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Food Science and Human Wellness 2019, 8(1): 25-33 https://doi.org/10.1016/j.fshw.2019.03.002
Research Article | Open Access | Issue | Published: 14 March 2019

Autophagy-associated signal pathways of functional foods for chronic diseases

Show Author's Information Jinfeng Xiea,,  Jiling Lianga,  Ning Chenb( )
Graduate School, Wuhan Sports University, Wuhan 430079, China
Tianjiu Research and Development Center for Exercise Nutrition and Foods, Hubei Key Laboratory of Exercise Training and Monitoring, College of Health Science, Wuhan Sports University, Wuhan 430079, China

Peer review under responsibility of KeAi Communications Co., Ltd.

Keywords:
Curcumin, Autophagy, Resveratrol, Trehalose, Chronic diseases, Epigallocatechin-3-gallate
Cite this article:
Xie J, Liang J, Chen N. Autophagy-associated signal pathways of functional foods for chronic diseases. Food Science and Human Wellness, 2019, 8(1): 25-33. https://doi.org/10.1016/j.fshw.2019.03.002
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Abstract Full text About this article

Functional foods, namely as natural or processed foods containing bioactive compounds, can provide health-promoting effects beyond basic nutrition, or offer the prevention or supplementary treatment of chronic diseases. The bioactive components in functional foods usually have pleiotropic effects, including antioxidant, anti-inflammatory, hypolipidemic, glycemic-regulating, cytoprotective, and neuroprotective functions. Autophagy is one of the highly conserved cellular processes for the clearance of aberrant components in eukaryotic cells, and plays an essential role in health promotion and prevention and treatment of a series of chronic diseases. Once the cells are in the stress environment, the induced autophagy will accelerate the clearance of cellular damaged or toxic protein aggregates or dysfunctional cellular organelles to maintain homeostasis in cells. In this article, we summarize several widely investigated bioactive components used as functional foods, such as resveratrol, epigallocatechin-3-gallate, curcumin and trehalose, with the regulatory function for autophagy during the intervention of chronic diseases, which will provide the references or novel thoughts for the development of functional foods with the modulation of autophagy.


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About this article

Autophagy-associated signal pathways of functional foods for chronic diseases

Show Author's information Jinfeng Xiea,, Jiling Lianga, Ning Chenb( )
Graduate School, Wuhan Sports University, Wuhan 430079, China
Tianjiu Research and Development Center for Exercise Nutrition and Foods, Hubei Key Laboratory of Exercise Training and Monitoring, College of Health Science, Wuhan Sports University, Wuhan 430079, China

Peer review under responsibility of KeAi Communications Co., Ltd.

Abstract

Functional foods, namely as natural or processed foods containing bioactive compounds, can provide health-promoting effects beyond basic nutrition, or offer the prevention or supplementary treatment of chronic diseases. The bioactive components in functional foods usually have pleiotropic effects, including antioxidant, anti-inflammatory, hypolipidemic, glycemic-regulating, cytoprotective, and neuroprotective functions. Autophagy is one of the highly conserved cellular processes for the clearance of aberrant components in eukaryotic cells, and plays an essential role in health promotion and prevention and treatment of a series of chronic diseases. Once the cells are in the stress environment, the induced autophagy will accelerate the clearance of cellular damaged or toxic protein aggregates or dysfunctional cellular organelles to maintain homeostasis in cells. In this article, we summarize several widely investigated bioactive components used as functional foods, such as resveratrol, epigallocatechin-3-gallate, curcumin and trehalose, with the regulatory function for autophagy during the intervention of chronic diseases, which will provide the references or novel thoughts for the development of functional foods with the modulation of autophagy.

Keywords: Curcumin, Autophagy, Resveratrol, Trehalose, Chronic diseases, Epigallocatechin-3-gallate

References(133)

[1]

C.K. Roberts, R.J. Barnard, Effects of exercise and diet on chronic disease, J. Appl. Physiol. 98 (2005) (1985) 3–30.
DOI Google Scholar
[2]

X. Kou, N. Chen, Resveratrol as a natural autophagy regulator for prevention and treatment of Alzheimer's disease, Nutrients 9 (2017).
DOI Google Scholar
[3]

M.H. Stipanuk, Macroautophagy and its role in nutrient homeostasis, Nutr. Rev. 67 (2009) 677–689.
DOI Google Scholar
[4]

S.F. Zhang, X.L. Wang, X.Q. Yang, N. Chen, Autophagy-associated targeting pathways of natural products during cancer treatment, Asian Pac. J. Cancer Prev. 15 (2014) 10557–10563.
DOI Google Scholar
[5]

S. Davinelli, N. Sapere, D. Zella, et al., Pleiotropic protective effects of phytochemicals in Alzheimer's disease, Oxid. Med. Cell. Longev. 2012 (2012), 386527.
DOI Google Scholar
[6]

G.M. Do, U.J. Jung, H.J. Park, et al., Resveratrol ameliorates diabetes-related metabolic changes via activation of AMP-activated protein kinase and its downstream targets in db/db mice, Mol. Nutr. Food Res. 56 (2012) 1282–1291.
DOI Google Scholar
[7]

J. Fan, X. Yang, J. Li, et al., Spermidine coupled with exercise rescues skeletal muscle atrophy from D-gal-induced aging rats through enhanced autophagy and reduced apoptosis via AMPK-FOXO3a signal pathway, Oncotarget 8 (2017) 17475–17490.
DOI Google Scholar
[8]

A.E. Ozen, A. Pons, J.A. Tur, Worldwide consumption of functional foods: a systematic review, Nutr. Rev. 70 (2012) 472–481.
DOI Google Scholar
[9]

R. Botchlett, S.L. Woo, M. Liu, et al., Nutritional approaches for managing obesity-associated metabolic diseases, J. Endocrinol. 233 (2017) R145–R171.
DOI Google Scholar
[10]

G. Mocciaro, N. Ziauddeen, J. Godos, et al., Does a Mediterranean-type dietary pattern exert a cardio-protective effect outside the Mediterranean region? A review of current evidence, Int. J. Food Sci. Nutr. 69 (2018) 524–535.
DOI Google Scholar
[11]

D.M. Martirosyan, J. Singh, A new definition of functional food by FFC: what makes a new definition unique?, Funct. Foods Health Dis. 5 (2015) 209–223.
DOI Google Scholar
[12]

J.R. Lupton, Scientific substantiation of claims in the USA: focus on functional foods, Eur. J. Nutr. 48 (Suppl 1) (2009) S27–31.
DOI Google Scholar
[13]

N. Chen, V. Karantza-Wadsworth, Role and regulation of autophagy in cancer, Biochim. Biophys. Acta 1793 (2009) 1516–1523.
DOI Google Scholar
[14]

A.M. Cuervo, E. Bergamini, U.T. Brunk, et al., Autophagy and aging: the importance of maintaining "clean" cells, Autophagy 1 (2005) 131–140.
DOI Google Scholar
[15]

D.C. Rubinsztein, G. Marino, G. Kroemer, Autophagy and aging, Cell 146 (2011) 682–695.
DOI Google Scholar
[16]

N. Chen, V. Karantza, Autophagy as a therapeutic target in cancer, Cancer Biol. Ther. 11 (2011) 157–168.
DOI Google Scholar
[17]

J. Fan, X. Kou, S. Jia, et al., Autophagy as a potential target for sarcopenia, J. Cell. Physiol. 231 (2016) 1450–1459.
DOI Google Scholar
[18]

X. Kou, J. Li, X. Liu, et al., Swimming attenuates D-galactose-induced brain aging via suppressing miR-34a-mediated autophagy impairment and abnormal mitochondrial dynamics, J. Appl. Physiol. 122 (2017) (1985) 1462–1469.
DOI Google Scholar
[19]

E. Wong, A.M. Cuervo, Autophagy gone awry in neurodegenerative diseases, Nat. Neurosci. 13 (2010) 805–811.
DOI Google Scholar
[20]

B. Levine, G. Kroemer, Autophagy in the pathogenesis of disease, Cell 132 (2008) 27–42.
DOI Google Scholar
[21]

Y. Zhang, N. Chen, Autophagy is a promoter for aerobic exercise performance during high altitude training, Oxid. Med. Cell. Longev. 2018 (2018), 3617508.
DOI Google Scholar
[22]

N. Mizushima, T. Yoshimori, Y. Ohsumi, The role of Atg proteins in autophagosome formation, Annu. Rev. Cell Dev. Biol. 27 (2011) 107–132.
DOI Google Scholar
[23]

Z. Papackova, M. Cahova, Important role of autophagy in regulation of metabolic processes in health, disease and aging, Physiol. Res. 63 (2014) 409–420.
DOI Google Scholar
[24]

T.P. Neufeld, TOR-dependent control of autophagy: biting the hand that feeds, Curr. Opin. Cell Biol. 22 (2010) 157–168.
DOI Google Scholar
[25]

C. He, D.J. Klionsky, Regulation mechanisms and signaling pathways of autophagy, Annu. Rev. Genet. 43 (2009) 67–93.
DOI Google Scholar
[26]

C.G. Noble, J.M. Dong, E. Manser, H. Song, Bcl-xL and UVRAG cause a monomer-dimer switch in Beclin1, J. Biol. Chem. 283 (2008) 26274–26282.
DOI Google Scholar
[27]

Y. Ichimura, T. Kirisako, T. Takao, et al., A ubiquitin-like system mediates protein lipidation, Nature 408 (2000) 488–492.
DOI Google Scholar
[28]

Y. Feng, D. He, Z. Yao, D.J. Klionsky, The machinery of macroautophagy, Cell Res. 24 (2014) 24–41.
DOI Google Scholar
[29]

B. Ravikumar, S. Sarkar, J.E. Davies, et al., Regulation of mammalian autophagy in physiology and pathophysiology, Physiol. Rev. 90 (2010) 1383–1435.
DOI Google Scholar
[30]

P. Jiang, N. Mizushima, Autophagy and human diseases, Cell Res. 24 (2014) 69–79.
DOI Google Scholar
[31]

K. Mizumura, A.M. Choi, S.W. Ryter, Emerging role of selective autophagy in human diseases, Front. Pharmacol. 5 (2014) 244.
DOI Google Scholar
[32]

J. Ezaki, N. Matsumoto, M. Takeda-Ezaki, et al., Liver autophagy contributes to the maintenance of blood glucose and amino acid levels, Autophagy 7 (2011) 727–736.
DOI Google Scholar
[33]

R. Singh, S. Kaushik, Y. Wang, et al., Autophagy regulates lipid metabolism, Nature 458 (2009) 1131–1135.
DOI Google Scholar
[34]

H.L. Hayes, B.S. Peterson, J.M. Haldeman, et al., Delayed apoptosis allows islet beta-cells to implement an autophagic mechanism to promote cell survival, PLoS One 12 (2017), e0172567.
DOI Google Scholar
[35]

Y. Riahi, J.D. Wikstrom, E. Bachar-Wikstrom, et al., Autophagy is a major regulator of beta cell insulin homeostasis, Diabetologia 59 (2016) 1480–1491.
DOI Google Scholar
[36]

C. Ebato, T. Uchida, M. Arakawa, et al., Autophagy is important in islet homeostasis and compensatory increase of beta cell mass in response to high-fat diet, Cell Metab. 8 (2008) 325–332.
DOI Google Scholar
[37]

R.P. Robertson, Chronic oxidative stress as a central mechanism for glucose toxicity in pancreatic islet beta cells in diabetes, J. Biol. Chem. 279 (2004) 42351–42354.
DOI Google Scholar
[38]

Y. Yagishita, T. Fukutomi, A. Sugawara, et al., Nrf2 protects pancreatic beta-cells from oxidative and nitrosative stress in diabetic model mice, Diabetes 63 (2014) 605–618.
DOI Google Scholar
[39]

R. Scherz-Shouval, Z. Elazar, ROS, mitochondria and the regulation of autophagy, Trends Cell Biol. 17 (2007) 422–427.
DOI Google Scholar
[40]

Q. He, S. Sha, L. Sun, et al., GLP-1 analogue improves hepatic lipid accumulation by inducing autophagy via AMPK/mTOR pathway, Biochem. Biophys. Res. Commun. 476 (2016) 196–203.
DOI Google Scholar
[41]

J.A. David, W.J. Rifkin, P.S. Rabbani, D.J. Ceradini, The Nrf2/Keap1/ARE pathway and oxidative stress as a therapeutic target in type Ⅱ diabetes mellitus, J. Diabetes Res. 2017 (2017), 4826724.
DOI Google Scholar
[42]

J. Kim, H. Cheon, Y.T. Jeong, et al., Amyloidogenic peptide oligomer accumulation in autophagy-deficient beta cells induces diabetes, J. Clin. Invest. 124 (2014) 3311–3324.
DOI Google Scholar
[43]

J.L. Fetterman, M. Holbrook, N. Flint, et al., Restoration of autophagy in endothelial cells from patients with diabetes mellitus improves nitric oxide signaling, Atherosclerosis 247 (2016) 207–217.
DOI Google Scholar
[44]

J.W. Zylke, H. Bauchner, The unrelenting challenge of obesity, JAMA 315 (2016) 2277–2278.
DOI Google Scholar
[45]

S. Alers, A.S. Loffler, S. Wesselborg, B. Stork, Role of AMPK-mTOR-Ulk1/2 in the regulation of autophagy: cross talk, shortcuts, and feedbacks, Mol. Cell. Biol. 32 (2012) 2–11.
DOI Google Scholar
[46]

L. Yang, P. Li, S. Fu, et al., Defective hepatic autophagy in obesity promotes ER stress and causes insulin resistance, Cell Metab. 11 (2010) 467–478.
DOI Google Scholar
[47]

M.S. Kim, W. Quan, M.S. Lee, Role of hypothalamic autophagy in the control of whole body energy balance, Rev. Endocr. Metab. Disord. 14 (2013) 377–386.
DOI Google Scholar
[48]

H.J. Jansen, P. van Essen, T. Koenen, et al., Autophagy activity is up-regulated in adipose tissue of obese individuals and modulates proinflammatory cytokine expression, Endocrinology 153 (2012) 5866–5874.
DOI Google Scholar
[49]

J. Kosacka, M. Kern, N. Kloting, et al., Autophagy in adipose tissue of patients with obesity and type 2 diabetes, Mol. Cell. Endocrinol. 409 (2015) 21–32.
DOI Google Scholar
[50]

H. Wen, D. Gris, Y. Lei, et al., Fatty acid-induced NLRP3-ASC inflammasome activation interferes with insulin signaling, Nat. Immunol. 12 (2011) 408–415.
DOI Google Scholar
[51]

S. Li, X. Dou, H. Ning, et al., Sirtuin 3 acts as a negative regulator of autophagy dictating hepatocyte susceptibility to lipotoxicity, Hepatology 66 (2017) 936–952.
DOI Google Scholar
[52]

G. Filomeni, D. De Zio, F. Cecconi, Oxidative stress and autophagy: the clash between damage and metabolic needs, Cell Death Differ. 22 (2015) 377–388.
DOI Google Scholar
[53]

M. Xie, C.R. Morales, S. Lavandero, J.A. Hill, Tuning flux: autophagy as a target of heart disease therapy, Curr. Opin. Cardiol. 26 (2011) 216–222.
DOI Google Scholar
[54]

D. Egan, J. Kim, R.J. Shaw, K.L. Guan, The autophagy initiating kinase ULK1 is regulated via opposing phosphorylation by AMPK and mTOR, Autophagy 7 (2011) 643–644.
DOI Google Scholar
[55]

A. Hamacher-Brady, N.R. Brady, R.A. Gottlieb, Enhancing macroautophagy protects against ischemia/reperfusion injury in cardiac myocytes, J. Biol. Chem. 281 (2006) 29776–29787.
DOI Google Scholar
[56]

L. Valentim, K.M. Laurence, P.A. Townsend, et al., Urocortin inhibits Beclin1-mediated autophagic cell death in cardiac myocytes exposed to ischaemia/reperfusion injury, J. Mol. Cell. Cardiol. 40 (2006) 846–852.
DOI Google Scholar
[57]

Y. Li, C. Chen, F. Yao, et al., AMPK inhibits cardiac hypertrophy by promoting autophagy via mTORC1, Arch. Biochem. Biophys. 558 (2014) 79–86.
DOI Google Scholar
[58]

C. Vindis, Autophagy: an emerging therapeutic target in vascular diseases, Br. J. Pharmacol. 172 (2015) 2167–2178.
DOI Google Scholar
[59]

Y. Li, Z. Zhang, X. Zhang, et al., A dual PI3K/AKT/mTOR signaling inhibitor miR-99a suppresses endometrial carcinoma, Am. J. Transl. Res. 8 (2016) 719–731.
Google Scholar
[60]

A. Ucar, S.K. Gupta, J. Fiedler, et al., The miRNA-212/132 family regulates both cardiac hypertrophy and cardiomyocyte autophagy, Nat. Commun. 3 (2012) 1078.
DOI Google Scholar
[61]

B. Razani, C. Feng, T. Coleman, et al., Autophagy links inflammasomes to atherosclerotic progression, Cell Metab. 15 (2012) 534–544.
DOI Google Scholar
[62]

M.O. Grootaert, P.A. da Costa Martins, N. Bitsch, et al., Defective autophagy in vascular smooth muscle cells accelerates senescence and promotes neointima formation and atherogenesis, Autophagy 11 (2015) 2014–2032.
DOI Google Scholar
[63]

I. Sergin, S. Bhattacharya, R. Emanuel, et al., Inclusion bodies enriched for p62 and polyubiquitinated proteins in macrophages protect against atherosclerosis, Sci. Signal. 9 (2016), ra2.
DOI Google Scholar
[64]

F.M. Menzies, A. Fleming, A. Caricasole, et al., Autophagy and neurodegeneration: pathogenic mechanisms and therapeutic opportunities, Neuron 93 (2017) 1015–1034.
DOI Google Scholar
[65]

M. Komatsu, S. Waguri, T. Chiba, et al., Loss of autophagy in the central nervous system causes neurodegeneration in mice, Nature 441 (2006) 880–884.
DOI Google Scholar
[66]

D.M. Wolfe, J.H. Lee, A. Kumar, et al., Autophagy failure in Alzheimer's disease and the role of defective lysosomal acidification, Eur. J. Neurosci. 37 (2013) 1949–1961.
DOI Google Scholar
[67]

D.D. Martin, S. Ladha, D.E. Ehrnhoefer, M.R. Hayden, Autophagy in Huntington disease and huntingtin in autophagy, Trends Neurosci. 38 (2015) 26–35.
DOI Google Scholar
[68]

T.E. Moors, J.J. Hoozemans, A. Ingrassia, et al., Therapeutic potential of autophagy-enhancing agents in Parkinson's disease, Mol. Neurodegener. 12 (2017) 11.
DOI Google Scholar
[69]

D.C. Rubinsztein, C.F. Bento, V. Deretic, Therapeutic targeting of autophagy in neurodegenerative and infectious diseases, J. Exp. Med. 212 (2015) 979–990.
DOI Google Scholar
[70]

Y. Omata, Y.M. Lim, Y. Akao, L. Tsuda, Age-induced reduction of autophagy-related gene expression is associated with onset of Alzheimer's disease, Am. J. Neurodegener. Dis. 3 (2014) 134–142.
Google Scholar
[71]

F. Pickford, E. Masliah, M. Britschgi, et al., The autophagy-related protein beclin 1 shows reduced expression in early Alzheimer disease and regulates amyloid beta accumulation in mice, J. Clin. Invest. 118 (2008) 2190–2199.
DOI Google Scholar
[72]

K.M. Lucin, C.E. O'Brien, G. Bieri, et al., Microglial beclin 1 regulates retromer trafficking and phagocytosis and is impaired in Alzheimer's disease, Neuron 79 (2013) 873–886.
DOI Google Scholar
[73]

C. Yang, C.Z. Cai, J.X. Song, et al., NRBF2 is involved in the autophagic degradation process of APP-CTFs in Alzheimer disease models, Autophagy 13 (2017) 2028–2040.
DOI Google Scholar
[74]

A. Caccamo, A. Magri, D.X. Medina, et al., mTOR regulates tau phosphorylation and degradation: implications for Alzheimer's disease and other tauopathies, Aging Cell 12 (2013) 370–380.
DOI Google Scholar
[75]

L. Li, S. Zhang, X. Zhang, et al., Autophagy enhancer carbamazepine alleviates memory deficits and cerebral amyloid-beta pathology in a mouse model of Alzheimer's disease, Curr. Alzheimer Res. 10 (2013) 433–441.
DOI Google Scholar
[76]

T. Jiang, J.T. Yu, X.C. Zhu, et al., Temsirolimus promotes autophagic clearance of amyloid-beta and provides protective effects in cellular and animal models of Alzheimer's disease, Pharmacol. Res. 81 (2014) 54–63.
DOI Google Scholar
[77]

Y. Tian, V. Bustos, M. Flajolet, P. Greengard, A small-molecule enhancer of autophagy decreases levels of Abeta and APP-CTF via Atg5-dependent autophagy pathway, FASEB J. 25 (2011) 1934–1942.
DOI Google Scholar
[78]

C.J. Cortes, A.R. La Spada, The many faces of autophagy dysfunction in Huntington's disease: from mechanism to therapy, Drug Discov. Today 19 (2014) 963–971.
DOI Google Scholar
[79]

B. Ravikumar, C. Vacher, Z. Berger, et al., Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease, Nat. Genet. 36 (2004) 585–595.
DOI Google Scholar
[80]

L.V. Kalia, A.E. Lang, Parkinson's disease, Lancet 386 (2015) 896–912.
DOI Google Scholar
[81]

K.J. De Vos, A.J. Grierson, S. Ackerley, C.C. Miller, Role of axonal transport in neurodegenerative diseases, Annu. Rev. Neurosci. 31 (2008) 151–173.
DOI Google Scholar
[82]

B. Spencer, R. Potkar, M. Trejo, et al., Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in alpha-synuclein models of Parkinson's and Lewy body diseases, J. Neurosci. 29 (2009) 13578–13588.
DOI Google Scholar
[83]

X. Kou, M. Kirberger, Y. Yang, N. Chen, Natural products for cancer prevention associated with Nrf2–ARE pathway, Food Sci. Hum. Wellness 2 (2013) 22–28.
DOI Google Scholar
[84]

A.A. Bertelli, D.K. Das, Grapes, wines, resveratrol, and heart health, J. Cardiovasc. Pharmacol. 54 (2009) 468–476.
DOI Google Scholar
[85]

J.A. Baur, D.A. Sinclair, Therapeutic potential of resveratrol: the in vivo evidence, Nat. Rev. Drug Discov. 5 (2006) 493–506.
DOI Google Scholar
[86]

G.T. Diaz-Gerevini, G. Repossi, A. Dain, et al., Beneficial action of resveratrol: How and why?, Nutrition 32 (2016) 174–178.
DOI Google Scholar
[87]

W.J. Yan, R.B. Liu, L.K. Wang, et al., Sirt3-mediated autophagy contributes to resveratrol-induced protection against ER stress in HT22 cells, Front. Neurosci. 12 (2018) 116.
DOI Google Scholar
[88]

T. Szkudelski, K. Szkudelska, Resveratrol and diabetes: from animal to human studies, Biochim. Biophys. Acta 1852 (2015) 1145–1154.
DOI Google Scholar
[89]

K. Xu, X.F. Liu, Z.Q. Ke, et al., Resveratrol modulates apoptosis and autophagy induced by high glucose and palmitate in cardiac cells, Cell. Physiol. Biochem. 46 (2018) 2031–2040.
DOI Google Scholar
[90]

M. Koushki, N. Amiri-Dashatan, N. Ahmadi, et al., Resveratrol: a miraculous natural compound for diseases treatment, Food Sci. Nutr. 6 (2018) 2473–2490.
DOI Google Scholar
[91]

J. Song, Y. Huang, W. Zheng, et al., Resveratrol reduces intracellular reactive oxygen species levels by inducing autophagy through the AMPK-mTOR pathway, Front. Med. 12 (2018) 697–706.
DOI Google Scholar
[92]

V. Vingtdeux, L. Giliberto, H. Zhao, et al., AMP-activated protein kinase signaling activation by resveratrol modulates amyloid-beta peptide metabolism, J. Biol. Chem. 285 (2010) 9100–9113.
DOI Google Scholar
[93]

J. Wang, I. Santa-Maria, L. Ho, et al., Grape derived polyphenols attenuate tau neuropathology in a mouse model of Alzheimer's disease, J. Alzheimers Dis. 22 (2010) 653–661.
DOI Google Scholar
[94]

H. Deng, M.T. Mi, Resveratrol attenuates Abeta25-35 caused neurotoxicity by inducing autophagy through the TyrRS-PARP1-SIRT1 signaling pathway, Neurochem. Res. 41 (2016) 2367–2379.
DOI Google Scholar
[95]

F. Jin, Q. Wu, Y.F. Lu, et al., Neuroprotective effect of resveratrol on 6-OHDA-induced Parkinson's disease in rats, Eur. J. Pharmacol. 600 (2008) 78–82.
DOI Google Scholar
[96]

C. Vidoni, E. Secomandi, A. Castiglioni, et al., Resveratrol protects neuronal-like cells expressing mutant Huntingtin from dopamine toxicity by rescuing ATG4-mediated autophagosome formation, Neurochem. Int. 117 (2018) 174–187.
DOI Google Scholar
[97]

K.L. Johnston, M.N. Clifford, L.M. Morgan, Coffee acutely modifies gastrointestinal hormone secretion and glucose tolerance in humans: glycemic effects of chlorogenic acid and caffeine, Am. J. Clin. Nutr. 78 (2003) 728–733.
DOI Google Scholar
[98]

I. Rodriguez-Ramiro, S. Ramos, L. Bravo, et al., Procyanidin B2 and a cocoa polyphenolic extract inhibit acrylamide-induced apoptosis in human Caco-2 cells by preventing oxidative stress and activation of JNK pathway, J. Nutr. Biochem. 22 (2011) 1186–1194.
DOI Google Scholar
[99]

N.A. Singh, A.K. Mandal, Z.A. Khan, Potential neuroprotective properties of epigallocatechin-3-gallate (EGCG), Nutr. J. 15 (2016) 60.
DOI Google Scholar
[100]

H.S. Kim, V. Montana, H.J. Jang, et al., Epigallocatechin gallate (EGCG) stimulates autophagy in vascular endothelial cells: a potential role for reducing lipid accumulation, J. Biol. Chem. 288 (2013) 22693–22705.
DOI Google Scholar
[101]

S.N. Kim, H.J. Kwon, S. Akindehin, et al., Effects of epigallocatechin-3-gallate on autophagic lipolysis in adipocytes, Nutrients 9 (2017).
DOI Google Scholar
[102]

M.A. Potenza, F.L. Marasciulo, M. Tarquinio, et al., EGCG, a green tea polyphenol, improves endothelial function and insulin sensitivity, reduces blood pressure, and protects against myocardial I/R injury in SHR, Am. J. Physiol. Endocrinol. Metab. 292 (2007) E1378–1387.
DOI Google Scholar
[103]

X.X. Zheng, Y.L. Xu, S.H. Li, et al., Effects of green tea catechins with or without caffeine on glycemic control in adults: a meta-analysis of randomized controlled trials, Am. J. Clin. Nutr. 97 (2013) 750–762.
DOI Google Scholar
[104]

P.A. Townsend, T.M. Scarabelli, E. Pasini, et al., Epigallocatechin-3-gallate inhibits STAT-1 activation and protects cardiac myocytes from ischemia/reperfusion-induced apoptosis, FASEB J. 18 (2004) 1621–1623.
DOI Google Scholar
[105]

S.R. Hsieh, C.S. Hsu, C.H. Lu, et al., Epigallocatechin-3-gallate-mediated cardioprotection by Akt/GSK-3beta/caveolin signalling in H9c2 rat cardiomyoblasts, J. Biomed. Sci. 20 (2013) 86.
DOI Google Scholar
[106]

J.H. Lee, J.H. Moon, S.W. Kim, et al., EGCG-mediated autophagy flux has a neuroprotection effect via a class Ⅲ histone deacetylase in primary neuron cells, Oncotarget 6 (2015) 9701–9717.
DOI Google Scholar
[107]

C. Dai, G.D. Ciccotosto, R. Cappai, et al., Curcumin attenuates colistin-induced neurotoxicity in N2a cells via anti-inflammatory activity, suppression of oxidative stress, and apoptosis, Mol. Neurobiol. 55 (2018) 421–434.
DOI Google Scholar
[108]

A. Asai, T. Miyazawa, Dietary curcuminoids prevent high-fat diet-induced lipid accumulation in rat liver and epididymal adipose tissue, J. Nutr. 131 (2001) 2932–2935.
DOI Google Scholar
[109]

J. Han, X.Y. Pan, Y. Xu, et al., Curcumin induces autophagy to protect vascular endothelial cell survival from oxidative stress damage, Autophagy 8 (2012) 812–825.
DOI Google Scholar
[110]

L. Zhang, Y. Fang, X. Cheng, et al., The potential protective effect of curcumin on amyloid-beta-42 induced cytotoxicity in HT-22 cells, Biomed Res. Int. 2018 (2018), 8134902.
DOI Google Scholar
[111]

W. Yu, J. Wu, F. Cai, et al., Curcumin alleviates diabetic cardiomyopathy in experimental diabetic rats, PLoS One 7 (2012), e52013.
DOI Google Scholar
[112]

Z. Huang, B. Ye, Z. Dai, et al., Curcumin inhibits autophagy and apoptosis in hypoxia/reoxygenation-induced myocytes, Mol. Med. Rep. 11 (2015) 4678–4684.
DOI Google Scholar
[113]

R. Liu, H.B. Zhang, J. Yang, et al., Curcumin alleviates isoproterenol-induced cardiac hypertrophy and fibrosis through inhibition of autophagy and activation of mTOR, Eur. Rev. Med. Pharmacol. Sci. 22 (2018) 7500–7508.
Google Scholar
[114]

K. Yang, C. Xu, X. Li, H. Jiang, Combination of D942 with curcumin protects cardiomyocytes from ischemic damage through promoting autophagy, J. Cardiovasc. Pharmacol. Ther. 18 (2013) 570–581.
DOI Google Scholar
[115]

S. Guo, M. Long, X. Li, et al., Curcumin activates autophagy and attenuates oxidative damage in EA. hy926 cells via the Akt/mTOR pathway, Mol. Med. Rep. 13 (2016) 2187–2193.
DOI Google Scholar
[116]

T.F. Jiang, Y.J. Zhang, H.Y. Zhou, et al., Curcumin ameliorates the neurodegenerative pathology in A53T alpha-synuclein cell model of Parkinson's disease through the downregulation of mTOR/p70S6K signaling and the recovery of macroautophagy, J. Neuroimmune Pharmacol. 8 (2013) 356–369.
DOI Google Scholar
[117]

C. Wang, X. Zhang, Z. Teng, et al., Downregulation of PI3K/Akt/mTOR signaling pathway in curcumin-induced autophagy in APP/PS1 double transgenic mice, Eur. J. Pharmacol. 740 (2014) 312–320.
DOI Google Scholar
[118]

Q. Chen, G.G. Haddad, Role of trehalose phosphate synthase and trehalose during hypoxia: from flies to mammals, J. Exp. Biol. 207 (2004) 3125–3129.
DOI Google Scholar
[119]

S. Darabi, A. Noori-Zadeh, H.A. Abbaszadeh, F. Rajaei, Trehalose activates autophagy and prevents hydrogen peroxide-induced apoptosis in the bone marrow stromal cells, Iran. J. Pharm. Res. 17 (2018) 1141–1149.
Google Scholar
[120]

Q. Wang, J. Ren, mTOR-Independent autophagy inducer trehalose rescues against insulin resistance-induced myocardial contractile anomalies: role of p38 MAPK and Foxo1, Pharmacol. Res. 111 (2016) 357–373.
DOI Google Scholar
[121]

T.D. Evans, S.J. Jeong, X. Zhang, et al., TFEB and trehalose drive the macrophage autophagy-lysosome system to protect against atherosclerosis, Autophagy 14 (2018) 724–726.
DOI Google Scholar
[122]

A. Sahebkar, M. Hatamipour, S.A. Tabatabaei, Trehalose administration attenuates atherosclerosis in rabbits fed a high-fat diet, J. Cell. Biochem.
Google Scholar
[123]

S. Sciarretta, D. Yee, N. Nagarajan, et al., Trehalose-induced activation of autophagy improves cardiac remodeling after myocardial infarction, J. Am. Coll. Cardiol. 71 (2018) 1999–2010.
DOI Google Scholar
[124]

S. Sarkar, J.E. Davies, Z. Huang, et al., Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and alpha-synuclein, J. Biol. Chem. 282 (2007) 5641–5652.
DOI Google Scholar
[125]

J.A. Rodriguez-Navarro, L. Rodriguez, M.J. Casarejos, et al., Trehalose ameliorates dopaminergic and tau pathology in parkin deleted/tau overexpressing mice through autophagy activation, Neurobiol. Dis. 39 (2010) 423–438.
DOI Google Scholar
[126]

H.E. El-Horany, R.N. El-Latif, M.M. ElBatsh, M.N. Emam, Ameliorative effect of quercetin on neurochemical and behavioral deficits in rotenone rat model of Parkinson's disease: modulating autophagy (quercetin on experimental Parkinson's disease), J. Biochem. Mol. Toxicol. 30 (2016) 360–369.
DOI Google Scholar
[127]

X. Cui, Y. Luo, C. Li, et al., Changes of intracellular Ca2+ in quercetin-induced autophagy progression, Acta Biochim Biophys Sin (Shanghai) 47 (2015) 908–914.
DOI Google Scholar
[128]

L. Liu, C. Gao, P. Yao, Z. Gong, Quercetin alleviates high-fat diet-induced oxidized low-density lipoprotein accumulation in the liver: implication for autophagy regulation, Biomed Res. Int. 2015 (2015), 607531.
DOI Google Scholar
[129]

L. Shi, T. Zhang, Y. Zhou, et al., Dihydromyricetin improves skeletal muscle insulin sensitivity by inducing autophagy via the AMPK-PGC-1alpha-Sirt3 signaling pathway, Endocrine 50 (2015) 378–389.
DOI Google Scholar
[130]

B. Wu, J. Lin, J. Luo, et al., Dihydromyricetin protects against diabetic cardiomyopathy in streptozotocin-induced diabetic mice, Biomed Res. Int. 2017 (2017), 3764370.
DOI Google Scholar
[131]

J. Zhang, Y. Chen, H. Luo, et al., Recent update on the pharmacological effects and mechanisms of dihydromyricetin, Front. Pharmacol. 9 (2018) 1204.
DOI Google Scholar
[132]

X. Kou, J. Li, J. Bian, et al., Ampelopsin attenuates 6-OHDA-induced neurotoxicity by regulating GSK-3β/NRF2/ARE signalling, J. Funct. Foods 19 (2015) 765–774.
DOI Google Scholar
[133]

X. Kou, N. Chen, Pharmacological potential of ampelopsin in Rattan tea, Food Sci. Hum. Wellness 1 (2012) 14–18.
DOI Google Scholar
Publication history
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Acknowledgements
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Publication history

Received: 07 January 2019
Accepted: 01 March 2019
Published: 14 March 2019
Issue date: March 2019

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© 2019 “Society information”.

Acknowledgements

Acknowledgements

This work was financially supported by the National Natural Science Foundation of China (No. 31571228 and No. 31771318), Hubei Superior Discipline Groups of Physical Education and Health Promotion, and Outstanding Youth Scientific and Technological Innovation Team (T201624) from Hubei Provincial Department of Education, as well as Chutian Scholar Program and Innovative Startup Foundation from Wuhan Sports University to Ning Chen.

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This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

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