Oridonin, a novel lysine acetyltransferases inhibitor, inhibits proliferation and induces apoptosis in gastric cancer cells through p53-and caspase-3-mediated mechanisms

Oncotarget

Volumn 7, Issue 16, 2016, Pages 22623-22631

  Shi, Min ^a   Lu, Xiao Jie ^a,b   Zhang, Juan ^c   Diao, Hua ^d   Li, Guangming ^e   Xu, Ling ^a   Wang, Ting ^a   Wei, Jue ^a   Meng, Wenying ^a   Ma, Jia Li ^a   Yu, Heguo ^d   Wang, Yu Gang ^a  

^a SHANGHAI JIAO TONG UNIVERSITY SCHOOL OF MEDICINE   (China)

^b SOUTHEAST UNIVERSITY   (China)

^c XUZHOU MEDICAL UNIVERSITY   (China)

^d FUDAN UNIVERSITY   (China)

^e XINHUA HOSPITAL AFFILIATED TO SHANGHAI JIAO TONG UNIVERSITY SCHOOL OF MEDICINE   (China)

Author keywords

Antiproliferation; Apoptosis; Gastric cancer; Lysine acetyltransferase inhibitor; Oridonin

Indexed keywords

1,4 DIAMINO 1,4 BIS(2 AMINOPHENYLTHIO) 2,3 DICYANOBUTADIENE; 2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; ACYLTRANSFERASE; ASBUTYROLACTONE 3; CASPASE 3; CURCUMIN; ENZYME INHIBITOR; GARCINOL; HISTONE ACETYLTRANSFERASE GCN5; HISTONE ACETYLTRANSFERASE PCAF; LYSINE ACETYLTRANSFERASE INHIBITOR; NATURAL PRODUCT; ORIDONIN; PIFITHRIN ALPHA; PROTEIN P53; TRICHOSTATIN A; UNCLASSIFIED DRUG; ANTINEOPLASTIC AGENT; CASP3 PROTEIN, HUMAN; KAURANE DERIVATIVE; LYSINE ACETYLTRANSFERASE; TP53 PROTEIN, HUMAN;

ANTINEOPLASTIC ACTIVITY; ANTIPROLIFERATIVE ACTIVITY; APOPTOSIS; ARTICLE; CANCER CELL; CANCER INHIBITION; CELL PROLIFERATION; CONCENTRATION RESPONSE; CONTROLLED STUDY; DOWN REGULATION; DRUG STRUCTURE; ENZYME ACTIVATION; ENZYME INHIBITION; GENE EXPRESSION REGULATION; HUMAN; HUMAN CELL; MITOCHONDRIAL MEMBRANE POTENTIAL; STOMACH CANCER; ANTAGONISTS AND INHIBITORS; DRUG EFFECTS; METABOLISM; PATHOLOGY; STOMACH TUMOR; TUMOR CELL LINE;

ANTINEOPLASTIC AGENTS; APOPTOSIS; CASPASE 3; CELL LINE, TUMOR; CELL PROLIFERATION; DITERPENES, KAURANE; ENZYME INHIBITORS; HUMANS; LYSINE ACETYLTRANSFERASES; STOMACH NEOPLASMS; TUMOR SUPPRESSOR PROTEIN P53;

EID: 84965020812     PISSN: None     EISSN: 19492553     Source Type: Journal    
DOI: 10.18632/oncotarget.8033     Document Type: Article

References (36)

1. Jemal A, Bray F, Center MM, Ferlay J, Ward E, Forman D. Global cancer statistics. CA Cancer J Clin. 2011; 61:69-90.
2. Hartgrink HH, Jansen EP, van Grieken NC, van de Velde CJ. Gastric cancer. Lancet. 2009; 374:477-90.
3. Wesolowski R, Lee C, Kim R. Is there a role for second-line chemotherapy in advanced gastric cancer? Lancet Oncol. 2009; 10:903-12.
4. Zhou GB, Chen SJ, Wang ZY, Chen Z. Back to the future of oridonin: again, compound from medicinal herb shows potent antileukemia efficacies in vitro and in vivo. Cell Res. 2007; 17:274-6.
5. Tang W, Eisenbrand G. Chinese drugs of plant origin: chemistry, pharmacology, and use in traditional and modern medicine. Berlin: Springer-Verlag 1992:817-847.
6. Li XT, Lin C, Li PY. [Characteristics of the cytostatic effects of oridonin in vitro]. [Article in Chinese]. Zhongguo Yao Li Xue Bao. 1986; 7:361-3.
7. Weng H, Huang H, Dong B, Zhao P, Zhou H, Qu L. Inhibition of miR-17 and miR-20a by oridonin triggers apoptosis and reverses chemoresistance by derepressing BIM-S. Cancer Res. 2014; 74:4409-4419.
8. Duan C, Gao J, Zhang D, Jia L, Liu Y, Zheng D, Liu G, Tian X, Wang F, Zhang Q. Galactose-decorated pH-responsive nanogels for hepatoma-targeted delivery of oridonin. Biomacromolecules. 2011; 12:4335-43.
9. Qi X, Zhang D, Xu X, Feng F, Ren G, Chu Q, Zhang Q, Tian K. Oridonin nanosuspension was more effective than free oridonin on G2/M cell cycle arrest and apoptosis in the human pancreatic cancer PANC-1 cell line. Int J Nanomedicine. 2012; 7:1793-804.
10. Cheng Y, Qiu F, Ikejima T. Molecular mechanisms of oridonin-induced apoptosis and autophagy in murine fibrosarcoma L929 cells. Autophagy. 2009; 5:430-431.
11. Cui Q, Tashiro S, Onodera S, Minami M, Ikejima T. Oridonin induced autophagy in human cervical carcinoma HeLa cells through Ras, JNK, and P38 regulation. J Pharmacol Sci. 2007 Dec; 105:317-25.
12. Haberland M, Montgomery RL, Olson EN. The many roles of histone deacetylases in development and physiology: implications for disease and therapy. Nat Rev Genet. 2009; 10:32-42.
13. Falkenberg KJ, Johnstone RW. Histone deacetylases and their inhibitors in cancer, neurological diseases and immune disorders. Nat Rev Drug Discov. 2014; 13:673-91.
14. Xu W, Li Y, Liu C, Zhao S. Protein lysine acetylation guards metabolic homeostasis to fight against cancer. Oncogene. 2014; 33:2279-2285.
15. Iyer A, Fairlie DP, Brown L. Lysine acetylation in obesity, diabetes and metabolic disease. Iyer A, Fairlie DP, Brown L. Lysine acetylation in obesity, diabetes and metabolic disease. Immunol Cell Biol. 2012; 90:39-46.
16. Faya M, Jia D, Liu Y. Targeting Apoptosis Pathways in Cancer and Perspectives with Natural Compounds from Mother Nature. Cancer Prev Res. 2014; 7.
17. Gryder BE, Sodji QH, Oyelere AK. Targeted cancer therapy: giving histone deacetylase inhibitors all they need to succeed. Future Med Chem. 2012; 4:505-24.
18. New M, Olzscha H, La Thangue NB. KDAC inhibitorbased therapies: can we interpret the code? Mol Oncol. 2012; 6:637-656.
19. Kim HJ, Bae SC. Histone deacetylase inhibitors: molecular mechanisms of action and clinical trials as anti-cancer drugs. Am J Transl Res. 2011; 3:166-79.
20. Souto JA, Conte M, Alvarez R. Synthesis of benzamides related to anacardic acid and their histone acetyltransferase (KAT) inhibitory activities. ChemMedChem. 2008; 3:1435-42.
21. K Choi, J Yoon S, Kwon. Epigallocatechin-3-gallate, a histone acetyltransferase inhibitor, inhibits EBV-induced B lymphocyte transformation via suppression of RelA acetylation. Cancer Res. 2009; 69:583-92.
22. Sun H, Yang X, Zhu J, Lv T, Chen Y, Chen G, Zhong L, Li Y, Huang X, Huang G, Tian J. Inhibition of p300-HAT results in a reduced histone acetylation and down-regulation of gene expression in cardiac myocytes. Life Sci. 2010; 87:707-14.
23. K Balasubramanyam, M Altaf, RA Varier. Polyisoprenylated benzophenone, garcinol, a natural KAT inhibitor represses chromatin transcription and alters global gene expression. J Biol Chem. 2004; 279:33716-26.
24. Legartová S, Stixová L, Strnad H, Kozubek S, Martinet N, Dekker FJ, Franek M, Bártová E. Basic nuclear processes affected by histone acetyltransferases and histone deacetylase inhibitors. Epigenomics. 2013; 5:379-96.
25. Czabotar PE, Lessene G, Strasser A, Adams JM. Control of apoptosis by the BCL-2 protein family: implications for physiology and therapy. Nat Rev Mol Cell Biol. 2014; 15:49-63.
26. Green DR, Reed JC. Mitochondria and apoptosis. Science. 1998; 281:1309-12.
27. Brooks CL, Gu W. The impact of acetylation and deacetylation on the p53 pathway. Protein Cell. 2011; 2:456-62.
28. Jain AK, Allton K, Iacovino M, Mahen E, Milczarek RJ, Zwaka TP, Kyba M, Barton MC. p53 regulates cell cycle and microRNAs to promote differentiation of human embryonic stem cells. PLoS Biol. 2012; 10:e1001268.
29. Gu W, Roeder RG. Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell. 1997; 90:595-606.
30. Harbauer AB, Opalinska M, Gerbeth C, Herman JS, Rao S, Schönfisch B, Guiard B, Schmidt O, Pfanner N, Meisinger C. Mitochondria. Cell cycle-dependent regulation of mitochondrial preprotein translocase. Science. 2014; 346:1109-13.
31. Xavier JM, Morgado AL, Rodrigues CM, Solá S. Tauroursodeoxycholic acid increases neural stem cell pool and neuronal conversion by regulating mitochondria-cell cycle retrograde signaling. Cell Cycle. 2014; 13:3576-89.
32. Liu H, Qian C, Shen Z. Anti-tumor activity of oridonin on SNU-5 subcutaneous xenograft model via regulation of c-Met pathway. Tumour Biol. 2014; 35:9139-46.
33. Yu H, Dong J, Gu Y, Liu H, Xin A, Shi H, Sun F, Zhang Y, Lin D, Diao H. The novel human β-defensin 114 regulates lipopolysaccharide (LPS)-mediated inflammation and protects sperm from motility loss. J Biol Chem. 2013; 288:12270-82.
34. Dal Piaz F, Cotugno R, Lepore L, Vassallo A, Malafronte N, Lauro G, Bifulco G, Belisario MA, De Tommasi N. Chemical proteomics reveals HSP70 1A as a target for the anticancer diterpene oridonin in Jurkat cells. J Proteomics. 2013; 82:14-26.
35. Sakamuro D, Sabbatini P, White E, Prendergast GC. The polyproline region of p53 is required to activate apoptosis but not growth arrest. Oncogene. 1997, 15:887-898.
36. Jin G, Westphalen CB, Hayakawa Y, Worthley DL, Asfaha S, Yang X, Chen X, Si Y, Wang H, Tailor Y, Friedman RA, Wang TC. Progastrin stimulates colonic cellproliferation via CCK2R-and β-arrestin-dependent suppression of BMP2. Gastroenterology. 2013; 145:820-30.e10.