Butyrate suppresses motility of colorectal cancer cells via deactivating Akt/ERK signaling in histone deacetylase dependent manner

Journal of Pharmacological Sciences

Volumn 135, Issue 4, 2017, Pages 148-155

  Li, Qingran ^a   Ding, Chujie ^a   Meng, Tuo ^a   Lu, Wenjie ^a   Liu, Wenyue ^a   Hao, Haiping ^a   Cao, Lijuan ^a  

^a CHINA PHARMACEUTICAL UNIVERSITY   (China)

Author keywords

Butyrate; Colorectal cancer; Histone deacetylase; Metastasis; Motility

Indexed keywords

BUTYRIC ACID; HISTONE DEACETYLASE 3; HISTONE DEACETYLASE INHIBITOR; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PROTEIN KINASE B; SMALL INTERFERING RNA; SUBERANILOHYDROXAMIC ACID; UNCLASSIFIED DRUG; BUTYRIC ACID DERIVATIVE; HISTONE DEACETYLASE; HYDROXAMIC ACID; VORINOSTAT;

AKT SIGNALING; ARTICLE; CANCER CHEMOTHERAPY; CELL ACTIVITY; CELL MOTILITY; COLORECTAL CANCER CELL LINE; CONTROLLED STUDY; DRUG EFFECT; DRUG TARGETING; ENZYME INACTIVATION; HCT 116 CELL LINE; HCT 8 CELL LINE; HEALTH CARE MANAGEMENT; HT-29 CELL LINE; HUMAN; HUMAN CELL; IN VITRO STUDY; LOVO CELL LINE; METASTATIC COLORECTAL CANCER; PATHOPHYSIOLOGY; PROTEIN TARGETING; WOUND HEALING; CELL MOTION; COLORECTAL TUMOR; DRUG EFFECTS; MAPK SIGNALING; METABOLISM; METASTASIS; MOLECULARLY TARGETED THERAPY; PATHOLOGY; PHYSIOLOGY; TUMOR CELL LINE;

BUTYRATES; CELL LINE, TUMOR; CELL MOVEMENT; COLORECTAL NEOPLASMS; HISTONE DEACETYLASE INHIBITORS; HISTONE DEACETYLASES; HUMANS; HYDROXAMIC ACIDS; MAP KINASE SIGNALING SYSTEM; MOLECULAR TARGETED THERAPY; NEOPLASM METASTASIS;

EID: 85039850255     PISSN: 13478613     EISSN: 13478648     Source Type: Journal    
DOI: 10.1016/j.jphs.2017.11.004     Document Type: Article

References (40)

1. Ciombor, K.K., Wu, C., Goldberg, R.M., Recent therapeutic advances in the treatment of colorectal cancer. Annu Rev Med 66 (2015), 83–95.
2. Gupta, G.P., Massague, J., Cancer metastasis: building a framework. Cell 127 (2006), 679–695.
3. Nicholson, J.K., Holmes, E., Kinross, J., et al. Host-gut microbiota metabolic interactions. Science 336 (2012), 1262–1267.
4. Louis, P., Hold, G.L., Flint, H.J., The gut microbiota, bacterial metabolites and colorectal cancer. Nat Rev Microbiol 12 (2014), 661–672.
5. Koh, A., De Vadder, F., Kovatcheva-Datchary, P., et al. From dietary fiber to host physiology: short-chain fatty acids as Key bacterial metabolites. Cell 165 (2016), 1332–1345.
6. Fung, K.Y., Cosgrove, L., Lockett, T., et al. A review of the potential mechanisms for the lowering of colorectal oncogenesis by butyrate. Br J Nutr 108 (2012), 820–831.
7. Singh, N., Gurav, A., Sivaprakasam, S., et al. Activation of Gpr109a, receptor for niacin and the commensal metabolite butyrate, suppresses colonic inflammation and carcinogenesis. Immunity 40 (2014), 128–139.
8. Li, X., Mikkelsen, I.M., Mortensen, B., et al. Butyrate reduces liver metastasis of rat colon carcinoma cells in vivo and resistance to oxidative stress in vitro. Clin Exp Metastasis 21 (2004), 331–338.
9. Emenaker, N.J., Calaf, G.M., Cox, D., et al. Short-chain fatty acids inhibit invasive human colon cancer by modulating uPA, TIMP-1, TIMP-2, mutant p53, Bcl-2, Bax, p21 and PCNA protein expression in an in vitro cell culture model. J Nutr, 131, 2001 3041S–6S.
10. Han, A., Bennett, N., MacDonald, A., et al. Cellular metabolism and dose reveal carnitine-dependent and -independent mechanisms of butyrate oxidation in colorectal cancer cells. J Cell Physiol 231 (2016), 1804–1813.
11. Zeng, H., Briske-Anderson, M., Prolonged butyrate treatment inhibits the migration and invasion potential of HT1080 tumor cells. J Nutr 135 (2005), 291–295.
12. Cantoni, S., Galletti, M., Zambelli, F., et al. Sodium butyrate inhibits platelet-derived growth factor-induced proliferation and migration in pulmonary artery smooth muscle cells through Akt inhibition. FEBS J 280 (2013), 2042–2055.
13. Maa, M.C., Chang, M.Y., Hsieh, M.Y., et al. Butyrate reduced lipopolysaccharide-mediated macrophage migration by suppression of Src enhancement and focal adhesion kinase activity. J Nutr Biochem 21 (2010), 1186–1192.
14. Meng, J., Zhang, H.H., Zhou, C.X., et al. The histone deacetylase inhibitor trichostatin A induces cell cycle arrest and apoptosis in colorectal cancer cells via p53-dependent and -independent pathways. Oncol Rep 28 (2012), 384–388.
15. Hsi, L.C., Xi, X., Lotan, R., et al. The histone deacetylase inhibitor suberoylanilide hydroxamic acid induces apoptosis via induction of 15-lipoxygenase-1 in colorectal cancer cells. Cancer Res 64 (2004), 8778–8781.
16. Bracker, T.U., Sommer, A., Fichtner, I., et al. Efficacy of MS-275, a selective inhibitor of class I histone deacetylases, in human colon cancer models. Int J Oncol 35 (2009), 909–920.
17. Wilson, A.J., Byun, D.S., Popova, N., et al. Histone deacetylase 3 (HDAC3) and other class I HDACs regulate colon cell maturation and p21 expression and are deregulated in human colon cancer. J Biol Chem 281 (2006), 13548–13558.
18. Spurling, C.C., Godman, C.A., Noonan, E.J., et al. HDAC3 overexpression and colon cancer cell proliferation and differentiation. Mol Carcinog 47 (2008), 137–147.
19. Chou, C.W., Wu, M.S., Huang, W.C., et al. HDAC inhibition decreases the expression of EGFR in colorectal cancer cells. PLoS One, 6, 2011, e18087.
20. Godman, C.A., Joshi, R., Tierney, B.R., et al. HDAC3 impacts multiple oncogenic pathways in colon cancer cells with effects on Wnt and vitamin D signaling. Cancer Biol Ther 7 (2008), 1570–1580.
21. Kim, H.C., Choi, K.C., Choi, H.K., et al. HDAC3 selectively represses CREB3-mediated transcription and migration of metastatic breast cancer cells. Cell Mol Life Sci 67 (2010), 3499–3510.
22. Hayashi, A., Horiuchi, A., Kikuchi, N., et al. Type-specific roles of histone deacetylase (HDAC) overexpression in ovarian carcinoma: HDAC1 enhances cell proliferation and HDAC3 stimulates cell migration with downregulation of E-cadherin. Int J Cancer 127 (2010), 1332–1346.
23. Zhu, J., Wan, H., Xue, C., et al. Histone deacetylase 3 implicated in the pathogenesis of children glioma by promoting glioma cell proliferation and migration. Brain Res 1520 (2013), 15–22.
24. Xue, G., Hemmings, B.A., PKB/Akt-dependent regulation of cell motility. J Natl Cancer Inst 105 (2013), 393–404.
25. Chen, G., Yue, Y., Qin, J., et al. Plumbagin suppresses the migration and invasion of glioma cells via downregulation of MMP-2/9 expression and inaction of PI3K/Akt signaling pathway in vitro. J Pharmacol Sci 134 (2017), 59–67.
26. Wu, W.S., Wu, J.R., Hu, C.T., Signal cross talks for sustained MAPK activation and cell migration: the potential role of reactive oxygen species. Cancer Metastasis Rev 27 (2008), 303–314.
27. Kim, J.H., Kim, M.S., Bak, Y., et al. The cadin-2-en-1beta-ol-1beta-D-glucuronopyranoside suppresses TPA-mediated matrix metalloproteinase-9 expression through the ERK signaling pathway in MCF-7 human breast adenocarcinoma cells. J Pharmacol Sci 118 (2012), 198–205.
28. Huang, C., Jacobson, K., Schaller, M.D., MAP kinases and cell migration. J Cell Sci 117 (2004), 4619–4628.
29. Li, L.H., Zheng, M.H., Luo, Q., et al. P21-activated protein kinase 1 induces colorectal cancer metastasis involving ERK activation and phosphorylation of FAK at Ser-910. Int J Oncol 37 (2010), 951–962.
30. Gout, S., Morin, C., Houle, F., et al. Death receptor-3, a new E-Selectin counter-receptor that confers migration and survival advantages to colon carcinoma cells by triggering p38 and ERK MAPK activation. Cancer Res 66 (2006), 9117–9124.
31. Agarwal, E., Brattain, M.G., Chowdhury, S., Cell survival and metastasis regulation by Akt signaling in colorectal cancer. Cell Signal 25 (2013), 1711–1719.
32. Liang, X., Kong, P., Wang, J., et al. Effects of metformin on proliferation and apoptosis of human megakaryoblastic Dami and MEG-01 cells. J Pharmacol Sci 135 (2017), 14–21.
33. Ye, Q., Cai, W., Zheng, Y., et al. ERK and AKT signaling cooperate to translationally regulate survivin expression for metastatic progression of colorectal cancer. Oncogene 33 (2014), 1828–1839.
34. Zhao, J., Ou, B., Han, D., et al. Tumor-derived CXCL5 promotes human colorectal cancer metastasis through activation of the ERK/Elk-1/Snail and AKT/GSK3beta/beta-catenin pathways. Mol Cancer, 16, 2017, 70.
35. Do, K., Speranza, G., Bishop, R., et al. Biomarker-driven phase 2 study of MK-2206 and selumetinib (AZD6244, ARRY-142886) in patients with colorectal cancer. Invest New Drugs 33 (2015), 720–728.
36. Janku, F., Hong, D.S., Fu, S., et al. Assessing PIK3CA and PTEN in early-phase trials with PI3K/AKT/mTOR inhibitors. Cell Rep 6 (2014), 377–387.
37. Do, K., Cao, L., Kang, Z., et al. A phase II study of sorafenib combined with cetuximab in EGFR-expressing, KRAS-mutated metastatic colorectal cancer. Clin Colorectal Cancer 14 (2015), 154–161.
38. Wells, A., Grahovac, J., Wheeler, S., et al. Targeting tumor cell motility as a strategy against invasion and metastasis. Trends Pharmacol Sci 34 (2013), 283–289.
39. Nakamura, K., Shinozuka, K., Yoshikawa, N., Anticancer and antimetastatic effects of cordycepin, an active component of Cordyceps sinensis. J Pharmacol Sci 127 (2015), 53–56.
40. Palmer, T.D., Ashby, W.J., Lewis, J.D., et al. Targeting tumor cell motility to prevent metastasis. Adv Drug Deliv Rev 63 (2011), 568–581.