. MacGarvey, N.C., Suliman, H.B., Bartz, R.R., Fu, P., Withers, C.M., Welty-Wolf, K.E., Activation of mitochondrial biogenesis by heme oxygenase-1-mediated NF-E2-related factor-2 induction rescues mice from lethal Staphylococcus aureus sepsis. Am. J. Respir. Crit. Care Med. 185 (2012), 851–861.
125. Marczylo, T.H., Steward, W.P., Gescher, A.J., Rapid analysis of curcumin and curcumin metabolites in rat biomatrices using a novel ultraperformance liquid chromatography (UPLC) method. J. Agric. Food Chem. 57 (2009), 797–803.
126. Martin, R.C., Aiyer, H.S., Malik, D., Li, Y., Effect on pro-inflammatory and antioxidant genes and bioavailable distribution of whole turmeric vs curcumin: Similar root but different effects. Food Chem. Toxicol. 50 (2012), 227–231.
127. McBride, H.M., Neuspiel, M., Wasiak, S., Mitochondria: more than just a powerhouse. Curr. Biol. 16 (2006), R551–R560.
128. Menon, V.P., Sudheer, A.R., Antioxidant and anti-inflammatory properties of curcumin. Adv. Exp. Med. Biol. 595 (2007), 105–125.
129. Metzler, M., Pfeiffer, E., Schulz, S.I., Dempe, J.S., Curcumin uptake and metabolism. Biofactors 39 (2013), 14–20.
130. Meyers, D.E., Basha, H.I., Koenig, M.K., Mitochondrial cardiomyopathy: pathophysiology, diagnosis, and management. Tex. Heart Inst. J. 40 (2013), 385–394.
131. Morris, G., Anderson, G., Dean, O., Berk, M., Galecki, P., Martin-Subero, M., The glutathione system: a new drug target in neuroimmune disorders. Mol. Neurobiol. 50 (2014), 1059–1084.
132. Muthumani, M., Miltonprabu, S., Ameliorative efficacy of tetrahydrocurcumin against arsenic induced oxidative damage, dyslipidemia and hepatic mitochondrial toxicity in rats. Chem. Biol. Interact. 235 (2015), 95–105.
133. Nabavi, S.F., Nabavi, S.M., Ebrahimzadeh, M.A., Eslami, S., Jafari, N., Moghaddam, A.H., The protective effect of curcumin against sodium fluoride-induced oxidative stress in rat heart. Arch. Biol. Sci. 63 (2011), 563–569.
134. Nabavi, S.F., Moghaddam, A.H., Eslami, S., Nabavi, S.M., Protective effects of curcumin against sodium fluoride-induced toxicity in rat kidneys. Biol. Trace Elem. Res. 145 (2012), 369–374.
135. Nabavi, S.F., Daglia, M., Moghaddam, A.H., Habtemariam, S., Nabavi, S.M., Curcumin and liver disease: from chemistry to medicine. Compr. Rev. Food Sci. Food Saf. 13 (2014), 62–77.
136. Nabavi, S.F., Russo, G.L., Daglia, M., Nabavi, S.M., Role of quercetin as an alternative for obesity treatment: you are what you eat!. Food Chem. 179 (2015), 305–310.
137. Nabavi, S.F., Thiagarajan, R., Rastrelli, L., Daglia, M., Sobarzo-Sanchez, E., Alinezhad, H., Curcumin: a natural product for diabetes and its complications. Curr. Top. Med. Chem. 15 (2015), 2445–2455.
138. Nabavi, S.M., Marchese, A., Izadi, M., Curti, V., Daglia, M., Nabavi, S.F., Plants belonging to the genus Thymus as antibacterial agents: from farm to pharmacy. Food Chem. 173 (2015), 339–347.
139. Natarajan, C., Bright, J.J., Curcumin inhibits experimental allergic encephalomyelitis by blocking IL-12 signaling through Janus kinase-STAT pathway in T lymphocytes. J. Immunol. 168 (2002), 6506–6513.
140. Nautiyal, J., Banerjee, S., Kanwar, S.S., Yu, Y., Patel, B.B., Sarkar, F.H., Curcumin enhances dasatinib‐induced inhibition of growth and transformation of colon cancer cells. Int. J. Cancer 128 (2011), 951–961.
141. Negrette-Guzmán, M., García-Niño, W.R., Tapia, E., Zazueta, C., Huerta-Yepez, S., León-Contreras, J.C., Curcumin attenuates gentamicin-induced kidney mitochondrial alterations: possible role of a mitochondrial biogenesis mechanism. Evid. Based Complement. Alternat. Med., 2015, 2015, 917435.
142. Newmeyer, D.D., Ferguson-Miller, S., Mitochondria: releasing power for life and unleashing the machineries of death. Cell 112 (2003), 481–490.
143. Nurfina, A., Reksohadiprodjo, M., Timmerman, H., Jenie, U., Sugiyanto, D., Van der Goot, H., Synthesis of some symmetrical curcumin derivatives and their antiinflammatory activity. Eur. J. Med. Chem. 32 (1997), 321–328.
144. Pan, M.H., Huang, T.M., Lin, J.K., Biotransformation of curcumin through reduction and glucuronidation in mice. Drug Metab. Dispos. 27 (1999), 486–494.
145. Pan, M.H., Lin-Shiau, S.Y., Lin, J.K., Comparative studies on the suppression of nitric oxide synthase by curcumin and its hydrogenated metabolites through down-regulation of IκB kinase and NFκB activation in macrophages. Biochem. Pharmacol. 60 (2000), 1665–1676.
146. Pan, Y., Zhu, G., Wang, Y., Cai, L., Cai, Y., Hu, J., Attenuation of high-glucose-induced inflammatory response by a novel curcumin derivative B06 contributes to its protection from diabetic pathogenic changes in rat kidney and heart. J. Nutr. Biochem. 24 (2013), 146–155.
147. Parimita, S.P., Ramshankar, Y.V., Suresh, S., Guru Row, T., Redetermination of curcumin(1E, 4Z, 6E)-5-hydroxy-1, 7-bis (4-hydroxy-3-methoxyphenyl) hepta-1, 4, 6-trien-3-one. Acta Crystallograph. Sect. E63 (2007), 860–862.
148. Pasinetti, G.M., Wang, J., Ho, L., Zhao, W., Dubner, L., Roles of resveratrol and other grape-derived polyphenols in Alzheimer's disease prevention and treatment. Biochim. Biophys. Acta (BBA)—Mol. Basis Dis. 1852 (2015), 1202–1208.
149. Patil, S., Choudhary, B., Rathore, A., Roy, K., Mahadik, K., Enhanced oral bioavailability and anticancer activity of novel curcumin loaded mixed micelles in human lung cancer cells. Phytomedicine 22 (2015), 1103–1111.
150. Payton, F., Sandusky, P., Alworth, W.L., NMR study of the solution structure of curcumin. J. Nat. Prod. 70 (2007), 143–146.
151. Peng, J.R., Qian, Z.Y., Drug delivery systems for overcoming the bioavailability of curcumin: not only the nanoparticle matters. Nanomedicine 9 (2014), 747–750.
152. Pfeiffer, E., Höhle, S., Solyom, A.M., Metzler, M., Studies on the stability of turmeric constituents. J. Food Eng. 56 (2003), 257–259.
153. Piantadosi, C.A., Carraway, M.S., Babiker, A., Suliman, H.B., Heme oxygenase-1 regulates cardiac mitochondrial biogenesis via Nrf2-mediated transcriptional control of nuclear respiratory factor-1. Circ. Res. 103 (2008), 1232–1240.
154. Picca, A., Lezza, A.M., Regulation of mitochondrial biogenesis through TFAM-mitochondrial DNA interactions: useful insights from aging and calorie restriction studies. Mitochondrion 25 (2015), 67–75.
155. Picone, P., Nuzzo, D., Caruana, L., Scafidi, V., Di Carlo, M., Mitochondrial dysfunction: different routes to Alzheimer's disease therapy. Oxidative Med. Cell. Longev., 2014, 2014, 780179.
156. Policegoudra, R., Aradhya, S., Singh, L., Mango ginger (Curcuma amada Roxb.)—a promising spice for phytochemicals and biological activities. J. Biosci. 36 (2011), 739–748.
157. Priyadarsini, K.I., Free radical reactions of curcumin in membrane models. Free Radic. Biol. Med. 23 (1997), 838–843.
158. Priyadarsini, K.I., Photophysics, photochemistry and photobiology of curcumin: studies from organic solutions, bio-mimetics and living cells. J Photochem Photobiol C: Photochem Rev 10 (2009), 81–95.
159. Priyadarsini, K.I., Maity, D.K., Naik, G., Kumar, M.S., Unnikrishnan, M., Satav, J., Role of phenolic OH and methylene hydrogen on the free radical reactions and antioxidant activity of curcumin. Free Radic. Biol. Med. 35 (2003), 475–484.
160. Priyanka, A., Anusree, S.S., Nisha, V.M., Raghu, K.G., Curcumin improves hypoxia induced dysfunctions in 3T3‐L1 adipocytes by protecting mitochondria and down regulating inflammation. Biofactors 40 (2014), 513–523.
161. Prusty, B.K., Das, B.C., Constitutive activation of transcription factor AP‐1 in cervical cancer and suppression of human papillomavirus (HPV) transcription and AP‐1 activity in HeLa cells by curcumin. Int. J. Cancer 113 (2005), 951–960.
162. Puigserver, P., Wu, Z., Park, C.W., Graves, R., Wright, M., Spiegelman, B.M., A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis. Cell 92 (1998), 829–839.
163. Pullakhandam, R., Srinivas, P., Nair, M.K., Reddy, G.B., Binding and stabilization of transthyretin by curcumin. Arch. Biochem. Biophys. 485 (2009), 115–119.
164. Quiñones, M., Miguel, M., Aleixandre, A., Beneficial effects of polyphenols on cardiovascular disease. Pharmacol. Res. 68 (2013), 125–131.
165. Radjaram, A., Hafid, A.F., Setyawan, D., Dissolution enhancement of curcumin by hydroxypropyl-β-cyclodextrin complexation. Int J Pharm Pharm Sci 5 (2013), 401–405.
166. Raha, S., McEachern, G.E., Myint, A.T., Robinson, B.H., Superoxides from mitochondrial complex III: the role of manganese superoxide dismutase. Free Radic. Biol. Med. 29 (2009), 170–180.
167. Rajagopalan, S., Rane, A., Chinta, S.J., Andersen, J.K., Regulation of ATP13A2 via PHD2-HIF1α signaling is critical for cellular iron homeostasis: implications for Parkinson's disease. J. Neurosci. 36 (2016), 1086–1095.
168. Rajasekaran, S.A., Therapeutic potential of curcumin in gastrointestinal diseases. World J. Gastrointest. Pathophysiol. 2 (2011), 1–14.
169. Ramirez-Ahumada Mdel, C., Timmermann, B.N., Gang, D.R., Biosynthesis of curcuminoids and gingerols in turmeric (Curcuma longa) and ginger (Zingiber officinale): identification of curcuminoid synthase and hydroxycinnamoyl-CoA thioesterases. Phytochemistry 67 (2006), 2017–2029.
170. Ranjan, A.P., Mukerjee, A., Helson, L., Gupta, R., Vishwanatha, J.K., Efficacy of liposomal curcumin in a human pancreatic tumor xenograft model: inhibition of tumor growth and angiogenesis. Anticancer Res. 33 (2013), 3603–3609.
171. Rao, M., Curcuminoids as potent inhibitors of lipid peroxidation. J. Pharm. Pharmacol. 46 (1994), 1013–1016.
172. Rao, K.M., Rao, K.K., Ramanjaneyulu, G., Ha, C.S., Curcumin encapsulated pH sensitive gelatin based interpenetrating polymeric network nanogels for anti cancer drug delivery. Int. J. Pharm. 478 (2015), 788–795.
173. Rashid, K., Sil, P.C., Curcumin ameliorates testicular damage in diabetic rats by suppressing cellular stress-mediated mitochondria and endoplasmic reticulum-dependent apoptotic death. Biochim. Biophys. Acta (BBA)—Mol. Basis Dis. 1852 (2015), 70–82.
174. Rasyid, A., Lelo, A., The effect of curcumin and placebo on human gall-bladder function: an ultrasound study. Aliment. Pharmacol. Ther. 13 (1999), 245–250.
175. Ravindranath, V., Chandrasekhara, N., Absorption and tissue distribution of curcumin in rats. Toxicology 16 (1980), 259–265.
176. Ravindranath, V., Chandrasekhara, N., Metabolism of curcumn-studies with [3 H] curcumin. Toxicology 22 (1982), 337–344.
177. Romero-Hernández, M.A., Eguía-Aguilar, P., Perézpeña-Diaz Conti, M., Rodríguez-Leviz, A., Sadowinski-Pine, S., Velasco-Rodríguez, L.A., Toxic effects induced by curcumin in human astrocytoma cell lines. Toxicol. Mech. Methods 23 (2013), 650–659.
178. Roy, S., Raychaudhuri, S.S., In vitro regeneration and estimation of curcumin content in four species of Curcuma. Plant Biol. 21 (2004), 299–302.
179. Ruby, A., Kuttan, G., Babu, K.D., Rajasekharan, K., Kuttan, R., Anti-tumour and antioxidant activity of natural curcuminoids. Cancer Lett. 94 (1995), 79–83.
180. Russo, M., Russo, G.L., Daglia, M., Kasi, P.D., Ravi, S., Nabavi, S.F., Understanding genistein in cancer: the “good” and the “bad” effects: a review. Food Chem. 196 (2016), 589–600.
181. Sakamoto, K., McCarthy, A., Smith, D., Green, K.A., Hardie, D.G., Ashworth, A., Deficiency of LKB1 in skeletal muscle prevents AMPK activation and glucose uptake during contraction. EMBO J. 24 (2005), 1810–1820.
182. Sari, T., Mann, B., Kumar, R., Singh, R., Sharma, R., Bhardwaj, M., Preparation and characterization of nanoemulsion encapsulating curcumin. Food Hydrocoll. 43 (2015), 540–546.
183. Scarpulla, R.C., Metabolic control of mitochondrial biogenesis through the PGC-1 family regulatory network. Biochim. Biophys. Acta 1813 (2011), 1269–1278.
184. Scherz-Shouval, R., Elazar, Z., ROS, mitochondria and the regulation of autophagy. Trends Cell Biol. 17 (2007), 422–427.
185. Schneider, C., Gordon, O.N., Edwards, R.L., Luis, P.B., Degradation of curcumin: from mechanism to biological implications. J. Agric. Food Chem. 63 (2015), 7606–7614.
186. Schreiber, S.N., Knutti, D., Brogli, K., Uhlmann, T., Kralli, A., The transcriptional coactivator PGC-1 regulates the expression and activity of the orphan nuclear receptor estrogen-related receptor alpha (ERRalpha). J. Biol. Chem. 278 (2003), 9013–9018.
187. Seigler, D.S., Plant Secondary Metabolism. 2012, Springer Science $_amp_$amp; Business Media.
188. Sethi, G., Sung, B., Aggarwal, B.B., The role of curcumin in modern medicine. Herbal Drugs: Ethnomedicine to Modern Medicine, 2009, Springer, 97–113.
189. 2+ signaling. Biochem. Pharmacol. 58 (1999), 1167–1172.
190. Sharma, R., Gescher, A., Steward, W., Curcumin: the story so far. Eur. J. Cancer 41 (2005), 1955–1968.
191. Sharma, A.V., Ganguly, K., Paul, S., Maulik, N., Swarnakar, S., Curcumin heals indomethacin-induced gastric ulceration by stimulation of angiogenesis and restitution of collagen fibers via VEGF and MMP-2 mediated signaling. Antioxid. Redox Signal. 16 (2012), 351–362.
192. Sharma, K., Karl, B., Mathew, A.V., Gangoiti, J.A., Wassel, C.L., Saito, R., Metabolomics reveals signature of mitochondrial dysfunction in diabetic kidney disease. J. Am. Soc. Nephrol. 24 (2013), 1901–1912.
193. Shehzad, A., Lee, Y., Curcumin: multiple molecular targets mediate multiple pharmacological actions: a review. Drugs Future, 35, 2010, 113.
194. Shelma, R., Sharma, C.P., In vitro and in vivo evaluation of curcumin loaded lauroyl sulphated chitosan for enhancing oral bioavailability. Carbohydr. Polym. 95 (2013), 441–448.
195. Shen, L., Ji, H.F., Theoretical study on physicochemical properties of curcumin. Spectrochim. Acta A Mol. Biomol. Spectrosc. 67 (2007), 619–623.
196. Shen, L., Ji, H.F., Zhang, H.Y., A TD-DFT study on triplet excited-state properties of curcumin and its implications in elucidating the photosensitizing mechanisms of the pigment. Chem. Phys. Lett. 409 (2005), 300–303.
197. Sheng, B., Wang, X., Su, B., Lee, H.G., Casadesus, G., Perry, G., Impaired mitochondrial biogenesis contributes to mitochondrial dysfunction in Alzheimer's disease. J. Neurochem. 120 (2012), 419–429.
198. Shin, S.K., Ha, T.Y., McGregor, R.A., Choi, M.S., Long‐term curcumin administration protects against atherosclerosis via hepatic regulation of lipoprotein cholesterol metabolism. Mol. Nutr. Food Res. 55 (2011), 1829–1840.
199. Shin, G.H., Chung, S.K., Kim, J.T., Joung, H.J., Park, H.J., Preparation of chitosan-coated nanoliposomes for improving the mucoadhesive property of curcumin using the ethanol injection method. J. Agric. Food Chem. 61 (2013), 11119–11126.
200. Shishodia, S., Molecular mechanisms of curcumin action: gene expression. Biofactors 39 (2013), 37–55.
201. Shishodia, S., Sethi, G., Aggarwal, B.B., Curcumin: getting back to the roots. Ann. N. Y. Acad. Sci. 1056 (2005), 206–217.
202. Shukla, P.K., Khanna, V.K., Khan, M.Y., Srimal, R.C., Protective effect of curcumin against lead neurotoxicity in rat. Hum. Exp. Toxicol. 22 (2003), 653–658.
203. Sidhu, G.S., Singh, A.K., Thaloor, D., Banaudha, K.K., Patnaik, G.K., Srimal, R.C., Enhancement of wound healing by curcumin in animals. Wound Repair Regen. 6 (1998), 167–177.
204. Siviero, A., Gallo, E., Maggini, V., Gori, L., Mugelli, A., Firenzuoli, F., Curcumin, a golden spice with a low bioavailability. J. Herb. Med. 5 (2015), 57–70.
205. Somparn, P., Phisalaphong, C., Nakornchai, S., Unchern, S., Morales, N.P., Comparative antioxidant activities of curcumin and its demethoxy and hydrogenated derivatives. Biol. Pharm. Bull. 30 (2007), 74–78.
206. Song, M., Mihara, K., Chen, Y., Scorrano, L., Dorn, G.W. 2nd, Mitochondrial fission and fusion factors reciprocally orchestrate mitophagic culling in mouse hearts and cultured fibroblasts. Cell Metab. 21 (2015), 273–285.
207. Songkroh, T., Xie, H., Yu, W., Liu, X., Sun, G., Xu, X., Injectable in situ forming chitosan-based hydrogels for curcumin delivery. Macromol. Res. 23 (2015), 53–59.
208. Stein, S., Woods, A., Jones, N., Davison, M., Carling, D., The regulation of AMP-activated protein kinase by phosphorylation. Biochem. J. 345 (2000), 437–443.
209. Su, B., Wang, X., Zheng, L., Perry, G., Smith, M.A., Zhu, X., Abnormal mitochondrial dynamics and neurodegenerative diseases. Biochim. Biophys. Acta 1802 (2010), 135–142.
210. Sun, Y., Zhang, J., Zhou, J., Huang, Z., Hu, H., Qiao, M., Synergistic effect of cucurbitacin B in combination with curcumin via enhancing apoptosis induction and reversing multidrug resistance in human hepatoma cells. Eur. J. Pharmacol. 768 (2015), 28–40.
211. Taylor, S.W., Fahy, E., Zhang, B., Glenn, G.M., Warnock, D.E., Wiley, S., Characterization of the human heart mitochondrial proteome. Nat. Biotechnol. 21 (2003), 281–286.
212. Thangapazham, R.L., Sharma, A., Maheshwari, R.K., Beneficial role of curcumin in skin diseases. The Molecular Targets and Therapeutic Uses of Curcumin in Health and Disease, 2007, Springer, 343–357.
213. Tong, M., Sadoshima, J., Mitochondrial autophagy in cardiomyopathy. Curr. Opin. Genet. Dev. 38 (2016), 8–15.
214. Tonnesen, H., Karlsen, J., Mostad, A., Structural studies of curcuminoids. 1. The crystal-structure of curcumin. Acta Chem. Scand. Ser. B 36 (1982), 475–479.
215. Tønnesen, H.H., De Vries, H., Karlsen, J., Henegouwen, V., Beijersbergen, G., Studies on curcumin and curcuminoids IX: investigation of the photobiological activity of curcumin using bacterial indicator systems. J. Pharm. Sci. 76 (1987), 371–373.
216. Tresserra-Rimbau, A., Rimm, E.B., Medina-Remón, A., Martínez-González, M.A., López-Sabater, M.C., Covas, M.I., Polyphenol intake and mortality risk: a re-analysis of the PREDIMED trial. BMC Med., 12, 2014, 77.
217. Turrens, J.F., Mitochondrial formation of reactive oxygen species. J. Physiol. 552 (2003), 335–344.
218. Ueki, M., Ueno, M., Morishita, J., Maekawa, N., Curcumin ameliorates cisplatin-induced nephrotoxicity by inhibiting renal inflammation in mice. J. Biosci. Bioeng. 115 (2013), 547–551.
219. Vandecasteele, G., Szabadkai, G., Rizzuto, R., Mitochondrial calcium homeostasis: mechanisms and molecules. IUBMB Life 52 (2001), 213–220.
220. Virbasius, C.A., Virbasius, J.V., Scarpulla, R.C., NRF-1, an activator involved in nuclear-mitochondrial interactions, utilizes a new DNA-binding domain conserved in a family of developmental regulators. Genes Dev. 7 (1993), 2431–2445.
221. Virbasius, J.V., Virbasius, C.A., Scarpulla, R.C., Identity of GABP with NRF-2, a multisubunit activator of cytochrome oxidase expression, reveals a cellular role for an ETS domain activator of viral promoters. Genes Dev. 7 (1993), 380–392.
222. Vögtle, F.N., Wortelkamp, S., Zahedi, R.P., Becker, D., Leidhold, C., Gevaert, K., Global analysis of the mitochondrial N-proteome identifies a processing peptidase critical for protein stability. Cell 139 (2009), 428–439.
223. Wahlström, B., Blennow, G., A study on the fate of curcumin in the rat. Acta Pharmacol. Toxicol. 43 (1978), 86–92.
224. Wang, Y.J., Pan, M.H., Cheng, A.L., Lin, L.I., Ho, Y.S., Hsieh, C.Y., Stability of curcumin in buffer solutions and characterization of its degradation products. J. Pharm. Biomed. Anal. 15 (1997), 1867–1876.
225. Wang, X., Leung, A.W., Luo, J., Xu, C., TEM observation of ultrasound-induced mitophagy in nasopharyngeal carcinoma cells in the presence of curcumin. Exp. Ther. Med. 3 (2012), 146–148.
226. Wang, N.P., Wang, Z.F., Tootle, S., Philip, T., Zhao, Z.Q., Curcumin promotes cardiac repair and ameliorates cardiac dysfunction following myocardial infarction. Br. J. Pharmacol. 167 (2012), 1550–1562.
227. Wang, S., Wang, X., Ye, Z., Xu, C., Zhang, M., Ruan, B., Curcumin promotes browning of white adipose tissue in a norepinephrine-dependent way. Biochem. Biophys. Res. Commun. 466 (2015), 247–253.
228. Weng, G., Zeng, Y., Huang, J., Fan, J., Guo, K., Curcumin enhanced busulfan-induced apoptosis through downregulating the expression of survivin in leukemia stem-like KG1a Cells. BioMed. Res. Int., 2015, 2015, 630397.
229. Widmer, R., Freund, M., Flammer, A., Sexton, J., Lennon, R., Romani, A., Beneficial effects of polyphenol-rich olive oil in patients with early atherosclerosis. Eur. J. Nutr. 52 (2013), 1223–1231.
230. Wilken, R., Veena, M.S., Wang, M.B., Srivatsan, E.S., Curcumin: a review of anti-cancer properties and therapeutic activity in head and neck squamous cell carcinoma. Mol. Cancer, 10, 2011, 1.
231. Wright, J.S., Predicting the antioxidant activity of curcumin and curcuminoids. J. Mol. Struct. THEOCHEM 591 (2002), 207–217.
232. Wu, J.Y., Lin, C.Y., Lin, T.W., Ken, C.F., Wen, Y.D., Curcumin affects development of zebrafish embryo. Biol. Pharm. Bull. 30 (2007), 1336–1339.
233. Xie, X., Tao, Q., Zou, Y., Zhang, F., Guo, M., Wang, Y., PLGA nanoparticles improve the oral bioavailability of curcumin in rats: characterizations and mechanisms. J. Agric. Food Chem. 59 (2011), 9280–9289.
234. Yan, G., Graham, K., Lanza‐Jacoby, S., Curcumin enhances the anticancer effects of trichostatin a in breast cancer cells. Mol. Carcinog. 52 (2013), 404–411.
235. Yang, F., Lim, G.P., Begum, A.N., Ubeda, O.J., Simmons, M.R., Ambegaokar, S.S., Curcumin inhibits formation of amyloid β oligomers and fibrils, binds plaques, and reduces amyloid in vivo. J. Biol. Chem. 280 (2005), 5892–5901.
236. Yu, G., Liu, L., Zhang, P., Li, Y., Protective effect of curcumin on chronic cerebral ischemia by altering expression of α-synuclein in 2VO model. Mol. Neurodegener., 7, 2012, S33.
237. Zamora, M., Pardo, R., Villena, J.A., Pharmacological induction of mitochondrial biogenesis as a therapeutic strategy for the treatment of type 2 diabetes. Biochem. Pharmacol. 98 (2015), 16–28.
238. Zhang, Q., Wu, Y., Zhang, P., Sha, H., Jia, J., Hu, Y., Exercise induces mitochondrial biogenesis after brain ischemia in rats. Neuroscience 205 (2012), 10–17.
239. Zhang, J., Tang, Q., Xu, X., Li, N., Development and evaluation of a novel phytosome-loaded chitosan microsphere system for curcumin delivery. Int. J. Pharm. 448 (2013), 168–174.