Fatty acid binding protein 5 promotes the proliferation, migration, and invasion of hepatocellular carcinoma cells by degradation of Krüppel-like factor 9 mediated by miR-889-5p via cAMP-response element binding protein

References

• Beroukhim R, Mermel CH, Porter D, Wei G, Raychaudhuri S, Donovan J, Barretina J, Boehm JS, Dobson J, Urashima M, et al. 2010. The landscape of somatic copy-number alteration across human cancers. Nature. 463(7283):899–905. DOI:10.1038/nature08822
   PubMed Web of Science ®Google Scholar
• Mattison J, Kool J, Uren AG, de Ridder J, Wessels L, Jonkers J, Bignell GR, Butler A, Rust AG, Brosch M, et al. Novel candidate cancer genes identified by a large-scale cross-species comparative oncogenomics approach. Cancer Res. 2010;70(3):883–895. DOI:10.1158/0008-5472. CAN-09-1737.
   PubMed Web of Science ®Google Scholar
• Lu X, Sun W, Tang Y, Zhu L, Li Y, Ou C, Yang C, Su J, Luo C, Hu Y, et al. Identification of key genes in hepatocellular carcinoma and validation of the candidate gene, cdc25a, using gene set enrichment analysis, meta-analysis and cross-species comparison. Mol Med Rep. 2016;13(2):1172–1178. DOI:10.3892/mmr.2015.4646
   PubMed Web of Science ®Google Scholar
• LiY, WanDF, SuJJ,CaoJ, OuC, QiuXK, BanKC, YangC,QinLL, LuoD, etal. Differential expression of genes during aflatoxin B (1)-induced hepatocarcinogenesis in tree shrews. World JGastroenterol. 2004;10(4):497–504.DOI:10.3748/wjg.v10.i4.497
   PubMed Web of Science ®Google Scholar
• Liang HJ, Wei W, Kang XN, Guo K, Cao J, Su JJ, Yang C, Yang C, Li Y, Liu YK, et al. Differentially expressed proteins in the precancerous stage of rat hepatocarcinogenesis induced by diethylnitrosamine. Chin J Hepato. 2009;17(9):669–674. DOI:10.3760/cma.j.1007-3418.2009.09.008.
   PubMedGoogle Scholar
• Storch J, Corsico B. The emerging functions and mechanisms of mammalian fatty acid-binding proteins. Annu Rev Nutr. 2008;28(1):73–95. doi:10.1146/annurev.nutr. 27.061406.093710.
   PubMedGoogle Scholar
• Zimmerman AW, Veerkamp JH. 2002. New insights into the structure and function of fatty acid-binding proteins. Cell Mol Life Sci. 59(7):1096–1116. DOI:10.1007/s00018-002-8490-y.
   PubMed Web of Science ®Google Scholar
• Hotamisligil GS. 2006. Inflammation and metabolic disorders. Nature. 444(7121):860–867. doi:10.1038/nature05485.
   PubMed Web of Science ®Google Scholar
• Kawaguchi K, Kinameri A, Suzuki S, Senga S, Ke Y, Fujii H. 2016. The cancer-promoting gene fatty acid-binding protein 5 (FABP5) is epigenetically regulated during human prostate carcinogenesis. Biochem J. 473(4):449–461. doi:10.1042/BJ20150926.
   PubMedGoogle Scholar
• Wang Y, Wahafu A, Wu W, Xiang J, Huo L, Ma X, Wang N, Liu H, Bai X, Xu D, et al. 2021. FABP5 enhances malignancies of lower-grade gliomas via canonical activation of NF-κB signaling. J Cell Mol Med. 25(9):4487–4500. DOI:10.1111/jcmm.16536
   PubMed Web of Science ®Google Scholar
• Apaya MK, Hsiao PW, Yang YC, Shyur LF. 2020. Deregulating the CYP2C19/Epoxy-Eicosatrienoic acid-associated FABP4/FABP5 signaling network as a therapeutic approach for metastatic triple-negative breast cancer. Cancers (Basel). 12(1):199. doi:10.3390/cancers12010199.
   PubMed Web of Science ®Google Scholar
• Kawaguchi K, Senga S, Kubota C, Kawamura Y, Ke Y, Fujii H. 2016. High expression of fatty acid-binding protein 5 promotes cell growth and metastatic potential of colorectal cancer cells. FEBS Open Bio. 6(3):190–199. doi:10.1002/2211-5463.12031.
   PubMed Web of Science ®Google Scholar
• Zhang C, Liao Y, Liu P, Du Q, Liang Y, Ooi S, Qin S, He S, Yao S, Wang W. FABP5 promotes lymph node metastasis in cervical cancer by reprogramming fatty acid metabolism. Theranostics. 2020;10(15):6561–6580. doi:10.7150/thno. 44868.
   PubMed Web of Science ®Google Scholar
• Carbonetti G, Wilpshaar T, Kroonen J, Studholme K, Converso C, d’Oelsnitz S, Kaczocha M. 2019. FABP5 coordinates lipid signaling that promotes prostate cancer metastasis. Sci Rep. 9(1):18944. DOI:10.1038/s41598-019-55418-x.
   PubMedGoogle Scholar
• Seo J, Jeong DW, Park JW, Lee KW, Fukuda J, Chun YS. 2020. Fatty-acid-induced FABP5/HIF-1 reprograms lipid metabolism and enhances the proliferation of liver cancer cells. Commun Biol. 3(1):638. DOI:10.1038/s42003-020-01367-5.
   PubMed Web of Science ®Google Scholar
• Senga S, Kobayashi N, Kawaguchi K, Ando A, Fujii H. 2018. Fatty acid-binding protein 5 (FABP5) promotes lipolysis of lipid droplets, de novo fatty acid (FA) synthesis and activation of nuclear factor-kappa B (NF-κB) signaling in cancer cells. Biochim Biophys Acta Mol Cell Biol Lipids. 1863(9):1057–1067. DOI:10.1016/j.bbalip.2018.06.010.
   PubMed Web of Science ®Google Scholar
• Pan L, Xiao H, Liao R, Chen Q, Peng C, Zhang Y, Mu T, Wu Z. 2018. Fatty acid binding protein 5 promotes tumor angiogenesis and activates the IL6/ STAT3/ VEGFA pathway in hepatocellular carcinoma. Biomed Pharmacother. 106:68–76. DOI:10.1016/j.biopha.2018.06.040.
   PubMed Web of Science ®Google Scholar
• Llovet J, Bru C, Bruix J. 1999. Prognosis of hepatocellular carcinoma: the BCLC staging classification. Semin Liver Dis. 19(3):329–338. DOI:10.1055/s-2007-1007122.
   PubMed Web of Science ®Google Scholar
• Winer J, Jung CKS, Shackel I, Williams PM. 1999. Development and validation of real - time quantitative reverse transcriptase-polymerase chain reaction for monitoring gene expression in cardiac myocytes in vitro. Analytical Biochem. 270(1):41–49. DOI:10.1006/abio.1999.4085.
   PubMed Web of Science ®Google Scholar
• Simmen RC, Pabona JM, Velarde MC, Simmons C, Rahal O, Simmen FA. The emerging role of Krüppel-like factors in endocrine-responsive cancers of female reproductive tissues. J Endocrinol. 2010;204(3):223–231. DOI:10.1677/JOE-09-0329
   PubMed Web of Science ®Google Scholar
• Ohata T, Yokoo H, Kamiyama T, Fukai M, Aiyama T, Hatanaka Y, Hatanaka K, Wakayama K, Orimo T, Kakisaka T, et al. 2017. Fatty acid-binding protein 5 function in hepatocellular carcinoma through induction of epithelial-mesenchymal transition. Cancer Med. 6(5):1049–1061. DOI:10.1002/cam4.1020
   PubMed Web of Science ®Google Scholar
• Ohira M, Yokoo H, Ogawa K, Fukai M, Kamiyama T, Sakamoto N, Taketomi A. 2021. Serum fatty acid-binding protein 5 is a significant factor in hepatocellular carcinoma progression independent of tissue expression level. Carcinogenesis. 42(6):794–803. DOI:10.1093/carcin/bgab025.
   PubMed Web of Science ®Google Scholar
• Sapio L, Salzillo A, Ragone A, Illiano M, Spina A, Naviglio S. 2020. Targeting CREB in cancer therapy: a key candidate or one of many? An update. Cancers (Basel). 12(11):3166. DOI:10.3390/cancers12113166.
   PubMed Web of Science ®Google Scholar
• Yamamoto KK, Gonzalez GA, Biggs WH, Montminy MR. 1988. Phosphorylation-induced binding and transcriptional efficacy of nuclear factor CREB. Nature. 334(6182):494–498. DOI:10.1038/334494a0.
   PubMed Web of Science ®Google Scholar
• Han J, Li E, Chen L, Zhang Y, Wei F, Liu J, Deng H, Wang Y. 2015. The CREB coactivator CRTC2 controls hepatic lipid metabolism by regulating SREBP1. Nature. 524(7564):243–246. DOI:10.1038/nature14557.
   PubMed Web of Science ®Google Scholar
• Hu PC, Li K, Tian YH, Pan WT, Wang Y, Xu XL, He YQ, Gao Y, Wei L, Zhang JW, et al. CREB1/Lin28/miR-638/VASP interactive network drives the development of breast cancer. Int J Biol Sci. 2019;15(12):2733–2749. DOI:10.7150/ijbs.36854.eCollection2019
   PubMed Web of Science ®Google Scholar
• Chen Z, Li JL, Lin S, Cao C, Gimbrone NT, Yang R, Fu DA, Carper MB, Haura EB, Schabath MB, et al. 2016. cAMP/CREB-regulated LINC00473 marks LKB1-inactivated lung cancer and mediates tumor growth. J Clin Invest. 126(6):2267–2279. DOI:10.1172/JCI85250
   PubMed Web of Science ®Google Scholar
• Wang J, Ma L, Weng W, Qiao Y, Zhang Y, He J, Wang H, Xiao W, Li L, Chu Q, et al. 2013. Mutual interaction between YAP and CREB promotes tumorigenesis in liver cancer. Hepatology. 58(3):1011–1020. DOI:10.1002/hep.26420
   PubMed Web of Science ®Google Scholar
• Li CJ, Lin HY, Ko CJ, Lai JC, Chu PY. 2020. A novel biomarker driving poor-prognosis liver cancer: overexpression of the mitochondrial calcium gatekeepers. Biomedicines. 8(11):451. DOI:10.3390/biomedicines8110451.
   PubMed Web of Science ®Google Scholar
• Tan X, Wang S, Yang B, Zhu L, Yin B, Chao T, Zhao J, Yuan J, Qiang B, Peng X, et al. The CREB-miR-9 negative feedback minicircuitry coordinates the migration and proliferation of glioma cells. PLoS One. 2012;7(11):e49570. DOI:10.1371/journal.pone.0049570
   PubMed Web of Science ®Google Scholar
• Zhang Y, Yang J, Cui X, Chen Y, Zhu VF, Hagan JP, Wang H, Yu X, Hodges SE, Fang J, et al. A novel epigenetic CREB-miR-373 axis mediates ZIP4-induced pancreatic cancer growth. EMBO Mol Med. 2013;5(9):1322–1334. DOI:10.1002/emmm.201302507
   PubMed Web of Science ®Google Scholar
• Xiao Y, Li ZH, Bi YH. 2019. MicroRNA-889 promotes cell proliferation in colorectal cancer by targeting DAB2IP. Eur Rev Med Pharmacol Sci. 23(8):3326–3334. DOI:10.26355/eurrev_201904_17695.
   PubMed Web of Science ®Google Scholar
• Ge D, Chen H, Zheng S, Zhang B, Ge Y, Yang L, Cao X. Hsa-miR-889-3p promotes the proliferation of osteosarcoma through inhibiting myeloid cell nuclear differentiation antigen expression. Hsa-miR-889-3p promotes the proliferation of osteosarcoma through inhibiting myeloid cell nuclear differentiation antigen expression. Biomed Pharmacother. 2019;114:108819. doi:10.1016/jbiopha.2019.108819
   PubMed Web of Science ®Google Scholar
• Dong Z, Li BC, Wang XJ. 2019. ΜicroRNA-889 plays a suppressive role in cell proliferation and invasion by directly targeting TAB1 in non-small cell lung cancer. Mol Med Rep. 20(1):261–269. DOI:10.3892/mmr.2019.10245.
   PubMed Web of Science ®Google Scholar
• McConnell BB, Yang VW. 2010. Mammalian Kruppel-like factors in health and diseases. Physiol Rev. 90(4):1337–1381. DOI:10.1152/physrev.00058.2009.
   PubMed Web of Science ®Google Scholar
• Kaczynski J, Cook T, Urrutia R. 2003. Sp1- and Krüppel-like transcription factors. Genome Biol. 4(2):206. DOI:10.1186/gb-2003-4-2-206.
   PubMed Web of Science ®Google Scholar
• Imataka H, Sogawa K, Yasumoto K, Kikuchi Y, Sasano K, Kobayashi A, Hayami M, Fujii-Kuriyama Y. Two regulatory proteins that bind to the basic transcription element (BTE), a GC box sequence in the promoter region of the rat P-4501A1 gene. EMBO J. 1992;11(10):3663–3671. doi:10.1002/j.1460-2075.1992.tb05451.x.
   PubMed Web of Science ®Google Scholar
• Li Y, Sun Q, Jiang M, Li S, Zhang J, Xu Z, Guo D, Gu T, Wang B, Xiao L, et al. KLF9 suppresses gastric cancer cell invasion and metastasis through transcriptional inhibition of MMP28. FASEB J. 2019;33(7):7915–7928. DOI:10.1096/fj.201802531R.Epub2019Mar26
   PubMed Web of Science ®Google Scholar
• Brown AR, Simmen RC, Raj VR, Van TT, MacLeod SL, Simmen FA. 2015. Krüppel -like factor 9 (KLF9) prevents colorectal cancer through inhibition of interferon-related signaling. Carcinogenesis. 36(9):946–955. DOI:10.1093/carcin/bgv104.
   PubMed Web of Science ®Google Scholar
• Bai XY, Li S, Wang M, Li X, Yang Y, Xu Z, Li B, Li Y, Xia K, Chen H, et al. 2018. Krüppel-like factor 9 down-regulates matrix metalloproteinase 9 transcription and suppresses human breast cancer invasion. Cancer Lett. 412:224–235. DOI:10.1016/j.canlet.2017.10.027.
   PubMed Web of Science ®Google Scholar
• Fu DZ, Cheng Y, He H, Liu HY, Liu YF. 2014. The fate of Krüppel-like factor 9-positive hepatic carcinoma cells may be determined by the programmed cell death protein 5. Int J Oncol. 44(1):153–160. DOI:10.3892/ijo.2013.2147.
   PubMed Web of Science ®Google Scholar
• Sun J, Wang B, Liu Y, Zhang L, Ma A, Yang Z, Ji Y, Liu Y. Transcription factor KLF9 suppresses the growth of hepatocellular carcinoma cells in vivo and positively regulates p53 expression. Cancer Lett. 2014;355(1):25–33. DOI:10.1016/j.canlet.2014.09.022
   PubMed Web of Science ®Google Scholar
• Huang C, Li J, Zhang X, Xiong T, Ye J, Yu J, Gui Y. 2020. The miR-140-5p/KLF9/ KCNQ1 axis promotes the progression of renal cell carcinoma. FASEB J. 34(8):10623–10639. DOI:10.1096/fj.202000088RR.
   PubMed Web of Science ®Google Scholar
• He Q, Huang L, Yan D, Bi J, Yang M, Huang J, Lin T. 2019. CircPTPRA acts as a tumor suppressor in bladder cancer by sponging miR-636 and upregulating KLF9. Aging (Albany NY). 11(23):11314–11328. DOI:10.18632/aging.102530.
   PubMedGoogle Scholar
• Zhang Y, Zhang Z, Yi Y, Wang Y, Fu J. 2020. CircNOL10 acts as a sponge of miR-135a/b-5p in suppressing colorectal cancer progression via regulating KLF9. Onco Targets Ther. 13:5165–5176. DOI:10.2147/OTT.S242001.
   PubMed Web of Science ®Google Scholar
• Khemlina G, Ikeda S, Kurzrock R. The biology of hepatocellular carcinoma: implications for genomic and immune therapies. Mol Cancer. 2017;16(1):149. DOI:10.1186/s12943-017-0712-x.
   PubMedGoogle Scholar
• Lv Q, Wang G, Zhang Y, Han X, Li H, Le W, Zhang M, Ma C, Wang P, Ding Q. FABP5 regulates the proliferation of clear cell renal cell carcinoma cells via the PI3K/AKT signaling pathway. Int J Oncol. 2019;54(4):1221–1232. DOI:10.3892/ijo.2019.4721
   PubMed Web of Science ®Google Scholar