Neuroprotective effect of trans-N-caffeoyltyramine from Lycium chinense against H2O2 induced cytotoxicity in PC12 cells by attenuating oxidative stress

Biomedicine and Pharmacotherapy

Volumn 93, Issue , 2017, Pages 895-902

  Olatunji, Opeyemi J ^a   Chen, Hongxia ^b   Zhou, Yifeng ^c,d  

^a PRINCE OF SONGKLA UNIVERSITY   (Thailand)

^b JIANGSU UNIVERSITY   (China)

^c INSTITUTE OF BOTANY   (China)

^d INSTITUTE OF GEOLOGY AND GEOPHYSICS   (China)

Author keywords

Hydrogen peroxide; Neuroprotection; Oxidative stress; PC12 cells; Trans N caffeoyltyramine

Indexed keywords

ANTIOXIDANT; CALCIUM ION; CASPASE 3; CATALASE; GLUTATHIONE; HYDROGEN PEROXIDE; LACTATE DEHYDROGENASE; MALONALDEHYDE; N CAFFEOYLTYRAMINE; NATURAL PRODUCT; NEUROPROTECTIVE AGENT; PROTEIN BAX; PROTEIN BCL 2; REACTIVE OXYGEN METABOLITE; SUPEROXIDE DISMUTASE; UNCLASSIFIED DRUG; CAFFEIC ACID DERIVATIVE; GLUTATHIONE PEROXIDASE; N-CAFFEOYLTYRAMINE; PLANT EXTRACT; TYRAMINE;

ANTIOXIDANT ACTIVITY; APOPTOSIS; ARTICLE; BARK; CALCIUM CELL LEVEL; CALCIUM TRANSPORT; CELL DAMAGE; CELL VIABILITY; CYTOTOXICITY; DRUG ISOLATION; DRUG MECHANISM; ENZYME ACTIVITY; EXPOSURE; LIPID PEROXIDATION; LYCIUM CHINENSE; MITOCHONDRIAL MEMBRANE POTENTIAL; NEUROPROTECTION; NEUROTOXICITY; OXIDATIVE STRESS; PC12 CELL LINE; PLANT ROOT; PRIORITY JOURNAL; ANALOGS AND DERIVATIVES; ANIMAL; CELL SURVIVAL; CHEMISTRY; DRUG EFFECTS; LYCIUM; METABOLISM; NERVE CELL; PHYSIOLOGY; RAT; TUMOR CELL LINE;

ANIMALS; ANTIOXIDANTS; APOPTOSIS; CAFFEIC ACIDS; CATALASE; CELL LINE, TUMOR; CELL SURVIVAL; GLUTATHIONE; GLUTATHIONE PEROXIDASE; HYDROGEN PEROXIDE; LYCIUM; MALONDIALDEHYDE; MEMBRANE POTENTIAL, MITOCHONDRIAL; NEURONS; NEUROPROTECTIVE AGENTS; OXIDATIVE STRESS; PC12 CELLS; PLANT EXTRACTS; RATS; REACTIVE OXYGEN SPECIES; SUPEROXIDE DISMUTASE; TYRAMINE;

EID: 85023606995     PISSN: 07533322     EISSN: 19506007     Source Type: Journal    
DOI: 10.1016/j.biopha.2017.07.013     Document Type: Article

References (39)

1. Yan, M.H., Wang, X., Zhu, X., Mitochondrial defects and oxidative stress in Alzheimer disease and Parkinson disease. Free Radic. Biol. Med. 62 (2013), 90–101.
2. Everse, J., Coates, P.W., Neurodegeneration and peroxidases. Neurobiol. Aging 30 (2009), 1011–1025.
3. Simonian, N.A., Coyle, J.T., Oxidative stress in neurodegenerative diseases. Annu. Rev. Pharmacol. Toxicol. 36 (1996), 83–106.
4. Barnham, K.J., Masters, C.L., Bush, A.I., Neurodegenerative diseases and oxidative stress. Nat. Rev. Drug Discov. 3 (2004), 205–214.
5. Underwood, B.R., Imarisio, S., Fleming, A., Rose, C., Krishna, G., Heard, P., Quick, M., Korolchuk, V.I., Renna, M., Sarkar, S., Garcia-Arencibia, M., O'Kane, C.J., Murphy, M.P., Rubinsztein, D.C., Antioxidants can inhibit basal autophagy and enhance neurodegeneration in models of polyglutamine disease. Hum. Mol. Gen. 19 (2010), 3413–3429.
6. Aseervatham, G.S., Sivasudha, T., Jeyadevi, R., Arul Ananth, D., Environmental factors and unhealthy lifestyle influence oxidative stress in humans—an overview. Environ. Sci. Pollut. Res. Int. 20 (2013), 4356–4369.
7. Pallast, S., Arai, K., Wang, X., Lo, E.H., van Leyen, K., 12/15-Lipoxygenase targets neuronal mitochondria under oxidative stress. J. Neurochem. 111 (2009), 882–889.
8. Jiang, X., Zhang, C., Xin, Y., Huang, Z., Tan, Y., Huang, Y., Wang, Y., Feng, W., Li, X., Li, W., Qu, Y., Cai, L., Protective effect of FGF21 on type 1 diabetes-induced testicular apoptotic cell death probably via both mitochondrial and endoplasmic reticulum stress-dependent pathways in the mouse model. Toxicol. Lett. 219 (2013), 65–76.
9. Ye, Z., Huang, Q., Ni, H.X., Wang, D., Cortex lycii radicis extracts improve insulin resistance and lipid metabolism in obese-diabetic rats. Phytother. Res. 22 (2008), 1665–1670.
10. Gao, D., Li, Q., Liu, Z., Li, Y., Liu, Z., Fan, Y., Li, K., Han, Z., Li, J., Hypoglycemic effects and mechanisms of action of cortex lycii radicis on alloxan-induced diabetic mice. Yakugaku Zasshi. 127 (2007), 1715–1721.
11. Chan, J.Y.W., Lam, F.C., Leung, P.C., Che, C.T., Fung, K.P., Antihyperglycemic and antioxidative effects of a herbal formulation of radix astragali, radix codonopsis and cortex lycii in a mouse model of type 2 diabetes mellitus. Phytother. Res. 23 (2009), 658–665.
12. Jeong, J.C., Kim, S.J., Kim, Y.K., Kwon, C.H., Kim, K.H., Lycii cortex radicis extract inhibits glioma tumor growth in vitro and in vivo through downregulation of the Akt/ERK athway. Oncol. Rep. 27 (2012), 1467–1474.
13. 2+ generation. Neurosci. Lett. 616 (2016), 111–118.
14. Chen, H., Olatunji, O.J., Zhou, Y., Anti-oxidative: anti-secretory and anti-inflammatory activities of the extract from the root bark of Lycium chinense (Cortex Lycii) against gastric ulcer in mice. J. Nat. Med. 70 (2016), 610–619.
15. Han, E.H., Kim, J.Y., Kim, H.G., Choi, J.H., Im, J.H., Woo, E.R., Jeong, H.G., Dihydro-N-caffeoyltyramine down-regulates cyclooxygenase-2 expression by inhibiting the activities of C/EBP and AP-1 transcription factors. Food Chem. Toxicol. 48 (2010), 579–586.
16. Xie, L.W., Atanasov, A.G., Guo, D.A., Malainer, C., Zhang, J.X., Zehl, M., Guan, S.H., Heiss, E.H., Urban, E., Dirsch, V.M., Activity-guided isolation of NF-κB inhibitors and PPARγ agonists from the root bark of Lycium chinense Miller. J. Ethnopharmacol. 152 (2014), 470–477.
17. Ma, X., Yan, J., Xu, K., Guo, L., Li, H., Binding mechanism of trans-N-caffeoyltyramine and human serum albumin: investigation by multi-spectroscopy and docking simulation. Bioorg. Chem. 66 (2016), 102–110.
18. Loh, K.P., Huang, S.H., De Silva, R., Tan, B.K., Zhu, Y.Z., Oxidative stress: apoptosis in neuronal injury. Curr. Alzheimer Res. 3 (2006), 327–337.
19. Gaki, G., Papavassiliou, A., Oxidative stress-induced signaling pathways implicated in the pathogenesis of Parkinson's disease. Neuromolecular Med. 16 (2014), 217–230.
20. Avshalumov, M.V., Rice, M.E., NMDA receptor activation mediates hydrogen peroxide-induced pathophysiology in rat hippocampal slices. J.Neurophysiol 87 (2002), 2896–2903.
21. Peng, T.I., Greenamyre, J.T., Privileged access to mitochondria of calcium influx through N-methyl-D-aspartate receptors. Mol. Pharmacol. 53 (1998), 974–980.
22. Jumblatt, J.E., Tischler, A.S., Regulation of muscarinic ligand binding sites by nerve growth factor in PC12 phaeochromocytoma cells. Nature 297 (1982), 152–154.
23. Patnaik, T., Dey, R.K., Gouda, P., Antimicrobial activity of friedelan-3β-ol and trans-N-caffeoyltyramine isolated from the root of Vitis trifolia. Asian J. Chem 20 (2008), 417–421.
24. Lee, D.G., Park, Y., Kim, M.R., Jung, H.J., Seu, Y.B., Hahm, K.S., Woo, E.R., Anti-fungal effects of phenolic amides isolated from the root bark of Lycium chinense. Biotechnol. Lett. 26 (2004), 1125–1130.
25. Uttara, B., Singh, A.V., Zamboni, P., Mahajan, R.T., Oxidative stress and neurodegenerative diseases: a review of upstream and downstream antioxidant therapeutic options. Curr. Neuropharmacol. 7 (2009), 65–74.
26. Pavlica, S., Gebhardt, R., Protective effects of flavonoids and two metabolites against oxidative stress in neuronal PC12 cells. Life Sci. 86 (2010), 79–86.
27. Satoh, T., Enokido, Y., Aoshima, H., Uchiyama, Y., Hatanaka, H., Changes in mitochondrial membrane potential during oxidative stress-induced apoptosis in PC12 cells. J. Neurosci. Res. 50 (1997), 413–420.
28. Zhang, S., Ye, J., Dong, G., Neuroprotective effect of baicalein on hydrogen peroxide-mediated oxidative stress and mitochondrial dysfunction in PC12 cells. J. Mol. Neurosci. 40 (2010), 311–330.
29. 2+-induced oxidative stress in brain mitochondria treated with the respiratory chain inhibitor rotenone. FEBS Lett. 543 (2003), 179–183.
30. Kuroda, J., Ago, T., Matsushima, S., Zhai, P., Schneider, M.D., Sadoshima, J., NADPH oxidase 4 (Nox4) is a major source of oxidative stress in the failing heart. Proc.Natl. Acad. Sci. U. S. A. 107 (2010), 15565–15570.
31. da Silva Morrone, M., de Assis, A.M., da Rocha, R.F., Gasparotto, J., Gazola, A.C., Costa, G.M., Zucolotto, S.M., Castellanos, L.H., Ramos, F.A., Schenkel, E.P., Reginatto, F.H., Gelain, D.P., Moreira, J.C., Passiflora manicata (Juss.) aqueous leaf extract protects against reactive oxygen species and protein glycation in vitro and ex vivo models. Food Chem. Toxicol. 60 (2013), 45–51.
32. Mates, J.M., Effects of antioxidant enzymes in the molecular control of reactive oxygen species toxicology. Toxicology 153 (2000), 83–104.
33. Nita, D.A., Nita, V., Spulber, S., Moldovan, M., Popa, D.P., Zagrean, A.M., Zagrean, L., Oxidative damage following cerebral ischemia depends on reperfusion—a biochemical study in rat. J. Cell. Mol. Med. 5 (2001), 163–170.
34. Beal, M.F., Mitochondria take center stage in aging and neurodegeneration. Ann. Neurol. 58 (2005), 495–505.
35. Li, P.F., Dietz, R., von Harsdorf, R., P53 regulates mitochondrial membrane potential through reactive oxygen species and induces cytochrome c independent apoptosis blocked by Bcl-2. EMBO J. 18 (1999), 6027–6036.
36. Cleary, M.L., Smith, S.D., Sklar, J., Cloning and structural analysis of cDNAs for bcl-2 and a hybrid bcl-2/immunoglobulin transcript resulting from the t(14;18) translocation. Cell 47 (1999), 19–28.
37. Cory, S., Adams, J.M., The Bcl2 family: regulators of the cellular life-or-death switch. Nat. Rev. Cancer 2 (2002), 647–656.
38. Gillardon, F., Lenz, C., Waschke, K.F., Krajewski, S., Reed, J.C., Zimmermann, M., Kuschinsky, W., Altered expression of Bcl-2, Bcl-X Bax, and c-Fos colocalizes with DNA fragmentation and ischemic cell damage following middle cerebral artery occlusion in rats. Brain Res. Mol. Brain Res. 40 (1996), 254–260.
39. Slee, E.A., Harte, M.T., Kluck, R.M., Wolf, B.B., Casiano, C.A., Newmeyer, D.D., Wang, H.G., Reed, J.C., Nicholson, D.W., Alnemri, E.S., Green, D.R., Martin, S.J., Ordering the cytochrome c-initiated caspase cascade: hierarchical activation of caspases-2 −3, −6, −7, −8, and −10 in a caspase-9- dependent manner. J. Cell Biol. 144 (1999), 281–292.