EGCG and stress reduction

The National Center for Complementary and Integrative Reduvtion NCCIH at Nutritional strategies for hypertension National Institute sress Health NIH notes that EGGC is Nutritional strategies for hypertension to consume up to 8 cups stdess green tea anv providing Body recomposition plan 1, mg EGCG. Spencer JPE. Activation of tyrosine kinase receptor signaling pathway by rasagiline facilitates neurorescue and restoration of nigrostriatal dopamine neurons in post-MPTP-induced parkinsonism. This finding is well aligned with the plethora of literature describing polyphenols as compounds targeting mitochondria [ 5354 ]. Jelinek, hjelinek csu. Article CAS PubMed Google Scholar Teixeira MDA, Souza CM, Menezes APF, Carmo MRS, Fonteles AA, Gurgel JP, et al. elegans after 6—12 h and the activity of complex I in isolated rodent mitochondria.

EGCG and stress reduction -
Rezai-Zadeh K, Shytle D, Sun N, Mori T, Hou H, Jeanniton D, et al. Green tea epigallocatechingallate EGCG modulates amyloid precursor protein cleavage and reduces cerebral amyloidosis in Alzheimer transgenic mice. Yeon J, Jeon S, Bae K, Song K, Hee Y.

Catechin and epicatechin from Smilacis chinae rhizome protect cultured rat cortical neurons against amyloid β protein 25 — 35 -induced neurotoxicity through inhibition of cytosolic calcium elevation.

Reznichenko L, Amit T, Youdim MBH, Mandel S. Green tea polyphenol - -epigallocatechingallate induces neurorescue of long-term serum-deprived PC12 cells and promotes neurite outgrowth. Sagi Y, Mandel S, Amit T, Youdim MBH. Activation of tyrosine kinase receptor signaling pathway by rasagiline facilitates neurorescue and restoration of nigrostriatal dopamine neurons in post-MPTP-induced parkinsonism.

Neurobiol Dis. Valko M, Leibfritz D, Moncol J, Cronin MT, Mazur M, Telser J. Free radicals and antioxidants in normal physiological functions and human disease. Int J Biochem Cell Biol. Zhu N, Huang TC, Yu Y, LaVoie EJ, Yang CS, Ho CT. Identification of oxidation products of - -epigallocatechin gallate and - -epigallocatechin with H2O2.

Zhao C, Li C, Liu S, Yang L. The galloyl catechins contributing to main antioxidant capacity of tea made from Camellia sinensis in China. Sci World J. Google Scholar. Young Park S, Jeong YJ, Kim SH, Jung JY, Kim WJ. Epigallocatechin gallate protects against nitric oxide-induced apoptosis via scavenging ROS and modulating the Bcl-2 family in human dental pulp cells.

J Toxicol Sci. Sato M, Toyazaki H, Yoshioka Y, Yokoi N, Yamasaki T. Structural characteristics for superoxide anion radical scavenging and productive activities of green tea polyphenols including proanthocyanidin dimers.

Chem Pharm Bull Tokyo. Weinreb O, Amit T, Mandel S, Youdim MBH. Neuroprotective molecular mechanisms of - -epigallocatechingallate: A reflective outcome of its antioxidant, iron chelating and neuritogenic properties.

Genes Nutr. Anderson RF, Fisher LJ, Hara Y, Harris T, Mak WB, Melton LD, et al. Green tea catechins partially protect DNA from. OH radical-induced strand breaks and base damage through fast chemical repair of DNA radicals. Guo Q, Zhao B, Li M, Shen S, Wenjuan X. Studies on protective mechanisms of four components of green tea polyphenols against lipid peroxidation in synaptosomes.

Biochim Biophys Acta - Lipids Lipid Metab. Devika PT, Stanely Mainzen Prince P. Protective effect of - -epigallocatechin-gallate EGCG on lipid peroxide metabolism in isoproterenol induced myocardial infarction in male Wistar rats: A histopathological study.

Biomed Pharmacother. Jelenković A, Jovanović MD, Stevanović I, Petronijević N, Bokonjić D, Živković J, et al. Influence of the green tea leaf extract on neurotoxicity of aluminium chloride in rats. Phyther Res. Srividhya R, Jyothilakshmi V, Arulmathi K, Senthilkumaran V, Kalaiselvi P.

Attenuation of senescence-induced oxidative exacerbations in aged rat brain by - -epigallocatechingallate. Int J Dev Neurosci.

Erba D, Riso P, Bordoni A, Foti P, Biagi PL, Testolin G. Effectiveness of moderate green tea consumption on antioxidative status and plasma lipid profile in humans. Panza VSP, Wazlawik E, Ricardo Schütz G, Comin L, Hecht KC, da Silva EL.

Consumption of green tea favorably affects oxidative stress markers in weight-trained men. Sartor L, Pezzato E, Garbisa S. J Leukoc Biol. Neutrophil restraint by green tea: inhibition of inflammation, associated angiogenesis, and pulmonary fibrosis.

Yeoh BS, Aguilera Olvera R, Singh V, Xiao X, Kennett MJ, Joe B, et al. Epigallocatechingallate inhibition of myeloperoxidase and its counter-regulation by dietary iron and lipocalin 2 in murine model of gut inflammation.

Am J Pathol. Urrutia PJ, Mena NP, Núñez MT. The interplay between iron accumulation, mitochondrial dysfunction, and inflammation during the execution step of neurodegenerative disorders.

Front Pharmacol. Amit T, Avramovich-Tirosh Y, Youdim MBH, Mandel S. Berg D. In vivo detection of iron and neuromelanin by transcranial sonography - A new approach for early detection of substantia nigra damage. J Neural Transm. Mochizuki H, Yasuda T. Collingwood JF. J Qual Res Dement.

Avramovich-Tirosh Y, Reznichenko L, Mit T, Zheng H, Fridkin M, Weinreb O, et al. Neurorescue activity, APP regulation and amyloid-beta peptide reduction by novel multi-functional brain permeable iron- chelating- antioxidants, M and green tea polyphenol, EGCG. Curr Alzheimer Res.

Li J, Ye L, Wang X, Liu J, Wang Y, Zhou Y, et al. Ryan P, Hynes MJ. The kinetics and mechanisms of the complex formation and antioxidant behaviour of the polyphenols EGCg and ECG with iron III. J Inorg Biochem. Bao GH, Xu J, Hu FL, Wan XC, Deng SX, Barasch J. EGCG inhibit chemical reactivity of iron through forming an Ngal-EGCG-iron complex.

Saffari Y, Sadrzadeh SMH. Green tea metabolite EGCG protects membranes against oxidative damage in vitro. Teixeira MDA, Souza CM, Menezes APF, Carmo MRS, Fonteles AA, Gurgel JP, et al. Catechin attenuates behavioral neurotoxicity induced by 6-OHDA in rats.

Pharmacol Biochem Behav. Lee SR, Im KJ, Suh SI, Jung JG. Protective effect of green tea polyphenol - -epigallocatechin gallate and other antioxidants on lipid peroxidation in gerbil brain homogenates. Chen M-H, Tsai C-F, Hsu Y-W, Lu F-J. Epigallocatechin gallate eye drops protect against ultraviolet B-induced corneal oxidative damage in mice.

Chen W, Hsieh S, Chiu C, Hsu B, Liou Y. Molecular identification for epigallocatechin gallate-mediated antioxidant intervention on the H 2 O 2 -induced oxidative stress in H9c2 rat cardiomyoblasts.

J Biomed Sci. Jeong JH, Kim HJ, Lee TJ, Kim MK, Park ES, Choi BS. Epigallocatechin 3-gallate attenuates neuronal damage induced by 3-hydroxykynurenine.

Dobrzynska I, Sniecinska A, Skrzydlewska E, Figaszewski Z. Green tea modulation of the biochemical and electric properties of rat liver cells that were affected by ethanol and aging. Cell Mol Biol Lett. PubMed Google Scholar. Ostrowska J, Łuczaj W, Kasacka I, Rózański A, Skrzydlewska E.

Green tea protects against ethanol-induced lipid peroxidation in rat organs. Kennedy DO. 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. de Barry J, Liégeois CM, Janoshazi A. Article PubMed CAS Google Scholar. Vianna MRM, Barros DM, Silva T, Choi H, Madche C, Rodrigues C, et al.

Pharmacological demonstration of the differential involvement of protein kinase C isoforms in short- and long-term memory formation and retrieval of one-trial avoidance in rats.

Psychopharmacology Berl. Sun MK, Alkon DL. Prog Mol Biol Transl Sci. Activation of protein kinase C isozymes for the treatment of dementias.

Adv Pharmacol. Pascale A, Amadio M, Govoni S, Battaini F. The aging brain, a key target for the future: The protein kinase C involvement. Pharmacol Res. Mansuri ML, Parihar P, Solanki I, Parihar MS. Flavonoids in modulation of cell survival signalling pathways.

Mehta KD. Emerging role of protein kinase C in energy homeostasis: A brief overview. World J Diabetes. Newton AC. Regulation of the ABC kinases by phosphorylation: protein kinase C as a paradigm. Biochem J. Kim SY, Ahn BH, Kim J, Bae YS, Kwak JY, Min G, et al.

Eur J Biochem. Mandel S, Weinreb O, Amit T, Youdim MBH. Cell signaling pathways in the neuroprotective actions of the green tea polyphenol - -epigallocatechingallate: implications for neurodegenerative diseases. Mandel SA, Amit T, Kalfon L, Reznichenko L, Youdim MBH. Targeting multiple neurodegenerative diseases etiologies with multimodal-acting green tea catechins.

Vasilevko V, Cribbs DH. Neurochem Int. Nunan J, Small DH. Regulation of APP cleavage by alpha-, beta- and gamma-secretases [Review].

Reznichenko L, Amit T, Zheng H, Avramovich-Tirosh Y, Youdim MBH, Weinreb O, et al. Choi D-S, Wang D, Yu G-Q, Zhu G, Kharazia VN, Paredes JP, et al. PKCepsilon increases endothelin converting enzyme activity and reduces amyloid plaque pathology in transgenic mice.

Proc Natl Acad Sci U S A. Li R, Peng N, Li XP, Le WD. Lu H, Meng X, Yang CS. Enzymology of methylation of tea catechins and inhibition of catechol- o -methyltransferase by - -epigallocatechin gallate. Drug Metab Dispos.

Hommes DW, Peppelenbosch MP, van Deventer SJH. Mitogen activated protein MAP kinase signal transduction pathways and novel anti-inflammatory targets. Johnson GL, Lapadat R. Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases.

Vauzour D, Vafeiadou K, Rice-Evans C, Williams RJ, Spencer JPE. Behrens a, Sibilia M, Wagner EF. Amino-terminal phosphorylation of c-Jun regulates stress-induced apoptosis and cellular proliferation. Nat Genet. Spencer JPE. The interactions of flavonoids within neuronal signalling pathways.

Arany I, Megyesi JK, Reusch JEB, Safirstein RL. CREB mediates ERK-induced survival of mouse renal tubular cells after oxidant stress. Kidney Int. Ah Kang K, Wang ZH, Zhang R, Piao MJ, Kim KC, Kang SS, et al.

Int J Mol Sci. Davis RJ. Signal transduction by the JNK group of MAP kinases. Hollenbach E, Vieth M, Roessner A, Neumann M, Malfertheiner P, Naumann M. Schroeter H, Bahia P, Spencer JPE, Sheppard O, Rattray M, Cadenas E, et al.

Huang CC, Wu WB, Fang JY, Chiang HS, Chen SK, Chen BH, et al. Chang CW, Hsieh YH, Yang WE, Yang SF, Chen Y, Hu DN. Biomed Res Int. Haegeman G, Goya L, Bravo L, Ramos S, Novais A. Br J Nutr. Na HK, Kim EH, Jung JH, Lee HH, Hyun JW, Surh YJ. Singer CA, Figueroa-Masot XA, Batchelor RH, Dorsa DM.

The mitogen-activated protein kinase pathway mediates estrogen neuroprotection after glutamate toxicity in primary cortical neurons. Jiménez C, Hernández C, Pimentel B, Carrera AC. The p85 regulatory subunit controls sequential activation of phosphoinositide 3-kinase by Tyr kinases and Ras.

Brazil DP, Hemmings BA. Ten years of protein kinase B signalling: A hard Akt to follow. Trends Biochem Sci. Song G, Ouyang G, Bao S. J Cell Mol Med. Kennedy SG, Wagner AJ, Conzen SD, Jordán J, Bellacosa A, Tsichlis PN, et al.

Genes Dev. Simpson L, Parsons R. PTEN: life as a tumor suppressor. Exp Cell Res. Neri LM, Borgatti P, Capitani S, Martelli AM. Biochim Biophys Acta - Mol Cell Biol Lipids.

Meske V, Albert F, Ohm TG. Coupling of mammalian target of rapamycin with phosphoinositide 3-kinase signaling pathway regulates protein phosphatase 2A- and glycogen synthase kinase-3 -dependent phosphorylation of Tau.

Paquet D, Bhat R, Sydow A, Mandelkow EM, Berg S, Hellberg S, et al. A zebrafish model of tauopathy allows in vivo imaging of neuronal cell death and drug evaluation. J Clin Invest. Available from: ISI Shen X, Zhang Y, Feng Y, Zhang L, Li J, Xie YA, et al.

Epigallocatechingallate inhibits cell growth, induces apoptosis and causes S phase arrest in hepatocellular carcinoma by suppressing the AKT pathway. Int J Oncol. Williams RJ, Spencer JPE.

Flavonoids, cognition, and dementia: Actions, mechanisms, and potential therapeutic utility for Alzheimer disease. Baptista FI, Henriques AG, Silva AMS, Wiltfang J, Da Cruz E Silva OAB. ACS Chem Neurosci. Koh SH, Kim SH, Kwon H, Park Y, Kim KS, Song CW, et al.

Mol Brain Res. Gassen M, Youdim M. Free radical scavengers: chemical concepts and clinical relevance. J Neural Transm Suppl. Mandel S, Grünblatt E, Riederer P, Gerlach M, Levites Y, Youdim MBH.

CNS Drugs. Weinreb O, Mandel S, Youdim MBH. Gene and protein expression profiles of anti- and pro-apoptotic actions of dopamine, R-apomorphine, green tea polyphenol - -epigallocatechinegallate, and melatonin.

Ann N Y Acad Sci. cDNA gene expression profile homology of antioxidants and their antiapoptotic and proapoptotic activities in human neuroblastoma cells. Beal MF, Rascol, Marek, Olanow, Kordower, Isacson, et al. Ann Neurol. Mattson MP, Kroemer G. Mitochondria in cell death: Novel targets for neuroprotection and cardioprotection.

Trends Mol Med. Masuda M, Suzui N, Weinstein IB. Effects of epigallocatechingallate on growth, epidermal growth factor receptor signaling pathways, gene expression, and chemosensitivity in human head and neck squamous cell carcinoma cell lines.

Clin Cancer Res. Hastak K, Gupta S, Ahmad N, Agarwal MK, Agarwal ML, Mukhtar H. Role of p53 and NF-kappaB in epigallocatechingallate-induced apoptosis of LNCaP cells. Hofmann CS, Sonenshein GE. Green tea polyphenol epigallocatechin-3 gallate induces apoptosis of proliferating vascular smooth muscle cells via activation of p FASEB J Off Publ Fed Am Soc Exp Biol.

Pool H, Quintanar D, Figueroa JDD, Marinho Mano C, Bechara JEH, Godínez L a. Antioxidant Effects of Quercetin and Catechin Encapsulated into PLGA Nanoparticles. J Nanomater. Wu TH, Yen FL, Lin LT, Tsai TR, Lin CC, Cham TM. Preparation, physicochemical characterization, and antioxidant effects of quercetin nanoparticles.

Int J Pharm. Pardeshi C, Rajput P, Belgamwar V, Tekade A, Patil G, Chaudhary K, et al. Solid lipid based nanocarriers: an overview. Acta Pharm. Karikalan K, Mandal AK. Bioreduction of gold metal to nanoparticles by tea Camellia sinensis plant extracts.

J Plant Crop. Prakash RT, Mandal AKA. Effect of alcohol on release of green tea polyphenols from casein nanoparticles and its mathematical modeling. Res J Biotechnol. Karikalan K, Kaur G, Mandal A. Int J tea Sci. Xu Z, Chen S, Li X, Luo G, Li L, Le W. Kang KS, Wen Y, Yamabe N, Fukui M, Bishop SC, Zhu BT.

Chen CM, Lin JK, Liu, SH, Lin-Shiau SY. Novel regimen through com- bination of memantine and tea polyphenol for neuroprotection against brain excitotoxicity. J Neurosci Res. Chang-Mu C, Jen-Kun L, Shing-Hwa L, Shoei-Yn LS. Characterization of neurotoxic effects of NMDA and the novel neuroprotection by phytopolyphenols in mice.

Behav Neurosci. Kim SJ, Jeong HJ, Lee KM, Myung NY, An NH, Yang WM, Park SK, Lee HJ, Hong SH, Kim HM, Um JY. Epigallocatechingallate suppresses NF-kappaB activation and phosphorylation of p38 MAPK and JNK in human astrocytoma UMG cells.

Weinreb O, Amit T, Youdim MB. Levites Y, Amit T, Mandel S, Youdim MB. Bieschke J, Russ J, Friedrich RP, Ehrnhoefer DE, Wobst H, Neugebauer K, Wanker EE. EGCG remodels mature alpha-synuclein and amyloid-beta fibrils and reduces cellular toxicity.

Hudson SA, Ecroyd H, Dehle FC, Musgrave IF, Carver JA. J Mol Biol. Ehrnhoefer DE, Bieschke J, Boeddrich A, Herbst M, Masino L, Lurz R, Engemann S, Pastore A, Wanker EE. EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers.

Nat Struct Mol Biol. Obregon DF, Rezai-Zadeh K, Bai Y, Sun N, Hou H, Ehrhart J, Zeng J, Mori T, Arendash GW, Shytle D, Town T, Tan J. Lee JW, Lee YK, Ban JO, Ha TY, Yun YP, Han SB, Oh KW, Hong JT. Download references. Department of Integrative Biology, School of Biosciences and Technology, VIT University, Vellore, , Tamil Nadu, India.

Department of Biotechnology, School of Biosciences and Technology, VIT University, Vellore, , Tamil Nadu, India. Centre for Interdisciplinary Biomedical Research, Adesh University, Bathinda, Punjab, India. You can also search for this author in PubMed Google Scholar. Correspondence to Zaved Ahmed Khan.

NAS had designed and drafted the manuscript. AKM and ZAK had primary responsibility for the final content. All authors have read and approved the final manuscript. Open Access This article is distributed under the terms of the Creative Commons Attribution 4.

Reprints and permissions. Singh, N. Potential neuroprotective properties of epigallocatechingallate EGCG. Nutr J 15 , 60 Download citation. Received : 31 March Accepted : 02 June Published : 07 June Anyone you share the following link with will be able to read this content:. Sorry, a shareable link is not currently available for this article.

Provided by the Springer Nature SharedIt content-sharing initiative. Skip to main content. Search all BMC articles Search. Download PDF. Download ePub. Introduction Neurodegenerative diseases impose a significant social and economic burden. Full size image. Current status of knowledge Green tea polyphenols Green tea is a traditional drink made from Camellia sinesis plant, widely consumed in Asian countries [ 18 ].

Neuroprotective properties of EGCG Green tea polyphenols are known to possess neuroprotective and neurorescue action. Free radical scavenging and antioxidant action Reactive oxygen and nitrogen species such as nitrite oxide, superoxide and hydroxyl free radicals are naturally produced to assist the host system in defence against oxidative stress and inflammation triggered through pathogens and infectious agents.

Iron chelating activity Iron accumulation is one of the major pathologies of neurodegenerative diseases causing neuron death at the site of iron accumulation [ 96 ]. Lipid peroxidation EGCG has been reported to protect from lipid peroxidation and DNA deamination by guarding cells from the initiators of lipid peroxidation i.

Modulation of cell signalling pathways, cell survival and death genes EGCG protects not only through their antioxidant potential but also through the modulation of signalling pathways, cell survival and cell death genes.

Table 1 Neuroprotective effects of EGCG in in vitro and in vivo models of neurotoxicity Full size table. New treatment approach Although EGCG is a good candidate for a neuroprotective agent due to its ability to manipulate multiple desired targets, its use as a therapeutic agent is limited.

Conclusion The multi-etiological character of neurodegenerative diseases demands the need for the development of therapeutic agents capable of manipulating multiple desired targets. Article CAS PubMed PubMed Central Google Scholar Sheridan C. Article CAS PubMed Google Scholar Guo S, Bezard E, Zhao B.

Article CAS PubMed Google Scholar Weinreb O, Mandel S, Amit T, Youdim MBH. Article CAS PubMed Google Scholar Singh R, Akhtar N, Haqqi TM. Article Google Scholar Lambert JD, Elias RJ. Article CAS PubMed Google Scholar Unno K, Takabayashi F, Yoshida H, Choba D, Fukutomi R, Kikunaga N, et al.

Article CAS PubMed Google Scholar Schaffer S, Asseburg H, Kuntz S, Muller WE, Eckert GP. Article CAS PubMed Google Scholar Lim HJ, Shim SB, Jee SW, Lee SH, Lim CJ, Hong JT, et al. Article CAS PubMed Google Scholar Levites Y, Amit T, Youdim MBH, Mandel S.

Article CAS PubMed Google Scholar Mandel SA, Avramovich-Tirosh Y, Reznichenko L, Zheng H, Weinreb O, Amit T, et al. Article CAS PubMed Google Scholar Khokhar S, Magnusdottir SGM. Article CAS PubMed Google Scholar Nanjo F, Goto K, Seto R, Suzuki M, Sakai M, Hara Y.

Article CAS PubMed Google Scholar Khan N, Afaq F, Saleem M, Ahmad N, Mukhtar H. Article CAS PubMed PubMed Central Google Scholar Ritchie K, Lovestone S. CAS PubMed Google Scholar Kennedy DO, Wightman EL.

Article CAS PubMed PubMed Central Google Scholar Checkoway H, Powers K, Smith-Weller T, Franklin GM, Longstreth WT, Swanson PD. Article PubMed Google Scholar Li F-J, Ji H-F, Shen L. Article PubMed Google Scholar Gao X, Cassidy A, Schwarzschild MA, Rimm EB, Ascherio A. Article CAS PubMed PubMed Central Google Scholar Quintana JLB, Allam MF, Castillo AS, Navajas RF-C.

Article CAS Google Scholar Tan E-K, Tan C, Fook-Chong SMC, Lum SY, Chai A, Chung H, et al. Article PubMed Google Scholar Lee MJ, Wang ZY, Li H, Chen L, Sun Y, Gobbo S, et al.

CAS Google Scholar Nakagawa K, Okuda S, Miyazawa T. Article CAS PubMed Google Scholar Nie G, Cao Y, Zhao B.

Article PubMed Google Scholar Grinberg LN, Newmark H, Kitrossky N, Rahamim E, Chevion M, Rachmilewitz EA. Article CAS PubMed Google Scholar Solanki I, Parihar P, Mansuri ML, Parihar MS. Article CAS PubMed PubMed Central Google Scholar Abd El Mohsen MM, Kuhnle G, Rechner AR, Schroeter H, Rose S, Jenner P, et al.

Article CAS PubMed Google Scholar Zhang B, Rusciano D, Osborne NN. Article CAS PubMed Google Scholar Stefanis L. Article PubMed PubMed Central CAS Google Scholar Bagad M, Chowdhury D, Khan ZA.

Article PubMed PubMed Central CAS Google Scholar Zhang H, Zhang Y-W, Chen Y, Huang X, Zhou F, Wang W, et al. Article CAS PubMed PubMed Central Google Scholar Mattson MP. Article PubMed PubMed Central Google Scholar Cavet ME, Harrington KL, Vollmer TR, Ward KW, Zhang J-Z.

CAS PubMed PubMed Central Google Scholar Li M-J, Yin Y-C, Wang J, Jiang Y-F. Article CAS PubMed PubMed Central Google Scholar Bahadoran Z, Mirmiran P, Azizi F.

Article CAS PubMed Google Scholar Okello EJ, Leylabi R, McDougall GJ. Article CAS PubMed Google Scholar Wobst HJ, Sharma A, Diamond MI, Wanker EE, Bieschke J. Article CAS PubMed Google Scholar Rezai-Zadeh K, Arendash GW, Hou H, Fernandez F, Jensen M, Runfeldt M, et al.

Article CAS PubMed Google Scholar Chesser AS, Ganeshan V, Yang J, Johnson GVW. CAS PubMed Google Scholar Agrawal M, Biswas A. Article CAS PubMed Google Scholar Zhang X, Wu M, Lu F, Luo N, He ZP, Yang H. CAS PubMed Google Scholar Han J, Wang M, Jing X, Shi H, Ren M, Lou H.

Article CAS PubMed Google Scholar Abib RT, Peres KC, Barbosa AM, Peres TV, Bernardes A, Zimmermann LM, et al. Article CAS PubMed Google Scholar Chao J, Lau WKW, Huie MJ, Ho YS, Yu MS, Lai CSW, et al. Article CAS PubMed Google Scholar Schroeder EK, Kelsey NA, Doyle J, Breed E, Bouchard RJ, Loucks FA, et al.

Article CAS PubMed Google Scholar Yu J, Jia Y, Guo Y, Chang G, Duan W, Sun M, et al. Article CAS PubMed Google Scholar Sutherland BA, Shaw OM, Clarkson AN, Jackson DN, Sammut IA, Appleton I.

CAS PubMed Google Scholar Herges K, Millward JM, Hentschel N, Infante-Duarte C, Aktas O, Zipp F. Article CAS PubMed Google Scholar Rezai-Zadeh K, Shytle D, Sun N, Mori T, Hou H, Jeanniton D, et al.

Article CAS PubMed Google Scholar Yeon J, Jeon S, Bae K, Song K, Hee Y. Article CAS Google Scholar Reznichenko L, Amit T, Youdim MBH, Mandel S. Article CAS PubMed Google Scholar Sagi Y, Mandel S, Amit T, Youdim MBH. Article CAS PubMed Google Scholar Valko M, Leibfritz D, Moncol J, Cronin MT, Mazur M, Telser J.

Article CAS PubMed Google Scholar Zhao C, Li C, Liu S, Yang L. Google Scholar Young Park S, Jeong YJ, Kim SH, Jung JY, Kim WJ.

Article CAS PubMed Google Scholar Guo Q, Zhao B, Li M, Shen S, Wenjuan X. Article CAS Google Scholar Devika PT, Stanely Mainzen Prince P. Article CAS PubMed Google Scholar Jelenković A, Jovanović MD, Stevanović I, Petronijević N, Bokonjić D, Živković J, et al.

Article CAS Google Scholar Srividhya R, Jyothilakshmi V, Arulmathi K, Senthilkumaran V, Kalaiselvi P. Article CAS PubMed Google Scholar Erba D, Riso P, Bordoni A, Foti P, Biagi PL, Testolin G. Article CAS PubMed Google Scholar Panza VSP, Wazlawik E, Ricardo Schütz G, Comin L, Hecht KC, da Silva EL.

Article CAS PubMed Google Scholar Sartor L, Pezzato E, Garbisa S. Article PubMed Google Scholar Yeoh BS, Aguilera Olvera R, Singh V, Xiao X, Kennett MJ, Joe B, et al. Article CAS Google Scholar Urrutia PJ, Mena NP, Núñez MT. Article CAS PubMed PubMed Central Google Scholar Berg D.

Article CAS PubMed Google Scholar Li J, Ye L, Wang X, Liu J, Wang Y, Zhou Y, et al. Article CAS PubMed Google Scholar Bao GH, Xu J, Hu FL, Wan XC, Deng SX, Barasch J. Article CAS PubMed PubMed Central Google Scholar Saffari Y, Sadrzadeh SMH. Article CAS PubMed Google Scholar Teixeira MDA, Souza CM, Menezes APF, Carmo MRS, Fonteles AA, Gurgel JP, et al.

Article CAS PubMed Google Scholar Lee SR, Im KJ, Suh SI, Jung JG. Article CAS Google Scholar Chen M-H, Tsai C-F, Hsu Y-W, Lu F-J. CAS PubMed PubMed Central Google Scholar Chen W, Hsieh S, Chiu C, Hsu B, Liou Y.

Article PubMed PubMed Central CAS Google Scholar Jeong JH, Kim HJ, Lee TJ, Kim MK, Park ES, Choi BS. Article CAS PubMed Google Scholar Dobrzynska I, Sniecinska A, Skrzydlewska E, Figaszewski Z. PubMed Google Scholar Ostrowska J, Łuczaj W, Kasacka I, Rózański A, Skrzydlewska E. Article CAS PubMed Google Scholar Kennedy DO.

Article PubMed CAS Google Scholar Vianna MRM, Barros DM, Silva T, Choi H, Madche C, Rodrigues C, et al. Article CAS Google Scholar Sun MK, Alkon DL. Article CAS PubMed Google Scholar Sun MK, Alkon DL. Article CAS PubMed Google Scholar Pascale A, Amadio M, Govoni S, Battaini F.

Article CAS PubMed Google Scholar Mansuri ML, Parihar P, Solanki I, Parihar MS. Article PubMed PubMed Central Google Scholar Newton AC.

Article CAS PubMed PubMed Central Google Scholar Kim SY, Ahn BH, Kim J, Bae YS, Kwak JY, Min G, et al. Article CAS PubMed Google Scholar Mandel SA, Amit T, Kalfon L, Reznichenko L, Youdim MBH. CAS PubMed Google Scholar Vasilevko V, Cribbs DH. Article CAS PubMed Google Scholar Nunan J, Small DH.

Article CAS PubMed Google Scholar Reznichenko L, Amit T, Zheng H, Avramovich-Tirosh Y, Youdim MBH, Weinreb O, et al. Article CAS PubMed Google Scholar Choi D-S, Wang D, Yu G-Q, Zhu G, Kharazia VN, Paredes JP, et al.

Article CAS PubMed PubMed Central Google Scholar Li R, Peng N, Li XP, Le WD. Article CAS PubMed Google Scholar Lu H, Meng X, Yang CS. Article CAS PubMed Google Scholar Hommes DW, Peppelenbosch MP, van Deventer SJH.

Article CAS PubMed PubMed Central Google Scholar Johnson GL, Lapadat R. Article CAS PubMed Google Scholar Vauzour D, Vafeiadou K, Rice-Evans C, Williams RJ, Spencer JPE. Article CAS PubMed Google Scholar Behrens a, Sibilia M, Wagner EF. Article PubMed Google Scholar Ah Kang K, Wang ZH, Zhang R, Piao MJ, Kim KC, Kang SS, et al.

Article CAS Google Scholar Davis RJ. Article CAS PubMed Google Scholar Hollenbach E, Vieth M, Roessner A, Neumann M, Malfertheiner P, Naumann M.

Article CAS PubMed Google Scholar Schroeter H, Bahia P, Spencer JPE, Sheppard O, Rattray M, Cadenas E, et al. Article CAS PubMed Google Scholar Huang CC, Wu WB, Fang JY, Chiang HS, Chen SK, Chen BH, et al. Article CAS PubMed Google Scholar Chang CW, Hsieh YH, Yang WE, Yang SF, Chen Y, Hu DN.

Google Scholar Na HK, Kim EH, Jung JH, Lee HH, Hyun JW, Surh YJ. CAS PubMed Google Scholar Jiménez C, Hernández C, Pimentel B, Carrera AC.

Article PubMed CAS Google Scholar Brazil DP, Hemmings BA. Article CAS PubMed Google Scholar Kennedy SG, Wagner AJ, Conzen SD, Jordán J, Bellacosa A, Tsichlis PN, et al. Article CAS PubMed Google Scholar Simpson L, Parsons R.

Article CAS PubMed Google Scholar Neri LM, Borgatti P, Capitani S, Martelli AM. CAS PubMed Google Scholar Williams RJ, Spencer JPE. Article CAS PubMed Google Scholar Gassen M, Youdim M. Article CAS PubMed Google Scholar Mandel S, Grünblatt E, Riederer P, Gerlach M, Levites Y, Youdim MBH.

CAS PubMed Google Scholar Beal MF, Rascol, Marek, Olanow, Kordower, Isacson, et al. CAS PubMed Google Scholar Hastak K, Gupta S, Ahmad N, Agarwal MK, Agarwal ML, Mukhtar H.

CAS Google Scholar Pool H, Quintanar D, Figueroa JDD, Marinho Mano C, Bechara JEH, Godínez L a. Article CAS PubMed Google Scholar Pardeshi C, Rajput P, Belgamwar V, Tekade A, Patil G, Chaudhary K, et al. Google Scholar Prakash RT, Mandal AKA.

CAS Google Scholar Karikalan K, Kaur G, Mandal A. Google Scholar Xu Z, Chen S, Li X, Luo G, Li L, Le W. Article CAS PubMed Google Scholar Chang-Mu C, Jen-Kun L, Shing-Hwa L, Shoei-Yn LS.

Article PubMed CAS Google Scholar Kim SJ, Jeong HJ, Lee KM, Myung NY, An NH, Yang WM, Park SK, Lee HJ, Hong SH, Kim HM, Um JY.

Article CAS PubMed Google Scholar Weinreb O, Amit T, Youdim MB. Formally known as epigallocatechin gallate, EGCG is a type of plant-based compound called catechin. Catechins may be further categorized into a larger group of plant compounds known as polyphenols 1.

EGCG and other related catechins act as potent antioxidants that may protect against cellular damage caused by free radicals 1. Free radicals are highly reactive particles formed in your body that can damage your cells when their numbers get too high. Eating foods high in antioxidants like catechins may help limit free radical damage.

Additionally, research suggests that catechins like EGCG may reduce inflammation and prevent certain chronic conditions, including heart disease, diabetes, and some cancers 1 , 2.

EGCG exists naturally in several plant-based foods but is also available as a dietary supplement usually sold in the form of an extract. EGCG is a type of plant compound called catechin. Research suggests that catechins like EGCG may play a role in protecting your cells from damage and preventing disease.

In fact, the numerous health benefits associated with drinking green tea are typically credited to its EGCG content 1. Though EGCG is predominantly found in green tea, it also exists in small amounts in other foods, such as 3 :. While EGCG is the most researched and potent catechin, other types like epicatechin, epigallocatechin, and epicatechin 3-gallate may offer similar benefits.

Plus, many of them are more widely available in the food supply 3 , 4. Red wine, dark chocolate, legumes, and most fruit are a few examples of foods that offer a hefty dose of health-promoting catechins 5.

EGCG is most prevalent in green tea but also found in smaller quantities in other types of tea, fruit, and some nuts. Other health-promoting catechins are plentiful in red wine, dark chocolate, legumes, and most fruit.

Test-tube, animal, and a few human studies indicate that EGCG provides numerous health benefits, including reduced inflammation, weight loss, and improved heart and brain health.

Ultimately, more research is needed to better understand how EGCG may be used as a preventative tool or treatment for disease, though current data is promising.

Free radicals are highly reactive particles that can cause damage to your cells. Excessive free radical production leads to oxidative stress. As an antioxidant, EGCG protects your cells from damage associated with oxidative stress and suppresses the activity of pro-inflammatory chemicals produced in your body, such as tumor necrosis factor-alpha TNF-alpha 6.

Stress and inflammation are linked to a variety of chronic illnesses, including cancer, diabetes, and heart disease. Thus, the anti-inflammatory and antioxidant effects of EGCG are thought to be one of the main reasons for its broad disease-preventing applications 1.

Research suggests that EGCG in green tea may support heart health by reducing blood pressure, cholesterol, and the accumulation of plaque in blood vessels — all major risk factors for heart disease 7 , 8.

In an 8-week study in 33 people, taking mg of EGCG-containing green tea extract daily resulted in a significant 4. A separate study in 56 people found significant reductions in blood pressure, cholesterol, and inflammatory markers in those taking a daily dose of mg of green tea extract over 3 months Though these results are encouraging, more research is needed to better understand how EGCG in green tea may reduce heart disease risk.

EGCG may also promote weight loss , especially when taken alongside the caffeine naturally found in green tea. Additional human studies have collectively found that taking — mg of EGCG together with 80— mg of caffeine for at least 12 weeks is linked to significant weight loss and reduction of body fat Still, changes in weight or body composition are not consistently seen when EGCG is taken without caffeine.

Early research suggests that EGCG in green tea may play a role in improving neurological cell function and preventing degenerative brain diseases. In some studies, EGCG injections significantly improved inflammation, as well as recovery and regeneration of neural cells in mice with spinal cord injuries 13 , However, the available data is inconsistent More research is needed to better understand whether EGCG may effectively prevent or treat degenerative brain diseases in humans.

EGCG in green tea may offer a variety of health benefits, such as reduced inflammation, weight loss, and the prevention of heart and brain diseases.

Still, more research on its effectiveness is needed. The reason for this is not completely understood, but it may be related to the fact that a lot of EGCG bypasses the small intestine too quickly and ends up being degraded by bacteria in the large intestine A single cup 8 ounces or ml of brewed green tea typically contains about 50— mg of EGCG.

Dosages used in scientific studies are often much higher, but exact amounts have been inconsistent 11 , Daily intakes equal to or above mg of EGCG per day increases the blood levels of transaminases, an indicator of liver damage One group of researchers suggested a safe intake level of mg of EGCG per day when ingested in solid supplemental form In fact, EGCG supplements have been associated with serious side effects, such as 16 :.

EGCG may also interfere with the absorption of some prescription medications, including certain types of cholesterol-lowering and antipsychotic drugs To ensure safety, always consult with your healthcare provider prior to starting a new dietary supplement. There is currently no clear dosage recommendation for EGCG, though mg daily for up to 4 weeks has been used safely in studies.

Thank you abd visiting nature. You are using a browser version redudtion limited support for CSS. To Nutritional strategies for hypertension snd best experience, we recommend you redyction EGCG and stress reduction more streas to date Body cleanse detox diets or turn reductiom compatibility mode in Internet Explorer. In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript. For centuries, people across the globe have testified to the relaxing and invigorating qualities of tea. The traditional calming effects of the plant Camellia sinensis have elevated the drink, which is produced from its leaves, to a role beyond quenching thirst — it is drunk as an aid for meditation, to help soothe the nerves or simply to unwind. But although the mental-health benefits of C.

The aim Cognitive function boosting strategies the present study was to dtress the effects of EGCG rexuction EGCG and stress reduction stdess brain under an abd stressful condition and to clarify the mechanism by which EGCG attenuates stress behavior with reductiln reference to Nutritional strategies for hypertension acid GABA.

Intracerebroventricular Optimal eating schedule. Nutritional strategies for hypertension of Stgess 50, and microg Nutritional strategies for hypertension the vocalization Nutrition for endurance athletes normally occurs during social separation stress.

EGCG decreased the time spent in active wakefulness and induced sleep-like behavior in a dose-dependent manner. Additionally, i. injection of EGCG attenuated plasma corticosterone release under social separation stress.

These effects of EGCG on distress-induced vocalization were significantly attenuated by the GABAA receptor antagonist picrotoxin but not by the GABAB receptor antagonist CGP 3-N- 1- 3,4-dichlorophenyl ethylamino hydroxypropyl cyclohexylmethyl phosphinic acid hydrochloride.

These results indicate that EGCG has sedative and hypnotic effects in the brain, partially through GABAA receptors, and consequently moderates an acute stress response.

Abstract - -Epigallocatechin gallate EGCGa flavonoid, is the principal catechin found in green tea and is distributed in the brain after tea consumption.

Publication types Research Support, Non-U. Substances Antioxidants GABA Antagonists GABA-B Receptor Antagonists Organophosphorus Compounds Receptors, GABA-B Picrotoxin CGP Catechin epigallocatechin gallate Corticosterone.
: EGCG and stress reduction

EGCG (Epigallocatechin Gallate): Benefits, Dosage, and Safety	BDNF is a brain protein that contributes to the survival, development, and maintenance of neurons and is involved in several learning and memory functions [ 11 ]. Epigallocatechin Gallate in Progressive MS: A Randomized, Placebo-Controlled Trial. A significant main effect of time was found for the decrease in immediate stress score 0. In an 8-week study in 33 people, taking mg of EGCG-containing green tea extract daily resulted in a significant 4. All authors discussed and contributed to the interpretation of the results of the research and writing of the paper. A 10 min baseline supine ECG was then conducted. Oral absorption and absolute bioavailability of green tea catechins are low in mammals [ 12 ], reaching total maximum plasma concentrations of 2.
Publication types	Sagi Y, Mandel S, Amit T, Youdim MBH. Activation of tyrosine kinase receptor signaling pathway by rasagiline facilitates neurorescue and restoration of nigrostriatal dopamine neurons in post-MPTP-induced parkinsonism. Neurobiol Dis. Valko M, Leibfritz D, Moncol J, Cronin MT, Mazur M, Telser J. Free radicals and antioxidants in normal physiological functions and human disease. Int J Biochem Cell Biol. Zhu N, Huang TC, Yu Y, LaVoie EJ, Yang CS, Ho CT. Identification of oxidation products of - -epigallocatechin gallate and - -epigallocatechin with H2O2. Zhao C, Li C, Liu S, Yang L. The galloyl catechins contributing to main antioxidant capacity of tea made from Camellia sinensis in China. Sci World J. Google Scholar. Young Park S, Jeong YJ, Kim SH, Jung JY, Kim WJ. Epigallocatechin gallate protects against nitric oxide-induced apoptosis via scavenging ROS and modulating the Bcl-2 family in human dental pulp cells. J Toxicol Sci. Sato M, Toyazaki H, Yoshioka Y, Yokoi N, Yamasaki T. Structural characteristics for superoxide anion radical scavenging and productive activities of green tea polyphenols including proanthocyanidin dimers. Chem Pharm Bull Tokyo. Weinreb O, Amit T, Mandel S, Youdim MBH. Neuroprotective molecular mechanisms of - -epigallocatechingallate: A reflective outcome of its antioxidant, iron chelating and neuritogenic properties. Genes Nutr. Anderson RF, Fisher LJ, Hara Y, Harris T, Mak WB, Melton LD, et al. Green tea catechins partially protect DNA from. OH radical-induced strand breaks and base damage through fast chemical repair of DNA radicals. Guo Q, Zhao B, Li M, Shen S, Wenjuan X. Studies on protective mechanisms of four components of green tea polyphenols against lipid peroxidation in synaptosomes. Biochim Biophys Acta - Lipids Lipid Metab. Devika PT, Stanely Mainzen Prince P. Protective effect of - -epigallocatechin-gallate EGCG on lipid peroxide metabolism in isoproterenol induced myocardial infarction in male Wistar rats: A histopathological study. Biomed Pharmacother. Jelenković A, Jovanović MD, Stevanović I, Petronijević N, Bokonjić D, Živković J, et al. Influence of the green tea leaf extract on neurotoxicity of aluminium chloride in rats. Phyther Res. Srividhya R, Jyothilakshmi V, Arulmathi K, Senthilkumaran V, Kalaiselvi P. Attenuation of senescence-induced oxidative exacerbations in aged rat brain by - -epigallocatechingallate. Int J Dev Neurosci. Erba D, Riso P, Bordoni A, Foti P, Biagi PL, Testolin G. Effectiveness of moderate green tea consumption on antioxidative status and plasma lipid profile in humans. Panza VSP, Wazlawik E, Ricardo Schütz G, Comin L, Hecht KC, da Silva EL. Consumption of green tea favorably affects oxidative stress markers in weight-trained men. Sartor L, Pezzato E, Garbisa S. J Leukoc Biol. Neutrophil restraint by green tea: inhibition of inflammation, associated angiogenesis, and pulmonary fibrosis. Yeoh BS, Aguilera Olvera R, Singh V, Xiao X, Kennett MJ, Joe B, et al. Epigallocatechingallate inhibition of myeloperoxidase and its counter-regulation by dietary iron and lipocalin 2 in murine model of gut inflammation. Am J Pathol. Urrutia PJ, Mena NP, Núñez MT. The interplay between iron accumulation, mitochondrial dysfunction, and inflammation during the execution step of neurodegenerative disorders. Front Pharmacol. Amit T, Avramovich-Tirosh Y, Youdim MBH, Mandel S. Berg D. In vivo detection of iron and neuromelanin by transcranial sonography - A new approach for early detection of substantia nigra damage. J Neural Transm. Mochizuki H, Yasuda T. Collingwood JF. J Qual Res Dement. Avramovich-Tirosh Y, Reznichenko L, Mit T, Zheng H, Fridkin M, Weinreb O, et al. Neurorescue activity, APP regulation and amyloid-beta peptide reduction by novel multi-functional brain permeable iron- chelating- antioxidants, M and green tea polyphenol, EGCG. Curr Alzheimer Res. Li J, Ye L, Wang X, Liu J, Wang Y, Zhou Y, et al. Ryan P, Hynes MJ. The kinetics and mechanisms of the complex formation and antioxidant behaviour of the polyphenols EGCg and ECG with iron III. J Inorg Biochem. Bao GH, Xu J, Hu FL, Wan XC, Deng SX, Barasch J. EGCG inhibit chemical reactivity of iron through forming an Ngal-EGCG-iron complex. Saffari Y, Sadrzadeh SMH. Green tea metabolite EGCG protects membranes against oxidative damage in vitro. Teixeira MDA, Souza CM, Menezes APF, Carmo MRS, Fonteles AA, Gurgel JP, et al. Catechin attenuates behavioral neurotoxicity induced by 6-OHDA in rats. Pharmacol Biochem Behav. Lee SR, Im KJ, Suh SI, Jung JG. Protective effect of green tea polyphenol - -epigallocatechin gallate and other antioxidants on lipid peroxidation in gerbil brain homogenates. Chen M-H, Tsai C-F, Hsu Y-W, Lu F-J. Epigallocatechin gallate eye drops protect against ultraviolet B-induced corneal oxidative damage in mice. Chen W, Hsieh S, Chiu C, Hsu B, Liou Y. Molecular identification for epigallocatechin gallate-mediated antioxidant intervention on the H 2 O 2 -induced oxidative stress in H9c2 rat cardiomyoblasts. J Biomed Sci. Jeong JH, Kim HJ, Lee TJ, Kim MK, Park ES, Choi BS. Epigallocatechin 3-gallate attenuates neuronal damage induced by 3-hydroxykynurenine. Dobrzynska I, Sniecinska A, Skrzydlewska E, Figaszewski Z. Green tea modulation of the biochemical and electric properties of rat liver cells that were affected by ethanol and aging. Cell Mol Biol Lett. PubMed Google Scholar. Ostrowska J, Łuczaj W, Kasacka I, Rózański A, Skrzydlewska E. Green tea protects against ethanol-induced lipid peroxidation in rat organs. Kennedy DO. 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. de Barry J, Liégeois CM, Janoshazi A. Article PubMed CAS Google Scholar. Vianna MRM, Barros DM, Silva T, Choi H, Madche C, Rodrigues C, et al. Pharmacological demonstration of the differential involvement of protein kinase C isoforms in short- and long-term memory formation and retrieval of one-trial avoidance in rats. Psychopharmacology Berl. Sun MK, Alkon DL. Prog Mol Biol Transl Sci. Activation of protein kinase C isozymes for the treatment of dementias. Adv Pharmacol. Pascale A, Amadio M, Govoni S, Battaini F. The aging brain, a key target for the future: The protein kinase C involvement. Pharmacol Res. Mansuri ML, Parihar P, Solanki I, Parihar MS. Flavonoids in modulation of cell survival signalling pathways. Mehta KD. Emerging role of protein kinase C in energy homeostasis: A brief overview. World J Diabetes. Newton AC. Regulation of the ABC kinases by phosphorylation: protein kinase C as a paradigm. Biochem J. Kim SY, Ahn BH, Kim J, Bae YS, Kwak JY, Min G, et al. Eur J Biochem. Mandel S, Weinreb O, Amit T, Youdim MBH. Cell signaling pathways in the neuroprotective actions of the green tea polyphenol - -epigallocatechingallate: implications for neurodegenerative diseases. Mandel SA, Amit T, Kalfon L, Reznichenko L, Youdim MBH. Targeting multiple neurodegenerative diseases etiologies with multimodal-acting green tea catechins. Vasilevko V, Cribbs DH. Neurochem Int. Nunan J, Small DH. Regulation of APP cleavage by alpha-, beta- and gamma-secretases [Review]. Reznichenko L, Amit T, Zheng H, Avramovich-Tirosh Y, Youdim MBH, Weinreb O, et al. Choi D-S, Wang D, Yu G-Q, Zhu G, Kharazia VN, Paredes JP, et al. PKCepsilon increases endothelin converting enzyme activity and reduces amyloid plaque pathology in transgenic mice. Proc Natl Acad Sci U S A. Li R, Peng N, Li XP, Le WD. Lu H, Meng X, Yang CS. Enzymology of methylation of tea catechins and inhibition of catechol- o -methyltransferase by - -epigallocatechin gallate. Drug Metab Dispos. Hommes DW, Peppelenbosch MP, van Deventer SJH. Mitogen activated protein MAP kinase signal transduction pathways and novel anti-inflammatory targets. Johnson GL, Lapadat R. Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases. Vauzour D, Vafeiadou K, Rice-Evans C, Williams RJ, Spencer JPE. Behrens a, Sibilia M, Wagner EF. Amino-terminal phosphorylation of c-Jun regulates stress-induced apoptosis and cellular proliferation. Nat Genet. Spencer JPE. The interactions of flavonoids within neuronal signalling pathways. Arany I, Megyesi JK, Reusch JEB, Safirstein RL. CREB mediates ERK-induced survival of mouse renal tubular cells after oxidant stress. Kidney Int. Ah Kang K, Wang ZH, Zhang R, Piao MJ, Kim KC, Kang SS, et al. Int J Mol Sci. Davis RJ. Signal transduction by the JNK group of MAP kinases. Hollenbach E, Vieth M, Roessner A, Neumann M, Malfertheiner P, Naumann M. Schroeter H, Bahia P, Spencer JPE, Sheppard O, Rattray M, Cadenas E, et al. Huang CC, Wu WB, Fang JY, Chiang HS, Chen SK, Chen BH, et al. Chang CW, Hsieh YH, Yang WE, Yang SF, Chen Y, Hu DN. Biomed Res Int. Haegeman G, Goya L, Bravo L, Ramos S, Novais A. Br J Nutr. Na HK, Kim EH, Jung JH, Lee HH, Hyun JW, Surh YJ. Singer CA, Figueroa-Masot XA, Batchelor RH, Dorsa DM. The mitogen-activated protein kinase pathway mediates estrogen neuroprotection after glutamate toxicity in primary cortical neurons. Jiménez C, Hernández C, Pimentel B, Carrera AC. The p85 regulatory subunit controls sequential activation of phosphoinositide 3-kinase by Tyr kinases and Ras. Brazil DP, Hemmings BA. Ten years of protein kinase B signalling: A hard Akt to follow. Trends Biochem Sci. Song G, Ouyang G, Bao S. J Cell Mol Med. Kennedy SG, Wagner AJ, Conzen SD, Jordán J, Bellacosa A, Tsichlis PN, et al. Genes Dev. Simpson L, Parsons R. PTEN: life as a tumor suppressor. Exp Cell Res. Neri LM, Borgatti P, Capitani S, Martelli AM. Biochim Biophys Acta - Mol Cell Biol Lipids. Meske V, Albert F, Ohm TG. Coupling of mammalian target of rapamycin with phosphoinositide 3-kinase signaling pathway regulates protein phosphatase 2A- and glycogen synthase kinase-3 -dependent phosphorylation of Tau. Paquet D, Bhat R, Sydow A, Mandelkow EM, Berg S, Hellberg S, et al. A zebrafish model of tauopathy allows in vivo imaging of neuronal cell death and drug evaluation. J Clin Invest. Available from: ISI Shen X, Zhang Y, Feng Y, Zhang L, Li J, Xie YA, et al. Epigallocatechingallate inhibits cell growth, induces apoptosis and causes S phase arrest in hepatocellular carcinoma by suppressing the AKT pathway. Int J Oncol. Williams RJ, Spencer JPE. Flavonoids, cognition, and dementia: Actions, mechanisms, and potential therapeutic utility for Alzheimer disease. Baptista FI, Henriques AG, Silva AMS, Wiltfang J, Da Cruz E Silva OAB. ACS Chem Neurosci. Koh SH, Kim SH, Kwon H, Park Y, Kim KS, Song CW, et al. Mol Brain Res. Gassen M, Youdim M. Free radical scavengers: chemical concepts and clinical relevance. J Neural Transm Suppl. Mandel S, Grünblatt E, Riederer P, Gerlach M, Levites Y, Youdim MBH. CNS Drugs. Weinreb O, Mandel S, Youdim MBH. Gene and protein expression profiles of anti- and pro-apoptotic actions of dopamine, R-apomorphine, green tea polyphenol - -epigallocatechinegallate, and melatonin. Ann N Y Acad Sci. cDNA gene expression profile homology of antioxidants and their antiapoptotic and proapoptotic activities in human neuroblastoma cells. Beal MF, Rascol, Marek, Olanow, Kordower, Isacson, et al. Ann Neurol. Mattson MP, Kroemer G. Mitochondria in cell death: Novel targets for neuroprotection and cardioprotection. Trends Mol Med. Masuda M, Suzui N, Weinstein IB. Effects of epigallocatechingallate on growth, epidermal growth factor receptor signaling pathways, gene expression, and chemosensitivity in human head and neck squamous cell carcinoma cell lines. Clin Cancer Res. Hastak K, Gupta S, Ahmad N, Agarwal MK, Agarwal ML, Mukhtar H. Role of p53 and NF-kappaB in epigallocatechingallate-induced apoptosis of LNCaP cells. Hofmann CS, Sonenshein GE. Green tea polyphenol epigallocatechin-3 gallate induces apoptosis of proliferating vascular smooth muscle cells via activation of p FASEB J Off Publ Fed Am Soc Exp Biol. Pool H, Quintanar D, Figueroa JDD, Marinho Mano C, Bechara JEH, Godínez L a. Antioxidant Effects of Quercetin and Catechin Encapsulated into PLGA Nanoparticles. J Nanomater. Wu TH, Yen FL, Lin LT, Tsai TR, Lin CC, Cham TM. Preparation, physicochemical characterization, and antioxidant effects of quercetin nanoparticles. Int J Pharm. Pardeshi C, Rajput P, Belgamwar V, Tekade A, Patil G, Chaudhary K, et al. Solid lipid based nanocarriers: an overview. Acta Pharm. Karikalan K, Mandal AK. Bioreduction of gold metal to nanoparticles by tea Camellia sinensis plant extracts. J Plant Crop. Prakash RT, Mandal AKA. Effect of alcohol on release of green tea polyphenols from casein nanoparticles and its mathematical modeling. Res J Biotechnol. Karikalan K, Kaur G, Mandal A. Int J tea Sci. Xu Z, Chen S, Li X, Luo G, Li L, Le W. Kang KS, Wen Y, Yamabe N, Fukui M, Bishop SC, Zhu BT. Chen CM, Lin JK, Liu, SH, Lin-Shiau SY. Novel regimen through com- bination of memantine and tea polyphenol for neuroprotection against brain excitotoxicity. J Neurosci Res. Chang-Mu C, Jen-Kun L, Shing-Hwa L, Shoei-Yn LS. Characterization of neurotoxic effects of NMDA and the novel neuroprotection by phytopolyphenols in mice. Behav Neurosci. Kim SJ, Jeong HJ, Lee KM, Myung NY, An NH, Yang WM, Park SK, Lee HJ, Hong SH, Kim HM, Um JY. Epigallocatechingallate suppresses NF-kappaB activation and phosphorylation of p38 MAPK and JNK in human astrocytoma UMG cells. Weinreb O, Amit T, Youdim MB. Levites Y, Amit T, Mandel S, Youdim MB. Bieschke J, Russ J, Friedrich RP, Ehrnhoefer DE, Wobst H, Neugebauer K, Wanker EE. EGCG remodels mature alpha-synuclein and amyloid-beta fibrils and reduces cellular toxicity. Hudson SA, Ecroyd H, Dehle FC, Musgrave IF, Carver JA. J Mol Biol. Ehrnhoefer DE, Bieschke J, Boeddrich A, Herbst M, Masino L, Lurz R, Engemann S, Pastore A, Wanker EE. EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers. Nat Struct Mol Biol. Obregon DF, Rezai-Zadeh K, Bai Y, Sun N, Hou H, Ehrhart J, Zeng J, Mori T, Arendash GW, Shytle D, Town T, Tan J. Lee JW, Lee YK, Ban JO, Ha TY, Yun YP, Han SB, Oh KW, Hong JT. Download references. Department of Integrative Biology, School of Biosciences and Technology, VIT University, Vellore, , Tamil Nadu, India. Department of Biotechnology, School of Biosciences and Technology, VIT University, Vellore, , Tamil Nadu, India. Centre for Interdisciplinary Biomedical Research, Adesh University, Bathinda, Punjab, India. You can also search for this author in PubMed Google Scholar. Correspondence to Zaved Ahmed Khan. NAS had designed and drafted the manuscript. AKM and ZAK had primary responsibility for the final content. All authors have read and approved the final manuscript. Open Access This article is distributed under the terms of the Creative Commons Attribution 4. Reprints and permissions. Singh, N. Potential neuroprotective properties of epigallocatechingallate EGCG. Nutr J 15 , 60 Download citation. Received : 31 March Accepted : 02 June Published : 07 June Anyone you share the following link with will be able to read this content:. Sorry, a shareable link is not currently available for this article. Provided by the Springer Nature SharedIt content-sharing initiative. Skip to main content. Search all BMC articles Search. Download PDF. Download ePub. Introduction Neurodegenerative diseases impose a significant social and economic burden. Full size image. Current status of knowledge Green tea polyphenols Green tea is a traditional drink made from Camellia sinesis plant, widely consumed in Asian countries [ 18 ]. Neuroprotective properties of EGCG Green tea polyphenols are known to possess neuroprotective and neurorescue action. Free radical scavenging and antioxidant action Reactive oxygen and nitrogen species such as nitrite oxide, superoxide and hydroxyl free radicals are naturally produced to assist the host system in defence against oxidative stress and inflammation triggered through pathogens and infectious agents. Iron chelating activity Iron accumulation is one of the major pathologies of neurodegenerative diseases causing neuron death at the site of iron accumulation [ 96 ]. Lipid peroxidation EGCG has been reported to protect from lipid peroxidation and DNA deamination by guarding cells from the initiators of lipid peroxidation i. Modulation of cell signalling pathways, cell survival and death genes EGCG protects not only through their antioxidant potential but also through the modulation of signalling pathways, cell survival and cell death genes. Table 1 Neuroprotective effects of EGCG in in vitro and in vivo models of neurotoxicity Full size table. New treatment approach Although EGCG is a good candidate for a neuroprotective agent due to its ability to manipulate multiple desired targets, its use as a therapeutic agent is limited. Conclusion The multi-etiological character of neurodegenerative diseases demands the need for the development of therapeutic agents capable of manipulating multiple desired targets. Article CAS PubMed PubMed Central Google Scholar Sheridan C. Article CAS PubMed Google Scholar Guo S, Bezard E, Zhao B. Article CAS PubMed Google Scholar Weinreb O, Mandel S, Amit T, Youdim MBH. Article CAS PubMed Google Scholar Singh R, Akhtar N, Haqqi TM. Article Google Scholar Lambert JD, Elias RJ. Article CAS PubMed Google Scholar Unno K, Takabayashi F, Yoshida H, Choba D, Fukutomi R, Kikunaga N, et al. Article CAS PubMed Google Scholar Schaffer S, Asseburg H, Kuntz S, Muller WE, Eckert GP. Article CAS PubMed Google Scholar Lim HJ, Shim SB, Jee SW, Lee SH, Lim CJ, Hong JT, et al. Article CAS PubMed Google Scholar Levites Y, Amit T, Youdim MBH, Mandel S. Article CAS PubMed Google Scholar Mandel SA, Avramovich-Tirosh Y, Reznichenko L, Zheng H, Weinreb O, Amit T, et al. Article CAS PubMed Google Scholar Khokhar S, Magnusdottir SGM. Article CAS PubMed Google Scholar Nanjo F, Goto K, Seto R, Suzuki M, Sakai M, Hara Y. Article CAS PubMed Google Scholar Khan N, Afaq F, Saleem M, Ahmad N, Mukhtar H. Article CAS PubMed PubMed Central Google Scholar Ritchie K, Lovestone S. CAS PubMed Google Scholar Kennedy DO, Wightman EL. Article CAS PubMed PubMed Central Google Scholar Checkoway H, Powers K, Smith-Weller T, Franklin GM, Longstreth WT, Swanson PD. Article PubMed Google Scholar Li F-J, Ji H-F, Shen L. Article PubMed Google Scholar Gao X, Cassidy A, Schwarzschild MA, Rimm EB, Ascherio A. Article CAS PubMed PubMed Central Google Scholar Quintana JLB, Allam MF, Castillo AS, Navajas RF-C. Article CAS Google Scholar Tan E-K, Tan C, Fook-Chong SMC, Lum SY, Chai A, Chung H, et al. Article PubMed Google Scholar Lee MJ, Wang ZY, Li H, Chen L, Sun Y, Gobbo S, et al. CAS Google Scholar Nakagawa K, Okuda S, Miyazawa T. Article CAS PubMed Google Scholar Nie G, Cao Y, Zhao B. Article PubMed Google Scholar Grinberg LN, Newmark H, Kitrossky N, Rahamim E, Chevion M, Rachmilewitz EA. Article CAS PubMed Google Scholar Solanki I, Parihar P, Mansuri ML, Parihar MS. Article CAS PubMed PubMed Central Google Scholar Abd El Mohsen MM, Kuhnle G, Rechner AR, Schroeter H, Rose S, Jenner P, et al. Article CAS PubMed Google Scholar Zhang B, Rusciano D, Osborne NN. Article CAS PubMed Google Scholar Stefanis L. Article PubMed PubMed Central CAS Google Scholar Bagad M, Chowdhury D, Khan ZA. Article PubMed PubMed Central CAS Google Scholar Zhang H, Zhang Y-W, Chen Y, Huang X, Zhou F, Wang W, et al. Article CAS PubMed PubMed Central Google Scholar Mattson MP. Article PubMed PubMed Central Google Scholar Cavet ME, Harrington KL, Vollmer TR, Ward KW, Zhang J-Z. CAS PubMed PubMed Central Google Scholar Li M-J, Yin Y-C, Wang J, Jiang Y-F. Article CAS PubMed PubMed Central Google Scholar Bahadoran Z, Mirmiran P, Azizi F. Article CAS PubMed Google Scholar Okello EJ, Leylabi R, McDougall GJ. Article CAS PubMed Google Scholar Wobst HJ, Sharma A, Diamond MI, Wanker EE, Bieschke J. Article CAS PubMed Google Scholar Rezai-Zadeh K, Arendash GW, Hou H, Fernandez F, Jensen M, Runfeldt M, et al. Article CAS PubMed Google Scholar Chesser AS, Ganeshan V, Yang J, Johnson GVW. CAS PubMed Google Scholar Agrawal M, Biswas A. Article CAS PubMed Google Scholar Zhang X, Wu M, Lu F, Luo N, He ZP, Yang H. CAS PubMed Google Scholar Han J, Wang M, Jing X, Shi H, Ren M, Lou H. Article CAS PubMed Google Scholar Abib RT, Peres KC, Barbosa AM, Peres TV, Bernardes A, Zimmermann LM, et al. Article CAS PubMed Google Scholar Chao J, Lau WKW, Huie MJ, Ho YS, Yu MS, Lai CSW, et al. Article CAS PubMed Google Scholar Schroeder EK, Kelsey NA, Doyle J, Breed E, Bouchard RJ, Loucks FA, et al. Article CAS PubMed Google Scholar Yu J, Jia Y, Guo Y, Chang G, Duan W, Sun M, et al. Article CAS PubMed Google Scholar Sutherland BA, Shaw OM, Clarkson AN, Jackson DN, Sammut IA, Appleton I. CAS PubMed Google Scholar Herges K, Millward JM, Hentschel N, Infante-Duarte C, Aktas O, Zipp F. Article CAS PubMed Google Scholar Rezai-Zadeh K, Shytle D, Sun N, Mori T, Hou H, Jeanniton D, et al. Article CAS PubMed Google Scholar Yeon J, Jeon S, Bae K, Song K, Hee Y. Article CAS Google Scholar Reznichenko L, Amit T, Youdim MBH, Mandel S. Article CAS PubMed Google Scholar Sagi Y, Mandel S, Amit T, Youdim MBH. Article CAS PubMed Google Scholar Valko M, Leibfritz D, Moncol J, Cronin MT, Mazur M, Telser J. Article CAS PubMed Google Scholar Zhao C, Li C, Liu S, Yang L. Google Scholar Young Park S, Jeong YJ, Kim SH, Jung JY, Kim WJ. Article CAS PubMed Google Scholar Guo Q, Zhao B, Li M, Shen S, Wenjuan X. Article CAS Google Scholar Devika PT, Stanely Mainzen Prince P. Article CAS PubMed Google Scholar Jelenković A, Jovanović MD, Stevanović I, Petronijević N, Bokonjić D, Živković J, et al. Article CAS Google Scholar Srividhya R, Jyothilakshmi V, Arulmathi K, Senthilkumaran V, Kalaiselvi P. Article CAS PubMed Google Scholar Erba D, Riso P, Bordoni A, Foti P, Biagi PL, Testolin G. Article CAS PubMed Google Scholar Panza VSP, Wazlawik E, Ricardo Schütz G, Comin L, Hecht KC, da Silva EL. Article CAS PubMed Google Scholar Sartor L, Pezzato E, Garbisa S. Article PubMed Google Scholar Yeoh BS, Aguilera Olvera R, Singh V, Xiao X, Kennett MJ, Joe B, et al. Article CAS Google Scholar Urrutia PJ, Mena NP, Núñez MT. Article CAS PubMed PubMed Central Google Scholar Berg D. Article CAS PubMed Google Scholar Li J, Ye L, Wang X, Liu J, Wang Y, Zhou Y, et al. Article CAS PubMed Google Scholar Bao GH, Xu J, Hu FL, Wan XC, Deng SX, Barasch J. Article CAS PubMed PubMed Central Google Scholar Saffari Y, Sadrzadeh SMH. Article CAS PubMed Google Scholar Teixeira MDA, Souza CM, Menezes APF, Carmo MRS, Fonteles AA, Gurgel JP, et al. Article CAS PubMed Google Scholar Lee SR, Im KJ, Suh SI, Jung JG. Article CAS Google Scholar Chen M-H, Tsai C-F, Hsu Y-W, Lu F-J. CAS PubMed PubMed Central Google Scholar Chen W, Hsieh S, Chiu C, Hsu B, Liou Y. Article PubMed PubMed Central CAS Google Scholar Jeong JH, Kim HJ, Lee TJ, Kim MK, Park ES, Choi BS. Article CAS PubMed Google Scholar Dobrzynska I, Sniecinska A, Skrzydlewska E, Figaszewski Z. PubMed Google Scholar Ostrowska J, Łuczaj W, Kasacka I, Rózański A, Skrzydlewska E. Article CAS PubMed Google Scholar Kennedy DO. Article PubMed CAS Google Scholar Vianna MRM, Barros DM, Silva T, Choi H, Madche C, Rodrigues C, et al. Article CAS Google Scholar Sun MK, Alkon DL. Article CAS PubMed Google Scholar Sun MK, Alkon DL. Article CAS PubMed Google Scholar Pascale A, Amadio M, Govoni S, Battaini F. Article CAS PubMed Google Scholar Mansuri ML, Parihar P, Solanki I, Parihar MS. Article PubMed PubMed Central Google Scholar Newton AC. Article CAS PubMed PubMed Central Google Scholar Kim SY, Ahn BH, Kim J, Bae YS, Kwak JY, Min G, et al. Article CAS PubMed Google Scholar Mandel SA, Amit T, Kalfon L, Reznichenko L, Youdim MBH. CAS PubMed Google Scholar Vasilevko V, Cribbs DH. Article CAS PubMed Google Scholar Nunan J, Small DH. Article CAS PubMed Google Scholar Reznichenko L, Amit T, Zheng H, Avramovich-Tirosh Y, Youdim MBH, Weinreb O, et al. Article CAS PubMed Google Scholar Choi D-S, Wang D, Yu G-Q, Zhu G, Kharazia VN, Paredes JP, et al. Article CAS PubMed PubMed Central Google Scholar Li R, Peng N, Li XP, Le WD. Article CAS PubMed Google Scholar Lu H, Meng X, Yang CS. Article CAS PubMed Google Scholar Hommes DW, Peppelenbosch MP, van Deventer SJH. Article CAS PubMed PubMed Central Google Scholar Johnson GL, Lapadat R. Article CAS PubMed Google Scholar Vauzour D, Vafeiadou K, Rice-Evans C, Williams RJ, Spencer JPE. Article CAS PubMed Google Scholar Behrens a, Sibilia M, Wagner EF. Article PubMed Google Scholar Ah Kang K, Wang ZH, Zhang R, Piao MJ, Kim KC, Kang SS, et al. Article CAS Google Scholar Davis RJ. Article CAS PubMed Google Scholar Hollenbach E, Vieth M, Roessner A, Neumann M, Malfertheiner P, Naumann M. Article CAS PubMed Google Scholar Schroeter H, Bahia P, Spencer JPE, Sheppard O, Rattray M, Cadenas E, et al. Article CAS PubMed Google Scholar Huang CC, Wu WB, Fang JY, Chiang HS, Chen SK, Chen BH, et al. Article CAS PubMed Google Scholar Chang CW, Hsieh YH, Yang WE, Yang SF, Chen Y, Hu DN. Google Scholar Na HK, Kim EH, Jung JH, Lee HH, Hyun JW, Surh YJ. CAS PubMed Google Scholar Jiménez C, Hernández C, Pimentel B, Carrera AC. Article PubMed CAS Google Scholar Brazil DP, Hemmings BA. Article CAS PubMed Google Scholar Kennedy SG, Wagner AJ, Conzen SD, Jordán J, Bellacosa A, Tsichlis PN, et al. Article CAS PubMed Google Scholar Simpson L, Parsons R. Article CAS PubMed Google Scholar Neri LM, Borgatti P, Capitani S, Martelli AM. CAS PubMed Google Scholar Williams RJ, Spencer JPE. Article CAS PubMed Google Scholar Gassen M, Youdim M. Article CAS PubMed Google Scholar Mandel S, Grünblatt E, Riederer P, Gerlach M, Levites Y, Youdim MBH. CAS PubMed Google Scholar Beal MF, Rascol, Marek, Olanow, Kordower, Isacson, et al. CAS PubMed Google Scholar Hastak K, Gupta S, Ahmad N, Agarwal MK, Agarwal ML, Mukhtar H. CAS Google Scholar Pool H, Quintanar D, Figueroa JDD, Marinho Mano C, Bechara JEH, Godínez L a. Article CAS PubMed Google Scholar Pardeshi C, Rajput P, Belgamwar V, Tekade A, Patil G, Chaudhary K, et al. Google Scholar Prakash RT, Mandal AKA. CAS Google Scholar Karikalan K, Kaur G, Mandal A. Google Scholar Xu Z, Chen S, Li X, Luo G, Li L, Le W. Article CAS PubMed Google Scholar Chang-Mu C, Jen-Kun L, Shing-Hwa L, Shoei-Yn LS. Article PubMed CAS Google Scholar Kim SJ, Jeong HJ, Lee KM, Myung NY, An NH, Yang WM, Park SK, Lee HJ, Hong SH, Kim HM, Um JY. Article CAS PubMed Google Scholar Weinreb O, Amit T, Youdim MB. Article CAS PubMed Google Scholar Levites Y, Amit T, Mandel S, Youdim MB. CAS PubMed Google Scholar Bieschke J, Russ J, Friedrich RP, Ehrnhoefer DE, Wobst H, Neugebauer K, Wanker EE. Article CAS PubMed PubMed Central Google Scholar Hudson SA, Ecroyd H, Dehle FC, Musgrave IF, Carver JA. Article CAS PubMed Google Scholar Ehrnhoefer DE, Bieschke J, Boeddrich A, Herbst M, Masino L, Lurz R, Engemann S, Pastore A, Wanker EE. Article CAS PubMed Google Scholar Obregon DF, Rezai-Zadeh K, Bai Y, Sun N, Hou H, Ehrhart J, Zeng J, Mori T, Arendash GW, Shytle D, Town T, Tan J. Article CAS PubMed Google Scholar Lee JW, Lee YK, Ban JO, Ha TY, Yun YP, Han SB, Oh KW, Hong JT. In the current study, we revealed that EGCG and ECG inhibit complex I of the ETC. This finding is well aligned with the plethora of literature describing polyphenols as compounds targeting mitochondria [ 53 , 54 ]. Consequently, we isolated mitochondria to investigate the impact of EGCG and ECG on the complexes of the mitochondrial ETC. Isolated mitochondria are separated from their natural environment and signaling processes, and the isolation process brings the risk of damaging mitochondrial membranes due to shear forces [ 55 ]. However, drug uptake by mitochondria is dependent on the integrity of the outer and inner mitochondrial membrane, including the function of transporter proteins and carriers [ 56 ]. Besides, the isolation of mitochondria yields a relatively homogenous population of spherical organelles with disorganized cristae and diluted matrix content. The structural alterations affect ETC activity and mitochondrial respiration rate [ 57 ]. We assume that structural changes in cristae organization due to the isolation process might be another reason why 25 μM of EGCG and ECG were necessary to significantly block complex I activity and mitochondrial respiration rate in isolated mitochondria. In addition, we present that a temporary hampered mitochondrial respiration goes along with a transient rise in ROS levels and a brief drop in ATP, triggering signaling pathways associated with lifespan extension in C. Our findings align with reports about the C. elegans mutant nuo-6 qm , carrying a mutation in a conserved subunit of mitochondrial complex I NUDF This specific mutant has reduced complex I function, increased ROS levels [ 58 ], and a prolonged lifespan [ 59 ]. It was also speculated that blockage of the complex I of the mitochondrial electron transport chain delays aging due to slowed embryonic development and larval growth, decreased pumping and defecation rate, or a reduced accumulation of ROS damage [ 60 — 62 ]. At this stage, mitochondria are already undergoing a period of dramatic proliferation and massive mitochondrial DNA expansion [ 63 ]. Moreover, inhibiting respiratory chain components during adulthood did not provoke lifespan extension anymore [ 64 — 66 ]. Consequently, one has to assume that a temporary sub-lethal rise in mitochondrial ROS during early adulthood induces lifespan extension by provoking changes in the homeostasis of proteins [ 59 , 67 ] and metabolism [ 58 ]. Notably, glucose restriction by 2-deoxy-D-glucose 2-DG -mediated inhibition of glycolysis increases the lifespan in C. elegans in a ROS-dependent manner [ 18 ], suggesting that the temporary drop in ATP levels due to complex I inhibition is an additional trigger to prolong lifespan. By activating these signaling cascades, the function of ROS defense enzymes, SOD and CTL, and the oxidative stress resistance gets boosted. Ahead of this report, SOD-3, DAF, and SKN-1 were already suggested as targets of EGCG due to enhanced expression [ 68 ] or translocation into the nucleus after respective compound treatment [ 48 ]. Notably, SKN-1 activation in neurons is necessary for dietary restriction-mediated lifespan extension [ 69 ]. DAF, the orthologue of mammalian FOXO, is a crucial regulator of longevity, metabolism, and dauer diapauses in C. Consequently, it seems reasonable that the ROS-sensing p38 MAPK and the energy-sensing AMPK activate the respective signaling cascades after blockage of complex I by EGCG and ECG. Reports showed that AMPK activates p38 MAPK [ 73 ]. The long-term effects also included reduced fat content in C. elegans after 5 days of catechin treatment. Align with this finding, inhibition of complex I and complex IV by rotenone and NaN3 reduced lipid accumulation in 3T3-L1 cells [ 74 ]. Moreover, a previous report revealed reduced body fat content in C. elegans after catechin treatment [ 75 ]. Besides, green tea catechins were associated with reduced obesity in zebrafish [ 76 ], mice [ 77 ], rats [ 78 , 79 ], and humans [ 80 , 81 ], suggesting a catechin-induced metabolic remodeling. Clinical trials have already confirmed the safety of EGCG [ 7 ] and highlighted the potential in counteracting age-related cardiovascular and metabolic diseases [ 1 — 4 ]. Experiments in rodents studying physical and clinical parameters over time and further clinical trials are required to identify the best timing and dosage for administering catechins. Finally, these studies might characterize additional effects and downstream mechanisms of complex I inhibition. Despite the promising results obtained in animal experiments, the low bioavailability of EGCG [ 7 ] still raises the question of whether green tea catechins can reliably provoke beneficial effects in humans. Consequently, additional efforts might be needed to identify complex I inhibitors with increased bioavailability. We conclude that applying the green tea catechins EGCG and ECG at a low dose extends the lifespan of C. elegans via inducing a mitohormetic response. In the long term, the re-wiring of these energy- and ROS-dependent pathways reduces the fat content and extends health- and lifespan. Figure 6. Green tea catechins enhance fitness and lifespan of Caenorhabditis elegance by complex I inhibition. elegans strains used in the current study were obtained from the Caenorhabditis Genetics Center CGC, University of Minnesota. Nematodes were grown and maintained at 20°C in 10 cm Petri dishes on nematode growth media NGM , with Escherichia coli E. coli OP50 bacteria as the food resource as previously described [ 18 , 82 , 83 ]. The strains used in this study included the following: N2 wild type , GA aak-2 ok , VC sir EGCG, ECG, and BHA dissolved in DMSO, reaching a stock concentration of 2. The NGM agar solution was autoclaved and subsequently cooled to 55°C, before supplements and compounds EGCG, ECG, BHA, or DMSO were added under continuous stirring. The final concentration for compounds was calculated regarding the volume of agar, and the same volume of DMSO was added to control plates. Agar plates were poured and dried, sealed with parafilm, and stored at 4°C. Before experiments, NGM plates were spotted with a bacterial lawn of heat-inactivated bacteria OP50 HIT to avoid interference by a potential xenobiotic-metabolizing activity of E. To exclude any effects on development, the incubation period with compounds started at the L4 stage by transferring nematodes to the respective NGM plates [ 84 ]. Louis, MO, USA to prevent progeny formation. After 16 h, we transferred animals to respective treatment groups and harvested them at the indicated time points [ 18 ]. According to standard protocols, all lifespan assays were performed at 20°C as previously described [ 18 , 19 ]. Briefly, the C. Eggs of nematodes were transferred to NGM plates with fresh OP50 bacteria to allow hatching and development. After approximately 64 h, at the L4 stage, we moved nematodes manually to freshly prepared NGM plates containing the respective compounds and supplied them with a lawn of OP50 HIT. During the first 10—14 days, nematodes were transferred to freshly prepared NGM treatment plates every day and later every second day. Nematodes without any reaction to gentle stimulation were classified as dead. Nematodes that crawled off the plate or suffered from non-natural death like internal hatching were censored and excluded from statistics on the day of premature death. Notably, for lifespan analysis using BHA, nematodes were propagated on BHA-containing NGM plates for four generations before synchronization; the same applied for the respective DMSO controls. Following the L4 stage, nematodes were treated with 0. Afterward, we transferred single worms into S-buffer containing 0. Movements of single worms within the liquid system were recorded for 20 seconds by a digital CCD camera Moticam , Motic, St. Ingbert, Germany coupled microscope SMZ , Motic, St. Ingbert, Germany equipped with Motic Images Plus 2. We analyzed the videos using the DanioTrack software Loligo Systems, Tjele, Denmark , subtracting the background and determining the center of gravity of all object pixels compared to the background. Resistance to lethal oxidative stress by paraquat Sigma-Aldrich, Munich, Germany was assessed as previously described [ 18 , 19 ]. Briefly, worms were treated with 0. Afterward, we transferred worms into well plates: 6 nematodes in μl of S-buffer, containing freshly dissolved 50 mM paraquat. Dead worms were scored every hour until all control worms were dead. Briefly, we treated worms with 0. Worms were also washed twice with S-buffer and transferred into the DW1 chamber to monitor oxygen consumption for 10 mins. Afterward, we collected worms for Bradford protein determination [ 86 ]. Before the ROS measurement, MitoTracker Red CM-H2X ROS Invitrogen, Carlsbad, CA, USA incubation plates were prepared as previously described [ 19 ]. Worms were additionally washed twice with S-buffer and transferred to freshly prepared MitoTracker Red CM-H2X incubation NGM plates containing μl of OP50 HIT mixed with μl freshly prepared MitoTracker Red CM-H2X stock solution μM. After 2 h at 20°C, worms were washed off MitoTracker Red CM-H2X incubation NGM plates and transferred to NGM agar plates with 0. Fluorescence intensity was measured on a microplate reader FLUOstar Optima, BMG Labtech, Offenburg, Germany using well-scanning mode ex: nm; em: nm. We collected worms from plates for Bradford protein determination [ 86 ]. We placed an equal number of nematodes on the NGM plates containing 0. After collection and two subsequent washes in S-buffer, worm pellets were resuspended in the incubation buffer. The latter were placed in 10 cm Petri dishes together with a second 4 cm Petri dish containing μl of 0. Hence, each 10 cm dish was equipped with two 4 cm dishes, one carrying nematodes and the other containing KOH. We added nonradioactive glucose into each sample to reach a final concentration of 0. The 10 cm Petri dishes were covered, sealed with parafilm in an air-tight manner, and incubated at 20°C for 3 h. Subsequently, an aliquot of μl of KOH was immersed in 4. to quantify the amount of trapped 14 CO 2. We treated nematodes with 0. After collection and washing with S-buffer twice, worm pellets were shock frozen in liquid nitrogen and grinded in a nitrogen-chilled mortar. The grinded samples were boiled with 4 M Guanidine-HCl at 99°C for 15 min to destroy ATPase activity [ 58 , 89 ]. ATP values were normalized to protein content using the Bradford assay [ 86 ]. After treating nematodes with 0. The produced formaldehyde was determined spectrophotometrically with 4-aminohydrazinomercapto-1, 2, 4-triazole Purpald, Applichem, Darmstadt, Germany. We measured SOD activity photometrically with a tetrazolium salt, forming a water-soluble formazan dye upon reduction with a superoxide anion. We determined fat content by applying a triglyceride determination kit Roche, Mannheim, Germany as previously described [ 18 , 88 ] and normalized to protein content using the Bradford assay [ 86 ]. Briefly, worms were incubated with 0. We centrifuged μl of the homogenized extract and extracted the supernatant for protein determination. The heating was repeated once to dissolve all triglycerides. We measured the activity of complex I spectrophotometrically at nm in 1 ml of 25 mM potassium phosphate buffer containing 3. Decylubiquinone and antimycin A were dissolved in DMSO as DCIP and NADH were dissolved in water as 10 mM for both. After being thawed, 30 μl of mitochondria were treated with μl of 10 mM Tris-Cl, pH 7. Subsequently, 20 μl mitochondria fragments were preincubated in a μl incubation mixture without NADH for 3 mins. After 3 mins, we added 20 μl of 10 mM NADH into the incubation mixture and measured the absorbance at 20 s intervals for 2 mins. Briefly, rodents were fasted overnight and killed by cervical dislocation. The washed liver fragments were placed into the tube with around 25 ml isolation buffer. The loose-fitting pestle was inserted, pressed down, and lifted four times, and then the tight-fitting pestle was applied in the same way twice. The mixture was poured into the 50 ml polypropylene falcon tube and centrifuged at g for 10 min at 4°C. We carefully removed the fat on the top of the supernatant by using tissue paper. The supernatant was extracted to a second polypropylene falcon tube centrifuged at g for 10 min at 4°C. Afterward, the fat was removed, the supernatant discarded, and the mitochondrial pellet resuspended in the remaining buffer. The suspension containing mitochondria was centrifuged again at g for 10 min at 4°C. The supernatant was removed entirely, and the mitochondrial pellet was resuspended in μl isolation buffer as described above. The concentration of isolated mitochondria was determined with Bradford After recording basal respiration for 2 min, 0. After ADP was wholly consumed, the oxygen consumption rate slowed down, 5 mM succinate, and ADP were added to study complex II, III, IV activity. At the end of each measurement 60 nM FCCP were supplied to check the viability of mitochondria. Data are expressed as means ±SD unless otherwise indicated. Statistical calculations were carried out using the log-rank test to compare significant distributions between the different groups in lifespan and stress resistance assays. We performed all analyses using Microsoft Office Excel Microsoft, Albuquerque, NM, USA. performed experiments, analyzed, and visualized the data. and M. wrote the manuscript. Funding was acquired by M. and C. All authors have read and agreed to the published version of the manuscript. elegans strains used in this work were provided by the Caenorhabditis Genetics Centre Univ. of Minnesota, USA , which is funded by NIH Office of Research Infrastructure Programs P40 OD Parts of this project are contained in a Ph. thesis J. thesis C. is currently funded by an Erwin Schroedinger Abroad Fellowship JB Corina T. Madreiter-Sokolowski corina. madreiter medunigraz. Michael Ristow michael-ristow ethz. Navigate Home Editorial Board Information For Authors Advance Online Publications Current Issue Archive Scientific Integrity Publication Ethics and Publication Malpractice Statements Contact Special Collections Podcast News Room Interviews with Outstanding Authors. Priority Research Paper Volume 13, Issue 19 pp — Cite this Article How to cite Tian J , Geiss C , Zarse K , Madreiter-Sokolowski CT , Ristow M ,. Abstract Green tea catechins are associated with a delay in aging. Introduction Clinical trials and epidemiological studies have revealed health benefits associated with green tea consumption, including a significant reduction in systolic blood pressure [ 1 ] and fasting glucose [ 2 ] as well as weight loss in type 2 diabetes patients [ 3 ] and in women with central obesity [ 4 ]. Results EGCG and ECG promote lifespan, fitness, and stress resistance when applied at low doses Oral absorption and absolute bioavailability of green tea catechins are low in mammals [ 12 ], reaching total maximum plasma concentrations of 2. Table 1. Lifespan results and statistical analysis. Strains, Compounds Max lifespan in days ± SD 10 th percentile Medium lifespan in days ± SD 50 th percentile Number of experiments n P value versus control Number of nematodes N2 DMSO p38 MAPK, NRF2, and FOXO are required for the lifespan extension induced by catechins As shown in Figure 2 , EGCG and ECG block complex I activity and, thus, induce a transient rise in ROS levels. Discussion Green tea is one of the most widely consumed beverages worldwide [ 32 ]. Conclusions We conclude that applying the green tea catechins EGCG and ECG at a low dose extends the lifespan of C. Methods Nematode strains and maintenance C. Compound treatment EGCG, ECG, and BHA dissolved in DMSO, reaching a stock concentration of 2. Lifespan analyses According to standard protocols, all lifespan assays were performed at 20°C as previously described [ 18 , 19 ]. Locomotion assay Following the L4 stage, nematodes were treated with 0. Paraquat stress resistance assay Resistance to lethal oxidative stress by paraquat Sigma-Aldrich, Munich, Germany was assessed as previously described [ 18 , 19 ]. ROS quantification Before the ROS measurement, MitoTracker Red CM-H2X ROS Invitrogen, Carlsbad, CA, USA incubation plates were prepared as previously described [ 19 ]. Glucose oxidation assay [ 14 C] D-glucose oxidation rates were determined as described previously [ 87 ]. ATP quantification We treated nematodes with 0.
Related Articles	Beneficial Properties of Green Tea Catechins. Additionally, i. Thus increasing the expression of neuroprotection [ ]. Chuan Jiang, Hua Wang, … Yonggang Gao. J Neurol Neurosurg Psychiatry. There was also a significant increase in the cGMP level following treatment with EGCG in the control group.
EGCG (Epigallocatechin Gallate): Benefits, Dosage, and Safety	Reduxtion tea protects against Nutritional strategies for hypertension lipid peroxidation in rat organs. Oral administration of EGCG, in vivo has Support healthy aging process significant reduction strwss levels of reducyion peroxidation products reducttion elevated levels Strfss enzymatic and non-enzymatic antioxidants [ 88 ]. This is an open-access article distributed under the terms of the Creative Commons Attribution License CC BY. We could show that BHA prevented lifespan extension by EGCG and ECG, suggesting that an initial rise in ROS levels is necessary to induce adaptational mechanisms causing improved antioxidant properties. Article Google Scholar. Am J Physiol. The grinded samples were boiled with 4 M Guanidine-HCl at 99°C for 15 min to destroy ATPase activity [ 5889 ].

Nutritional strategies for hypertension tea Strees gained popularity reducgion an accessible streas to reuction the impact of chronic stress-induced autonomic imbalance and increased risk for cardiovascular Boost your metabolism despite a lack of evidence EGCCG the reductino acid ECG content in Cramp relief for elderly individuals cup of the tea and its effects on redution and psychological ECGG EGCG and stress reduction measures of cognitive function. EGCG and stress reduction aimed to measure the effects of GABA-fortified tea consumption on heart rate variability HRV and stress in 30 participants using a pre-post cohort study design. Ten minute lead II ECG recordings were analyzed with Kubios software. Frequency domain parameters including total power, high and low frequency power, along with heart rate, were determined. A control group that consumed a non-fortified tea was included in the research. Oolong tea consumption led to a significant decrease in the immediate stress score and a significant improvement in HRV. We conclude that autonomic imbalance and HRV in people with acute stress is significantly reduced following a cup of GABA fortified oolong tea and highlights the complex interaction between autonomic nervous system function and mood.

Category: Family

EGCG and stress reduction

0 thoughts on “EGCG and stress reduction”

Leave a comment Cancel