Vol 58, No 2 (2020)
Original paper
Published online: 2020-06-18

open access

Page views 2151
Article views/downloads 1231
Get Citation

Connect on Social Media

Connect on Social Media

Bisdemethoxycurcumin exerts a cell-protective effect via JAK2/STAT3 signaling in a rotenone-induced Parkinson’s disease model in vitro

Duanqun He12, Shuangxi Chen1, Zijian Xiao1, Heng Wu1, Guijuan Zhou1, Chenlin Xu1, Yunqian Chang1, Yihui Li1, Gang Wang3, Ming Xie1
Pubmed: 32557525
Folia Histochem Cytobiol 2020;58(2):127-134.

Abstract

Introduction. Oxidative stress and cell apoptosis have both been suggested to be closely associated with the pathogenesis of Parkinson’s disease (PD). Previously, bisdemethoxycurcumin (BDMC) has been shown to exhibit several desirable characteristics as a candidate neuroprotective agent, including antioxidant and anti-inflammatory activities in the nervous system. However, whether BDMC can exert cell-protective roles in an in vitro model of PD remains unknown.

Material and methods. SH-SY5Y cells were pretreated with BDMC, with or without AG490 and SI-201, for 30 min, followed by a co-incubation with rotenone for 24 h. Subsequently, a cell viability assay and western blotting was performed, and SOD and GSH activities were analyzed.

Results. The results revealed that the pretreatment with BDMC enhanced the cell survival, antioxidative stress capacity and the phosphorylation levels of JAK/STAT3 in SH-SY5Y cells treated with rotenone. However, following the incubation with AG490 and SI-201, inhibitors of the JAK/STAT3 signaling pathway, BDMC was unable to exert cell-protective roles in SH-SY5Y cells treated with rotenone.

Conclusions. In conclusion, the results suggested that BDMC may exert a cell-protective role in SH-SY5Y cells in vitro via JAK2/STAT3 signaling, thus suggesting the possible application of BDMC for the treatment of neurodegenerative diseases related to JAK2/STAT3 signaling.

Article available in PDF format

View PDF Download PDF file

References

  1. Cao Xu, Cao L, Ding L, et al. A New Hope for a Devastating Disease: Hydrogen Sulfide in Parkinson's Disease. Mol Neurobiol. 2018; 55(5): 3789–3799.
  2. Keeney PM, Xie J, Capaldi RA, et al. Parkinson's disease brain mitochondrial complex I has oxidatively damaged subunits and is functionally impaired and misassembled. J Neurosci. 2006; 26(19): 5256–5264.
  3. Chaudhuri K, Schapira A. Non-motor symptoms of Parkinson's disease: dopaminergic pathophysiology and treatment. The Lancet Neurology. 2009; 8(5): 464–474.
  4. Xia R, Mao ZH. Progression of motor symptoms in Parkinson's disease. Neurosci Bull. 2012; 28(1): 39–48.
  5. Mattson MP. Apoptosis in neurodegenerative disorders. Nat Rev Mol Cell Biol. 2000; 1(2): 120–129.
  6. Onyango IG. Mitochondrial dysfunction and oxidative stress in Parkinson's disease. Neurochem Res. 2008; 33(3): 589–597.
  7. Youn JK, Kim DW, Kim ST, et al. PEP-1-HO-1 prevents MPTP-induced degeneration of dopaminergic neurons in a Parkinson's disease mouse model. BMB Rep. 2014; 47(10): 569–574.
  8. Gagliardi S, Ghirmai S, Abel KJ, et al. Evaluation in vitro of synthetic curcumins as agents promoting monocytic gene expression related to β-amyloid clearance. Chem Res Toxicol. 2012; 25(1): 101–112.
  9. Sandur SK, Pandey MK, Sung B, et al. Curcumin, demethoxycurcumin, bisdemethoxycurcumin, tetrahydrocurcumin and turmerones differentially regulate anti-inflammatory and anti-proliferative responses through a ROS-independent mechanism. Carcinogenesis. 2007; 28(8): 1765–1773.
  10. Ramezani M, Hatamipour M, Sahebkar A. Promising anti-tumor properties of bisdemethoxycurcumin: A naturally occurring curcumin analogue. J Cell Physiol. 2018; 233(2): 880–887.
  11. Basile V, Ferrari E, Lazzari S, et al. Curcumin derivatives: molecular basis of their anti-cancer activity. Biochem Pharmacol. 2009; 78(10): 1305–1315.
  12. Jenner P. Oxidative stress in Parkinson's disease. Ann Neurol. 2003; 53 Suppl 3: S26–36; discussion S36.
  13. Reynolds A, Laurie C, Mosley RL, et al. Oxidative Stress and the Pathogenesis of Neurodegenerative Disorders. Int Rev Neurobiol. 2007: 297–325.
  14. La Fortezza M, Schenk M, Cosolo A, et al. JAK/STAT signalling mediates cell survival in response to tissue stress. Development. 2016; 143(16): 2907–2919.
  15. Hoffmann CJ, Harms U, Rex A, et al. Vascular signal transducer and activator of transcription-3 promotes angiogenesis and neuroplasticity long-term after stroke. Circulation. 2015; 131(20): 1772–1782.
  16. Eum WS, Shin MJ, Lee CH, et al. Neuroprotective effects of Tat-ATOX1 protein against MPP-induced SH-SY5Y cell deaths and in MPTP-induced mouse model of Parkinson's disease. Biochimie. 2019; 156: 158–168.
  17. Park SI, Lee EH, Kim SoRa, et al. Anti-apoptotic effects of Curcuma longa L. extract and its curcuminoids against blue light-induced cytotoxicity in A2E-laden human retinal pigment epithelial cells. J Pharm Pharmacol. 2017; 69(3): 334–340.
  18. Im JH, Yeo InJ, Hwang CJu, et al. PEGylated Erythropoietin Protects against Brain Injury in the MCAO-Induced Stroke Model by Blocking NF-κB Activation. Biomol Ther (Seoul). 2020; 28(2): 152–162.
  19. Chen S, Hou Y, Zhao Z, et al. Neuregulin-1 Accelerates Functional Motor Recovery by Improving Motoneuron Survival After Brachial Plexus Root Avulsion in Mice. Neuroscience. 2019; 404: 510–518.
  20. Li J, Chen S, Zhao Z, et al. Effect of VEGF on Inflammatory Regulation, Neural Survival, and Functional Improvement in Rats following a Complete Spinal Cord Transection. Front Cell Neurosci. 2017; 11: 381.
  21. Chen SX, He JH, Mi YJ, et al. A mimetic peptide of α2,6-sialyllactose promotes neuritogenesis. Neural Regen Res. 2020; 15(6): 1058–1065.
  22. Yuhai GU, Zhen Z. Significance of the changes occurring in the levels of interleukins, SOD and MDA in rat pulmonary tissue following exposure to different altitudes and exposure times. Exp Ther Med. 2015; 10(3): 915–920.
  23. Mao GX, Zheng LD, Cao YB, et al. Antiaging effect of pine pollen in human diploid fibroblasts and in a mouse model induced by D-galactose. Oxid Med Cell Longev. 2012; 2012: 750963.
  24. Zhang Bo, Chen Na, Chen H, et al. The critical role of redox homeostasis in shikonin-induced HL-60 cell differentiation via unique modulation of the Nrf2/ARE pathway. Oxid Med Cell Longev. 2012; 2012: 781516.
  25. Xu J, Hu C, Chen S, et al. Neuregulin-1 protects mouse cerebellum against oxidative stress and neuroinflammation. Brain Res. 2017; 1670: 32–43.
  26. Chen Sx, Hu Cl, Liao Yh, et al. L1 modulates PKD1 phosphorylation in cerebellar granule neurons. Neurosci Lett. 2015; 584: 331–336.
  27. Jiang Q, Chen S, Hu C, et al. Neuregulin-1 (Nrg1) signaling has a preventive role and is altered in the frontal cortex under the pathological conditions of Alzheimer's disease. Mol Med Rep. 2016; 14(3): 2614–2624.
  28. Vogt Weisenhorn DM, Giesert F, Wurst W. Diversity matters - heterogeneity of dopaminergic neurons in the ventral mesencephalon and its relation to Parkinson's Disease. J Neurochem. 2016; 139 Suppl 1: 8–26.
  29. Olanow CW, Schapira AHV, Agid Y. Neuroprotection for Parkinson's disease: prospects and promises. Ann Neurol. 2003; 53 Suppl 3: S1–S2.
  30. Xie Hr, Hu Ls, Li Gy. SH-SY5Y human neuroblastoma cell line: in vitro cell model of dopaminergic neurons in Parkinson's disease. Chin Med J (Engl). 2010; 123(8): 1086–1092.
  31. Xicoy H, Wieringa Bé, Martens GJM. The SH-SY5Y cell line in Parkinson's disease research: a systematic review. Mol Neurodegener. 2017; 12(1): 10.
  32. Morales-Garcia JA, Aguilar-Morante D, Hernandez-Encinas E, et al. Silencing phosphodiesterase 7B gene by lentiviral-shRNA interference attenuates neurodegeneration and motor deficits in hemiparkinsonian mice. Neurobiol Aging. 2015; 36(2): 1160–1173.
  33. Dexter DT, Jenner P. Parkinson disease: from pathology to molecular disease mechanisms. Free Radic Biol Med. 2013; 62: 132–144.
  34. Agrawal S, Singh A, Tripathi P, et al. Cypermethrin-induced nigrostriatal dopaminergic neurodegeneration alters the mitochondrial function: a proteomics study. Mol Neurobiol. 2015; 51(2): 448–465.
  35. Lee HJ, Shin SY, Choi C, et al. Formation and removal of alpha-synuclein aggregates in cells exposed to mitochondrial inhibitors. J Biol Chem. 2002; 277(7): 5411–5417.
  36. Zheng Wx, Wang F, Cao Xl, et al. Baicalin protects PC-12 cells from oxidative stress induced by hydrogen peroxide via anti-apoptotic effects. Brain Inj. 2014; 28(2): 227–234.