Curcumin Inhibited Podocyte Cell Apoptosis and Accelerated Cell Autophagy in Diabetic Nephropathy via Regulating Beclin1/UVRAG/Bcl2

References

• Gnudi L, Coward RJM, Long DA. Diabetic nephropathy: perspective on novel molecular mechanisms. Trends Endocrinol Metab. 2016;27(11):820–830. doi:10.1016/j.tem.2016.07.002
   PubMed Web of Science ®Google Scholar
• Al-rubeaan K, Siddiqui K, Alghonaim M, Youssef AM, AlNaqeb D. The Saudi Diabetic Kidney Disease study (Saudi-DKD): clinical characteristics and biochemical parameters. Ann Saudi Med. 2018;38(1):46–56. doi:10.5144/0256-4947.2018.03.01.1010
   PubMed Web of Science ®Google Scholar
• Kim YI, Kim CH, Choi CS, et al. Microalbuminuria is associated with the insulin resistance syndrome independent of hypertension and type 2 diabetes in the Korean population. Diabetes Res Clin Pract. 2001;52(2):145–152. doi:10.1016/S0168-8227(01)00228-5
   PubMed Web of Science ®Google Scholar
• Doshi SM, Friedman AN. Diagnosis and management of Type 2 diabetic kidney disease. Clin J Am Soc Nephrol. 2017;12(8):1366–1373. doi:10.2215/CJN.11111016
   PubMed Web of Science ®Google Scholar
• Van Buren PN, Toto R. Current update in the management of diabetic nephropathy. Curr Diabetes Rev. 2013;9(1):62–77. doi:10.2174/157339913804143207
   PubMedGoogle Scholar
• Lopez-vargas PA, Tong A, Howell M, Craig JC. Educational interventions for patients with CKD: a systematic review. Am J Kidney Dis. 2016;68(3):353–370. doi:10.1053/j.ajkd.2016.01.022
   PubMed Web of Science ®Google Scholar
• DeFronzo RA, Norton L, Abdul-ghani M. Renal, metabolic and cardiovascular considerations of SGLT2 inhibition. Nat Rev Nephrol. 2017;13(1):11–26. doi:10.1038/nrneph.2016.170
   PubMed Web of Science ®Google Scholar
• Lin JS, Susztak K. Podocytes: the weakest link in diabetic kidney disease? Curr Diab Rep. 2016;16(5):45. doi:10.1007/s11892-016-0735-5
   PubMed Web of Science ®Google Scholar
• Muhldorfer J, Pfister E, Buttner-herold M, Klewer M, Amann K, Daniel C. Bi-nucleation of podocytes is uniformly accompanied by foot processes widening in renal disease. Nephrol Dialysis Transplant. 2018;33(5):796–803. doi:10.1093/ndt/gfx201
   PubMedGoogle Scholar
• Jourdan T, Park JK, Varga ZV, et al. Cannabinoid-1 receptor deletion in podocytes mitigates both glomerular and tubular dysfunction in a mouse model of diabetic nephropathy. Diabetes Obes Metab. 2018;20(3):698–708. doi:10.1111/dom.13150
   PubMed Web of Science ®Google Scholar
• Yasuda-yamahara M, Kume S, Tagawa A, Maegawa H, Uzu T. Emerging role of podocyte autophagy in the progression of diabetic nephropathy. Autophagy. 2015;11(12):2385–2386. doi:10.1080/15548627.2015.1115173
   PubMed Web of Science ®Google Scholar
• Tagawa A, Yasuda M, Kume S, et al. Impaired podocyte autophagy exacerbates proteinuria in diabetic nephropathy. Diabetes. 2016;65(3):755–767. doi:10.2337/db15-0473
   PubMed Web of Science ®Google Scholar
• Mizushima N, Komatsu M. Autophagy: renovation of cells and tissues. Cell. 2011;147(4):728–741. doi:10.1016/j.cell.2011.10.026
   PubMed Web of Science ®Google Scholar
• Roohbakhsh A, Shirani K, Karimi G. Methamphetamine-induced toxicity: the role of autophagy? Chem Biol Interact. 2016;260:163–167. doi:10.1016/j.cbi.2016.10.012
   PubMed Web of Science ®Google Scholar
• Li B, Chen R, Chen L, et al. Effects of DDIT4 in methamphetamine-induced autophagy and apoptosis in dopaminergic neurons. Mol Neurobiol. 2017;54(3):1642–1660. doi:10.1007/s12035-015-9637-9
   PubMed Web of Science ®Google Scholar
• Ding Y, Choi ME. Autophagy in diabetic nephropathy. J Endocrinol. 2015;224(1):R15–30. doi:10.1530/JOE-14-0437
   PubMed Web of Science ®Google Scholar
• Funderburk SF, Wang QJ, Yue Z, Beclin T. 1-VPS34 complex–at the crossroads of autophagy and beyond. Trends Cell Biol. 2010;20(6):355–362. doi:10.1016/j.tcb.2010.03.002
   PubMed Web of Science ®Google Scholar
• Liu Y, Zhang J, Wang Y, Zeng X. Apelin involved in progression of diabetic nephropathy by inhibiting autophagy in podocytes. Cell Death Dis. 2017;8(8):e3006. doi:10.1038/cddis.2017.414
   PubMed Web of Science ®Google Scholar
• Tian B, Wang Z, Zhao Y, et al. Effects of curcumin on bladder cancer cells and development of urothelial tumors in a rat bladder carcinogenesis model. Cancer Lett. 2008;264(2):299–308. doi:10.1016/j.canlet.2008.01.041
   PubMed Web of Science ®Google Scholar
• Ramsewak RS, DeWitt DL, Nair MG. Cytotoxicity, antioxidant and anti-inflammatory activities of curcumins I-III from Curcuma longa. Phytomedicine. 2000;7(4):303–308. doi:10.1016/S0944-7113(00)80048-3
   PubMed Web of Science ®Google Scholar
• Zha W, Bai Y, Xu L, et al. Curcumin attenuates testicular injury in rats with streptozotocin-induced diabetes. Biomed Res Int. 2018;2018:7468019.
   PubMed Web of Science ®Google Scholar
• Hu S, Xu Y, Meng L, Huang L, Sun H. Curcumin inhibits proliferation and promotes apoptosis of breast cancer cells. Exp Ther Med. 2018;16(2):1266–1272. doi:10.3892/etm.2018.6345
   PubMed Web of Science ®Google Scholar
• Murray-stewart T, Dunworth M, Lui Y, Giardiello FM, Woster PM, Casero RA Jr. Curcumin mediates polyamine metabolism and sensitizes gastrointestinal cancer cells to antitumor polyamine-targeted therapies. PLoS One. 2018;13(8):e0202677. doi:10.1371/journal.pone.0202677
   PubMedGoogle Scholar
• Wang K, Tan SL, Lu Q, et al. Curcumin suppresses microRNA-7641-mediated regulation of p16 expression in bladder cancer. Am J Chin Med (Gard City N Y). 2018;1–12.
   Google Scholar
• Xu H, Gong Z, Zhou S, et al. Liposomal curcumin targeting endometrial cancer through the NF-kappaB pathway. Cell Physiol Biochem. 2018;48(2):569–582. doi:10.1159/000491886
   PubMedGoogle Scholar
• Chen G, Liu S, Pan R, et al. Curcumin attenuates gp120-induced microglial inflammation by inhibiting autophagy via the PI3K pathway. Cell Mol Neurobiol. 2018;38:1465–1477. doi:10.1007/s10571-018-0616-3
   PubMedGoogle Scholar
• Seo SU, Woo SM, Lee HS, Kim SH, Min KJ, Kwon TK. mTORC1/2 inhibitor and curcumin induce apoptosis through lysosomal membrane permeabilization-mediated autophagy. Oncogene. 2018;37:5205–5220. doi:10.1038/s41388-018-0345-6
   PubMed Web of Science ®Google Scholar
• Wang WH, Chen J, Zhang BR, et al. Curcumin inhibits proliferation and enhances apoptosis in A549 cells by downregulating lncRNA UCA1. Pharmazie. 2018;73(7):402–407. doi:10.1691/ph.2018.8402
   PubMed Web of Science ®Google Scholar
• Yao Q, Ke ZQ, Guo S, et al. Curcumin protects against diabetic cardiomyopathy by promoting autophagy and alleviating apoptosis. J Mol Cell Cardiol. 2018;124:26–34. doi:10.1016/j.yjmcc.2018.10.004
   PubMed Web of Science ®Google Scholar
• Soetikno V, Sari FR, Sukumaran V, et al. Curcumin decreases renal triglyceride accumulation through AMPK-SREBP signaling pathway in streptozotocin-induced type 1 diabetic rats. J Nutr Biochem. 2013;24(5):796–802. doi:10.1016/j.jnutbio.2012.04.013
   PubMed Web of Science ®Google Scholar
• Soetikno V, Watanabe K, Sari FR, et al. Curcumin attenuates diabetic nephropathy by inhibiting PKC-α and PKC-β1 activity in streptozotocin-induced type I diabetic rats. Mol Nutr Food Res. 2011;55(11):1655–1665. doi:10.1002/mnfr.v55.11
   PubMed Web of Science ®Google Scholar
• Gao P, Li L, Yang L, et al. 1 protein ameliorates diabetic nephropathy pathology through transcriptional repression of TGFbeta1. Sci Transl Med. 2019;11(510). doi:10.1126/scitranslmed.aav5519
   Google Scholar
• Wang JＲ, Zhao JJ, Ye CL, et al. Hypolipemic and hypoglycemic effects of total triterpenoids from Psidium guajava leaves on type 2 diabetic rats. Chin J Pathophysiol. 2012;28(6):1109.
   Google Scholar
• Zhao WC, Zhang B, Liao MJ, et al. Curcumin ameliorated diabetic neuropathy partially by inhibition of NADPH oxidase mediating oxidative stress in the spinal cord. Neurosci Lett. 2014;560:81–85. doi:10.1016/j.neulet.2013.12.019
   PubMed Web of Science ®Google Scholar
• Liu WT, Peng FF, Li HY, et al. Metadherin facilitates podocyte apoptosis in diabetic nephropathy. Cell Death Dis. 2016;7(11):e2477. doi:10.1038/cddis.2016.335
   PubMedGoogle Scholar
• Jankowski M, Piwkowska A, Rogacka D, Audzeyenka I, Janaszak-jasiecka A, Angielski S. Expression of membrane-bound NPP-type ecto-phosphodiesterases in rat podocytes cultured at normal and high glucose concentrations. Biochem Biophys Res Commun. 2011;416(1–2):64–69. doi:10.1016/j.bbrc.2011.10.144
   PubMedGoogle Scholar
• Zhu LN, Mei X, Zhang ZG, Xie YP, Lang F. Curcumin intervention for cognitive function in different types of people: a systematic review and meta-analysis. Phytother Res. 2019;33(3):524–533. doi:10.1002/ptr.6257
   PubMed Web of Science ®Google Scholar
• Khajehdehi P, Pakfetrat M, Javidnia K, et al. Oral supplementation of turmeric attenuates proteinuria, transforming growth factor-beta and interleukin-8 levels in patients with overt type 2 diabetic nephropathy: a randomized, double-blind and placebo-controlled study. Scand J Urol Nephrol. 2011;45(5):365–370. doi:10.3109/00365599.2011.585622
   PubMed Web of Science ®Google Scholar
• Feng Y, Chen S, Xu J, et al. Dysregulation of lncRNAs GM5524 and GM15645 involved in high-glucose-induced podocyte apoptosis and autophagy in diabetic nephropathy. Mol Med Rep. 2018. doi:10.3892/mmr.2018.9412
   Google Scholar
• Sifuentes-franco S, Padilla-tejeda DE, Carrillo-ibarra S, Miranda-diaz AG. Oxidative stress, apoptosis, and mitochondrial function in diabetic nephropathy. Int J Endocrinol. 2018;2018:1875870.
   PubMed Web of Science ®Google Scholar
• Tian N, Gao Y, Wang X, et al. Emodin mitigates podocytes apoptosis induced by endoplasmic reticulum stress through the inhibition of the PERK pathway in diabetic nephropathy. Drug Des Devel Ther. 2018;12:2195–2211. doi:10.2147/DDDT.S167405
   PubMed Web of Science ®Google Scholar
• Chang WW, Liang W, Yao XM, et al. Tumour necrosis factor-related apoptosis-inducing ligand expression in patients with diabetic nephropathy. J Renin Angiotensin Aldosterone Syst. 2018;19(3):1470320318785744. doi:10.1177/1470320318785744
   Web of Science ®Google Scholar
• Wang Y, Li H, Song SP. beta-arrestin 1/2 aggravates podocyte apoptosis of diabetic nephropathy via Wnt/beta-Catenin pathway. Med Sci Monitor. 2018;24:1724–1732.
   PubMedGoogle Scholar
• Lin -H-H, Chen J-H, Huang -C-C, Wang C-J. Apoptotic effect of 3,4-dihydroxybenzoic acid on human gastric carcinoma cells involving JNK/p38 MAPK signaling activation. Int J Cancer. 2007;120(11):2306–2316. doi:10.1002/(ISSN)1097-0215
   PubMedGoogle Scholar
• Scorrano L, Korsmeyer SJ. Mechanisms of cytochrome c release by proapoptotic BCL-2 family members. Biochem Biophys Res Commun. 2003;304(3):437–444. doi:10.1016/S0006-291X(03)00615-6
   PubMedGoogle Scholar
• Hartleben B, Gödel M, Meyer-schwesinger C, et al. Autophagy influences glomerular disease susceptibility and maintains podocyte homeostasis in aging mice. J Clin Invest. 2010;120(4):1084–1096. doi:10.1172/JCI39492
   PubMed Web of Science ®Google Scholar
• Qin Z, Yu X, Lin M, Wu J, Ma S, Wang N. Prognostic and clinicopathological value of Beclin-1 expression in hepatocellular carcinoma: a meta-analysis. World J Surg Oncol. 2018;16(1):170.
   PubMedGoogle Scholar
• Naguib M, Rashed LA. Serum level of the autophagy biomarker Beclin-1 in patients with diabetic kidney disease. Diabetes Res Clin Pract. 2018;143:56–61. doi:10.1016/j.diabres.2018.06.022
   PubMedGoogle Scholar
• Fernandez AF, Sebti S, Wei Y, et al. Disruption of the beclin 1-BCL2 autophagy regulatory complex promotes longevity in mice. Nature. 2018;558(7708):136–140. doi:10.1038/s41586-018-0162-7
   PubMed Web of Science ®Google Scholar
• Liang XH, Kleeman LK, Jiang HH, et al. Protection against fatal Sindbis virus encephalitis by beclin, a novel Bcl-2-interacting protein. J Virol. 1998;72(11):8586–8596. doi:10.1128/JVI.72.11.8586-8596.1998
   PubMed Web of Science ®Google Scholar
• Maiuri MC, Criollo A, Tasdemir E, et al. BH3-only proteins and BH3 mimetics induce autophagy by competitively disrupting the interaction between Beclin 1 and Bcl-2/Bcl-X(L). Autophagy. 2007;3(4):374–376. doi:10.4161/auto.4237
   PubMed Web of Science ®Google Scholar
• Pattingre S, Tassa A, Qu X, et al. Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy. Cell. 2005;122(6):927–939. doi:10.1016/j.cell.2005.07.002
   PubMed Web of Science ®Google Scholar
• Liang C, Feng P, Ku B, et al. Autophagic and tumour suppressor activity of a novel Beclin1-binding protein UVRAG. Nat Cell Biol. 2006;8(7):688–699. doi:10.1038/ncb1426
   PubMed Web of Science ®Google Scholar