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However, the underlying mechanism remains unknown. M6A modifications in cancer cells are dynamic and reversible and have been found to impact tumor initiation and progression through various mechanisms. In this study, we explored the regulatory mechanism of breast cancer cell proliferation and metabolism through m6A methylation in the Hippo pathway. \u003C\u002Fjats:p>\n              \u003C\u002Fjats:sec>\u003Cjats:sec>\n                \u003Cjats:title>Methods\u003C\u002Fjats:title>\n                \u003Cjats:p>A combination of MeRIP-seq, RNA-seq and metabolomics-seq was utilized to reveal a map of m6A modifications in breast cancer tissues and cells. We conducted RNA pull-down assays, RIP-qPCR, MeRIP-qPCR, and RNA stability analysis to identify the relationship between m6A proteins and LATS1 in m6A regulation in breast cancer cells. The expression and biological functions of m6A proteins were confirmed in breast cancer cells in vitro and in vivo. Furthermore, we investigated the phosphorylation levels and localization of YAP\u002FTAZ to reveal that the activity of the Hippo pathway was affected by m6A regulation of LATS1 in breast cancer cells. \u003C\u002Fjats:p>\n              \u003C\u002Fjats:sec>\u003Cjats:sec>\n                \u003Cjats:title>Results\u003C\u002Fjats:title>\n                \u003Cjats:p>We demonstrated that m6A regulation plays an important role in proliferation and glycolytic metabolism in breast cancer through the Hippo pathway factor, LATS1. METTL3 was identified as the m6A writer, with YTHDF2 as the reader protein of LATS1 mRNA, which plays a positive role in promoting both tumorigenesis and glycolysis in breast cancer. High levels of m6A modification were induced by METTL3 in LATS1 mRNA. YTHDF2 identified m6A sites in LATS1 mRNA and reduced its stability. Knockout of the protein expression of METTL3 or YTHDF2 increased the expression of LATS1 mRNA and suppressed breast cancer tumorigenesis by activating YAP\u002FTAZ in the Hippo pathway.\u003C\u002Fjats:p>\n              \u003C\u002Fjats:sec>\u003Cjats:sec>\n                \u003Cjats:title>Conclusions\u003C\u002Fjats:title>\n                \u003Cjats:p>In summary, we discovered that the METTL3-LATS1-YTHDF2 pathway plays an important role in the progression of breast cancer by activating YAP\u002FTAZ in the Hippo pathway.\u003C\u002Fjats:p>\n              \u003C\u002Fjats:sec>",{"EN":172,"VI":173},"The N6-methyladenosine METTL3 regulates tumorigenesis and glycolysis by mediating m6A methylation of the tumor suppressor LATS1 in breast cancer","METTL3 N6-methyladenosine điều hòa quá trình sinh u và đường phân qua trung gian methyl hóa m6A của gen ức chế khối u LATS1 trong ung thư 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H, Ferlay J, Siegel RL, Laversanne M, Soerjomataram I, Jemal A, Bray F. Global Cancer Statistics 2020: GLOBOCAN Estimates of Incidence and Mortality Worldwide for 36 Cancers in 185 Countries. CA Cancer J Clin. 2021;71(3):209–49.",{"doi":519},"10.3322\u002Fcaac.21660",{"id":18,"text":521,"url":18,"identifiers":522},"Shieh Y, Tice JA. Medications for Primary Prevention of Breast Cancer. JAMA. 2020;324(3):291–2.",{"doi":523},"10.1001\u002Fjama.2020.9246",{"id":18,"text":525,"url":18,"identifiers":526},"Denkert C, von Minckwitz G, Darb-Esfahani S, Lederer B, Heppner BI, Weber KE, Budczies J, Huober J, Klauschen F, Furlanetto J, et al. Tumour-infiltrating lymphocytes and prognosis in different subtypes of breast cancer: a pooled analysis of 3771 patients treated with neoadjuvant therapy. Lancet Oncol. 2018;19(1):40–50.",{"doi":527},"10.1016\u002FS1470-2045(17)30904-X",{"id":18,"text":529,"url":18,"identifiers":530},"Harbeck N, Gnant M. Breast cancer. Lancet. 2017;389(10074):1134–50.",{"doi":531},"10.1016\u002FS0140-6736(16)31891-8",{"id":18,"text":533,"url":18,"identifiers":534},"Hanahan D. Hallmarks of Cancer: New Dimensions. Cancer Discov. 2022;12(1):31–46.",{"doi":535},"10.1158\u002F2159-8290.CD-21-1059",{"id":18,"text":537,"url":18,"identifiers":538},"Chen XY, Zhang J, Zhu JS. The role of m(6)A RNA methylation in human cancer. Mol Cancer. 2019;18(1):103.",{"doi":539},"10.1186\u002Fs12943-019-1033-z",{"id":18,"text":541,"url":18,"identifiers":542},"Cai X, Wang X, Cao C, Gao Y, Zhang S, Yang Z, Liu Y, Zhang X, Zhang W, Ye L. HBXIP-elevated methyltransferase METTL3 promotes the progression of breast cancer via inhibiting tumor suppressor let-7g. Cancer Lett. 2018;415:11–9.",{"doi":543},"10.1016\u002Fj.canlet.2017.11.018",{"id":18,"text":545,"url":18,"identifiers":546},"Pan X, Hong X, Li S, Meng P, Xiao F. METTL3 promotes adriamycin resistance in MCF-7 breast cancer cells by accelerating pri-microRNA-221-3p maturation in a m6A-dependent manner. Exp Mol Med. 2021;53(1):91–102.",{"doi":547},"10.1038\u002Fs12276-020-00510-w",{"id":18,"text":549,"url":18,"identifiers":550},"Wang H, Xu B, Shi J. N6-methyladenosine METTL3 promotes the breast cancer progression via targeting Bcl-2. Gene. 2020;722: 144076.",{"doi":551},"10.1016\u002Fj.gene.2019.144076",{"id":18,"text":553,"url":18,"identifiers":554},"Koo JH, Guan KL. Interplay between YAP\u002FTAZ and Metabolism. Cell Metab. 2018;28(2):196–206.",{"doi":555},"10.1016\u002Fj.cmet.2018.07.010",{"id":18,"text":557,"url":18,"identifiers":558},"Yu T, Bachman J, Lai ZC. Mutation analysis of large tumor suppressor genes LATS1 and LATS2 supports a tumor suppressor role in human cancer. Protein Cell. 2015;6(1):6–11.",{"doi":559},"10.1007\u002Fs13238-014-0122-4",{"id":18,"text":561,"url":18,"identifiers":562},"Xu Y, Ji K, Wu M, Hao B, Yao KT, Xu Y. A miRNA-HERC4 pathway promotes breast tumorigenesis by inactivating tumor suppressor LATS1. Protein Cell. 2019;10(8):595–605.",{"doi":563},"10.1007\u002Fs13238-019-0607-2",{"id":18,"text":565,"url":18,"identifiers":566},"Cheng L, Zhang X, Huang YZ, Zhu YL, Xu LY, Li Z, Dai XY, Shi L, Zhou XJ, Wei JF, et al. Metformin exhibits antiproliferation activity in breast cancer via miR-483-3p\u002FMETTL3\u002Fm(6)A\u002Fp21 pathway. Oncogenesis. 2021;10(1):7.",{"doi":567},"10.1038\u002Fs41389-020-00290-y",{"id":18,"text":569,"url":18,"identifiers":570},"Rong D, Dong Q, Qu H, Deng X, Gao F, Li Q, Sun P. m(6)A-induced LINC00958 promotes breast cancer tumorigenesis via the miR-378a-3p\u002FYY1 axis. Cell Death Discov. 2021;7(1):27.",{"doi":571},"10.1038\u002Fs41420-020-00382-z",{"id":18,"text":573,"url":18,"identifiers":574},"Kim J, Yu L, Chen W, Xu Y, Wu M, Todorova D, Tang Q, Feng B, Jiang L, He J, et al. Wild-Type p53 Promotes Cancer Metabolic Switch by Inducing PUMA-Dependent Suppression of Oxidative Phosphorylation. Cancer Cell. 2019;35(2):191-203 e198.",{"doi":575},"10.1016\u002Fj.ccell.2018.12.012",{"id":18,"text":577,"url":18,"identifiers":578},"Kim J, Xu S, Xiong L, Yu L, Fu X, Xu Y. SALL4 promotes glycolysis and chromatin remodeling via modulating HP1alpha-Glut1 pathway. Oncogene. 2017;36(46):6472–9.",{"doi":579},"10.1038\u002Fonc.2017.265",{"id":18,"text":581,"url":18,"identifiers":582},"Zhou Y, Zeng P, Li YH, Zhang Z, Cui Q. SRAMP: prediction of mammalian N6-methyladenosine (m6A) sites based on sequence-derived features. Nucleic Acids Res. 2016;44(10):e91.",{"doi":583},"10.1093\u002Fnar\u002Fgkw104",{"id":18,"text":585,"url":18,"identifiers":586},"Wen B, Mei Z, Zeng C, Liu S. metaX: a flexible and comprehensive software for processing metabolomics data. BMC Bioinformatics. 2017;18(1):183.",{"doi":587},"10.1186\u002Fs12859-017-1579-y",{"id":18,"text":589,"url":18,"identifiers":590},"Surmacki J, Brozek-Pluska B, Kordek R, Abramczyk H. The lipid-reactive oxygen species phenotype of breast cancer. Raman spectroscopy and mapping, PCA and PLSDA for invasive ductal carcinoma and invasive lobular carcinoma. Molecular tumorigenic mechanisms beyond Warburg effect. Analyst. 2015;140(7):2121–33.",{"doi":591},"10.1039\u002FC4AN01876A",{"id":18,"text":593,"url":18,"identifiers":594},"Qi S, Zhu Y, Liu X, Li P, Wang Y, Zeng Y, Yu A, Wang Y, Sha Z, Zhong Z, et al. WWC proteins mediate LATS1\u002F2 activation by Hippo kinases and imply a tumor suppression strategy. Mol Cell. 2022;82(10):1850-1864 e1857.",{"doi":595},"10.1016\u002Fj.molcel.2022.03.027",{"id":18,"text":597,"url":18,"identifiers":598},"Chen X, Zhou X, Wang X. m(6)A binding protein YTHDF2 in cancer. Exp Hematol Oncol. 2022;11(1):21.",{"doi":599},"10.1186\u002Fs40164-022-00269-y",false,{"id":602,"createTime":603,"updateTime":604,"relativeEntities":605,"slug":606,"properties":607,"entityType":178,"verifyStatus":179,"verifyTime":618,"verifyNote":181,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":619,"fullTextUrl":18,"authors":620,"publicationType":462,"publisherRelationship":722,"citationCount":19,"citationInfo":773,"publishDate":776,"publishYear":774,"citationAnalyzeStatus":512,"lastCitationAnalyze":777,"indexDatabases":778,"openAccess":18,"references":18,"isForceReanalyzing":600},"10a9728f-ff04-450f-8135-449c2c567bfb","2023-12-24T00:18:06.054+00:00","2026-08-24T15:20:21.608+00:00",[],"A-study-of-association-between-expression-of-hOGG1-VDAC1-HK-2-and-cervical-carcinoma",{"abstract":608,"title":610,"gsPaper":612,"references":614,"doi":616},{"EN":609},"Human 8-oguanine glycosylase 1(hOGG1), voltage-dependent anion channel 1(VDAC1), hexokinase 2(HK-2), represented the process of oxidative DNA damage, cell apoptosis and glycolysis, respectively. This study aims to explore the association between expression of hOGG1, VDAC1, HK-2 and cervical carcinoma. A case-control study was conducted. 65 cervical biopsy samples consist of 20 control and 45 cases. The expression of hOGG1, VDAC1 and HK-2 were examined with immunohistochemistry(IHC), immunolabeling was evaluated with stereological cell counts. The data showed that the positive proportion of hOGG1 and HK-2 in the case group was higher than that of the control group (P \u003C 0.05). Further, there was an increasing trend for the positive proportion and expression degree of hOGG1 and HK-2 from Control, Mild cervical carcinoma (MCC), Intermediate cervical carcinoma(ICC) to Severe cervical carcinoma(SCC) in order (P \u003C 0.05). To VDAC1, the significant result was not obtained. The results suggested that there was a close association between expression of hOGG1, HK-2 and cervical cancer. hOGG1 and HK-2 might play a key role at the early stage of cervical cancer, and the findings of hOGG1 and HK-2 should be considered as a significant biomarker at the early stage of cervical cancer.",{"EN":611},"A study of association between expression of hOGG1, VDAC1, HK-2 and cervical carcinoma",{"VOID":613},"[\"14108488397434717488\"]",{"VOID":615},"Parkin D Maxwell, Bray Freddie, Ferlay Jacques, Pisani Paola: Estimating the world burden: Globocan 2000[J]. Int J cancer. 2001, 94 (2): 153-156. 10.1002\u002Fijc.1440.\nDing MA, Ling XI: Epidemiology and etiology research progress of Cervical Cancer. Journal of Practical Obstetrics and Gynecology. 2001, 17 (02): 61-62.\nRussell JM, Blair V, Hunter RD: Cervical carcinoma: Prognosis in younger patients[J]. Br Med J. 1987, 295: 300-10.1136\u002Fbmj.295.6593.300.\nWenhua Zhang, Ping Bai, Shaokang Ma: Carcinoma of the cervix in younger women (≤ 35 year). Chinese Journal of Clinical Oncology and Rehabilitation. 1999, 6 (6): 39-41.\nElliott PM, Tattersall MH, Coppleson M, Russell P, Wong F, Coates AS, Solomon HJ, Bannatyne PM, Atkinson KH, Murray JC: Changing character of cervical cancer in young women[J]. Br Med J. 1989, 298 (2): 288-290. 10.1136\u002Fbmj.298.6669.288.\nThomas DB, Ray RM, Qin Q: Risk factors for progression of squamous cell cervical carcinoma in-situ to invasive cervical cancer:results of a multinational study[J]. Cancer Causes Control. 2002, 13 (7): 683-690. 10.1023\u002FA:1019527113057.\nUrsin G, Pike MC, Preston-Martin S, d'Ablaing G, Peters RK: Sexual, reproductive and other risk factors for adenocarcinoma of the cervix, results from a population based control study(California, united states) [J]. Cancer Causes Control. 1996, 7 (3): 391-401. 10.1007\u002FBF00052946.\nCAO Ze-yi: The First Cervical Diseases Academic Conference of Chinese Medical Association. 2002, 36-39.\nReddy VG, Khanna N, Jain SK, Das BC, Singh N: Telomerase-A molecular marker for cervical cancer screening. Int J Gynecol Cancer. 2001, 11 (2): 100-106. 10.1046\u002Fj.1525-1438.2001.011001100.x.\nRiethdorf S, Riethdorf L, Schulz G, Ikenberg H, Janicke F, Loning T, Park TW: Relationship between telomerase activation and HPV16\u002F18 oncogene expression in squamous intraepithelial lesions and squamous cell carcinomas of the uterine cervix. Int J Gynecol Pathol. 2001, 20 (2): 177-185. 10.1097\u002F00004347-200104000-00011.\nKlaes R, Benner A, Friedrich T, Ridder R, Herrington S, Jenkins D, Kurman RJ, Schmidt D, Stoler M, Doeberitz MV: p16(1NK4a) immunohistochemistry improves interobserver agreement in the diagnosis of cervical intraepithelial neoplasia. Am J Surg Patho. 2002, 26 (11): 1389-1399. 10.1097\u002F00000478-200211000-00001.\nMurphy N, Ring M, Heffron CCBB, King B, Killalea AG, Hughes C, Martin CM, McGuinness E, Sheils O, O'Leary JJ: p161NK4a, CDC6, and MCM5:predictive biomarkers in cervical preinvasive neoplasia and cervical cancer. Clin Pathol. 2005, 58 (5): 525-534. 10.1136\u002Fjcp.2004.018895.\nCooke MS, Evans MD, Dizdaroglu M, Lunec J: Oxidative DNA damage: mechanisms, mutation and disease[J]. FASEB l. 2003, 17 (10): 1195-1214. 10.1096\u002Ffj.02-0752rev.\nReed JC: Dysregulation of apoptosis in cancer. J Clin Oncol. 1999, 17: 2941-2953.\nGatenby RA, Gillies RJ: Why do cancers have high aerobic glycolysis?. Nature Reviews Cancer. 2004, 4 (11): 891-899. 10.1038\u002Fnrc1478.\nRosenquist TA, Zharkov DO, Grollman AP: Cloning and characterization of a mammalian 8-oxoguanine DNA glycosylase[J]. Proc Natl Acad Sci USA. 1997, 94 (14): 7429-7434. 10.1073\u002Fpnas.94.14.7429.\nRyerse J, Blachly-Dyson E, Forte M, Nagel B: Cloning and molecular characterization of a voltage-dependent anion-selective channel(VDAC) from Drosophila melanogaster. Biochim Biophys Acta. 1997, 1327 (2): 204-212. 10.1016\u002FS0005-2736(97)00059-X.\nShinohara Y: Identification and characterization of hexokinase isozyme predominantly expressed in malignant tumor cells. Yakugaku Zasshi. 2000, 120 (8): 657-666.\nDantzer F, Bjoras M, Luna L, Klungland A, Seeberg E: Comparative analysis of 8-oxoG: C, 8-oxoG: A, A:C and C:C DNA repair in extracts from wild type or 8-oxoG DNA glycosylase deficient mammalian and bacterial cells. DNA Repair. 2003, 2 (6): 707-718.\nKoukourakis MI, Pitiakoudis M, Giatromanolaki A, Tsarouha A, Polychronidis A, Sivridis E, Simopoulos C: Oxygen and glucose consumption in gastrointestinal adenocarcinomas: Correlation with markers of hypoxia, acidity and anaerobic glycolysis. Cancer Science. 2006, 97 (10): 1056-1060. 10.1111\u002Fj.1349-7006.2006.00298.x.\nGolshani-Hebroni SG, Bessman SP: Hexokinase binding to mitochondria:a basis for proliferative energy metabolism[J]. J Bioenerg Biomembr. 1997, 29 (4): 331-338. 10.1023\u002FA:1022442629543.\nSun L, Shukair S, Naik TJ, Moazed F, Ardehali H: Glucose phosphorylation and mitochondrial binding are required for the protective effects of hexokinases I and II. Mol Cell Biol. 2008, 28 (3): 1007-1017. 10.1128\u002FMCB.00224-07.\nPastorino JG, Shulga N, Hoek JB: Mitochondrial binding of hexokinse II inhibits Bax induced cytochrome c release and apoptosis. Journal of Biological Chemistry. 2002, 277: 7610-7618. 10.1074\u002Fjbc.M109950200.",{"VOID":617},"10.1186\u002F1756-9966-29-129","2024-06-24T04:27:28.451+00:00","https:\u002F\u002Fjeccr.biomedcentral.com\u002Farticles\u002F10.1186\u002F1756-9966-29-129",[621,646,668,681,696,709],{"id":622,"sortIndex":19,"researcher":18,"roles":623,"affiliations":625,"properties":643,"displayName":645,"givenName":18,"familyName":18},"e9f0d9ec-4566-4772-8880-c4448a0e892f",[624],"AUTHOR",[626,634],{"id":627,"sortIndex":19,"affiliation":628,"properties":18},"f4d28a55-e94c-4e67-b300-e5ffd3efc93a",{"id":627,"createTime":18,"updateTime":18,"relativeEntities":629,"slug":18,"properties":630,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":633,"statistic":18},[],{"title":631},{"VI":632},"Department of O & G, Xiangya Hospital Central-South University, Changsha Hunan, 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cancer (CRC) is one of the most common malignant tumors globally. Angiogenesis is a key event maintaining tumor cell survival and aggressiveness. The expression of vascular endothelial growth factor A (VEGFA), one of the most significant tumor cell-secreted proangiogenic factors, is frequently upregulated in CRC. The MTT assay was used to detect the viability of CRC cells. Transwell assays were performed to detect the invasion capacity of target cells. Relative protein levels were determined by immunoblotting. Pathological characteristics of tissues were detected by H&E staining and immunohistochemical (IHC) staining. A RIP assay was conducted to validate the predicted binding between genes. We observed that circ-001971 expression was dramatically increased in CRC tissue samples and cells. Circ-001971 knockdown suppressed the capacity of CRC cells to proliferate and invade and HUVEC tube formation in vitro, as well as tumor growth in mice bearing SW620 cell-derived tumors in vivo. The expression of circ-001971 and VEGFA was dramatically increased whereas the expression of miR-29c-3p was reduced in tumor tissue samples. Circ-001971 relieved miR-29c-3p-induced inhibition of VEGFA by acting as a ceRNA, thereby aggravating the proliferation, invasion and angiogenesis of CRC. Consistent with the above findings, the expression of VEGFA was increased, whereas the expression of miR-29c-3p was decreased in tumor tissue samples. miR-29c-3p had a negative correlation with both circ-001971 and VEGFA, while circ-001971 was positively correlated with VEGFA. In conclusion, the circ-001971\u002FmiR-29c-3p axis modulated CRC cell proliferation, invasion, and angiogenesis by targeting VEGFA.",{"EN":789},"RETRACTED ARTICLE: The circular RNA 001971\u002FmiR-29c-3p axis modulates colorectal cancer growth, metastasis, and angiogenesis through VEGFA",{"VOID":791},"[\"4954273690088653081\"]",{"VOID":793},"Torre LA, Bray F, Siegel RL, Ferlay J, Lortet-Tieulent J, Jemal A. 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Oncotarget. 2017;8:104508–24.",{"VOID":795},"10.1186\u002Fs13046-020-01594-y","2024-05-16T07:39:54.004+00:00","https:\u002F\u002Fjeccr.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs13046-020-01594-y",[799,814,829,842,855,868,881],{"id":800,"sortIndex":19,"researcher":18,"roles":801,"affiliations":802,"properties":811,"displayName":813,"givenName":18,"familyName":18},"7ea742a9-4230-46a7-b950-6fd8d6acb069",[624],[803],{"id":804,"sortIndex":19,"affiliation":805,"properties":18},"114e164e-2ed5-44f3-8163-5566fa4cc3ab",{"id":804,"createTime":18,"updateTime":18,"relativeEntities":806,"slug":18,"properties":807,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":810,"statistic":18},[],{"title":808},{"VI":809},"Department of Pediatrics, XiangYa Hospital, Central South University, Changsha, People’s Republic of China",[],{"title":812},{"VI":813},"Chen 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has been shown to be a candidate tumor suppressor in several tumors, but its role in glioma remains poorly understood. In this study, we examined the mRNA expression of ECRG4 and investigated its biological role in glioma cells. Real-time PCR was used to examine expression of ECRG4 in gliomas and their matched brain tissues. The effect of ECRG4 expression on cell proliferation, invasion, and migration was investigated in human U251 glioma cells. Finally, the regulation of transcription factor NF-kB by ECRG4 was evaluated by western blotting. Of the 10 paired samples analyzed, 9 glioma tissues displayed the decreased expression of ECRG4 compared to matched normal brain tissues. Cells transfected with ECRG4 showed significantly decreased cell proliferation as evaluated by MTT and colony formation assays. Furthermore, overexpression inhibited cell migration and invasion in transwell and Boyden chamber experiments and retarded the cell cycle progression from G1 to S phase by FACSCaliber cytometry. Protein levels of nuclear transcription factor NF-kB, which is involved in cell proliferation, inversely correlated with ECRG4 expression. Our data suggest that ECRG4 serves as a tumor suppressor in glioma.",{"EN":964},"Overexpression of candidate tumor suppressor ECRG4 inhibits glioma proliferation and invasion",{"VOID":966},"[\"4619552036065125036\"]",{"VOID":968},"Su T, Liu H, Lu S: Cloning and identification of cDNA fragments related to human esophageal cancer. Zhonghua Zhong Liu Za Zhi. 1998, 20 (4): 254-257.\nBi MX, Han WD, Lu SX: Using lab on-line to clone and identify the esophageal cancer related gene 4. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 2001, 33 (3): 257-261.\nYue CM, Deng DJ, Bi MX, Guo LP, Lu SH: Expression of ECRG4, a novel esophageal cancer-related gene, downregulated by CpG island hypermethylation in human esophageal squamous cell carcinoma. World J Gastroenterol. 2003, 9 (6): 1174-1178.\nLi LW, Yu XY, Yang Y, Zhang CP, Guo LP, Lu SH: Expression of esophageal cancer related gene 4 (ECRG4), a novel tumor suppressor gene, in esophageal cancer and its inhibitory effect on the tumor growth in vitro and in vivo. Int J Cancer. 2009, 125 (7): 1505-1513. 10.1002\u002Fijc.24513.\nMori Y, Ishiguro H, Kuwabara Y, Kimura M, Mitsui A, Kurehara H, Mori R, Tomoda K, Ogawa R, Katada T, Harata K, Fujii Y: Expression of ECRG4 is an independent prognostic factor for poor survival in patients with esophageal squamous cell carcinoma. Oncol Rep. 2007, 18 (4): 981-985.\nDemokan S, Chang X, Chuang A, Mydlarz WK, Kaur J, Huang P, Khan Z, Khan T, Ostrow KL, Brait M, Hoque MO, Liegeois NJ, Sidransky D, Koch W, Califano JA: KIF1A and EDNRB are differentially methylated in primary HNSCC and salivary rinses. Int J Cancer. 2010,\nLee J, Jeong DJ, Kim J, Lee S, Park JH, Chang B, Jung SI, Yi L, Han Y, Yang Y, Kim KI, Lim JS, Yang I, Jeon S, Bae DH, Kim CJ, Lee MS: The anti-aging gene KLOTHO is a novel target for epigenetic silencing in human cervical carcinoma. Mol Cancer. 2010, 9: 109-10.1186\u002F1476-4598-9-109.\nYang Z, Wang Y, Fang J, Chen F, Liu J, Wu J, Wang Y: Expression and aberrant promoter methylation of Wnt inhibitory factor-1 in human astrocytomas. J Exp Clin Cancer Res. 2010, 29: 26-10.1186\u002F1756-9966-29-26.\nTorng PL, Lin CW, Chan MW, Yang HW, Huang SC, Lin CT: Promoter methylation of IGFBP-3 and p53 expression in ovarian endometrioid carcinoma. Mol Cancer. 2009, 8: 120. 10.1186\u002F1476-4598-8-120.\nWu CS, Lu YJ, Li HP, Hsueh C, Lu CY, Leu YW, Liu HP, Lin KH, Hui-Ming Huang T, Chang YS: Glutamate receptor, ionotropic, kainate 2 silencing by DNA hypermethylation possesses tumor suppressor function in gastric cancer. Int J Cancer. 2010, 126 (11): 2542-2552.\nVanaja DK, Ehrich M, Van den BD: Hypermethylation of Genes for Diagnosis and Risk Stratification of Prostate Cancer. Cancer Invest. 2009, 27 (5): 549-560. 10.1080\u002F07357900802620794.\nGötze S, Feldhaus V, Traska T, Wolter M, Reifenberger G, Tannapfel A, Kuhnen C, Martin D, Müller O, Sievers S: ECRG4 is a candidate tumor suppressor gene frequently hypermethylated in colorectal carcinoma and glioma. BMC Cancer. 2009, 9: 447-10.1186\u002F1471-2407-9-447.\nTu L, Liu Z, He X, He Y, Yang H, Jiang Q, Xie S, Xiao G, Li X, Yao K, Fang W: Over-expression of eukaryotic translation initiation factor 4 gamma 1 correlates with tumor progression and poor prognosis in nasopharyngeal carcinoma. Mol Cancer. 2010, 9: 78-10.1186\u002F1476-4598-9-78.\nSteck E, Breit S, Breusch SJ, Axt M, Richter W: Enhanced expression of the human chitinase 3-like 2 gene (YKL-39) but not chitinase 3-like 1 gene (YKL-40) in osteoarthritic cartilage. Biochem Biophys Res Commun. 2002, 299 (1): 109-115. 10.1016\u002FS0006-291X(02)02585-8.\nGilmore TD, Koedood M, Piffat KA, White DW: Rel\u002FNF-kappaB\u002FIkappaB proteins and cancer. Oncogene. 1996, 13 (7): 1367-1378.\nLee CH, Jeon YT, Kim SH, Song YS: NF-κB as a potential molecular target for cancer therapy. Biofactors. 2007, 29 (1): 19-35. 10.1002\u002Fbiof.5520290103. Review\nLerebours F, Vacher S, Andrieu C, Espie M, Marty M, Lidereau R, Bieche I: NF-kappa B genes have a major role in Inflammatory Breast Cancer. 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Epigenetics that ensure the somatic inheritance of differentiated state is defined as a crucial factor influencing malignant phenotype without altering genotype. Histone modification is one such alteration playing an essential role in tumor formation, progression, and resistance to treatment. Notably, changes in histone acetylation have been strongly linked to gene expression, cell cycle, and carcinogenesis. The balance of two types of enzyme, histone acetyltransferases (HATs) and histone deacetylases (HDACs), determines the stage of histone acetylation and then the architecture of chromatin. Changes in chromatin structure result in transcriptional dysregulation of genes that are involved in cell-cycle progression, differentiation, apoptosis, and so on. Recently, HDAC inhibitors (HDACis) are identified as novel agents to keep this balance, leading to numerous researches on it for more effective strategies against cancers, including glioblastoma (GBM). 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Clinical development of histone deacetylase inhibitors as anticancer agents.; 2005. pp 495-528.",{"doi":2228},"10.1146\u002Fannurev.pharmtox.45.120403.095825",{"id":18,"text":2230,"url":18,"identifiers":2231},"Thurn KT, Thomas S, Moore A, Munster PN. Rational therapeutic combinations with histone deacetylase inhibitors for the treatment of cancer.; 2011. pp 263-283.",{"doi":2232},"10.2217\u002Ffon.11.2",{"id":18,"text":2234,"url":18,"identifiers":2235},"Lee DH, Ryu H, Won H, Kwon SH. Advances in epigenetic glioblastoma therapy.; 2017. pp 18577-18589.",{"doi":2236},"10.18632\u002Foncotarget.14612",{"id":18,"text":2238,"url":18,"identifiers":2239},"Adamopoulou E, Naumann U. HDAC inhibitors and their potential applications to glioblastoma therapy.; 2013. p e25219.",{"doi":2240},"10.4161\u002Fonci.25219",{"id":2242,"createTime":2243,"updateTime":2244,"relativeEntities":2245,"slug":2246,"properties":2247,"entityType":178,"verifyStatus":179,"verifyTime":2258,"verifyNote":181,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":2259,"fullTextUrl":18,"authors":2260,"publicationType":462,"publisherRelationship":2459,"citationCount":19,"citationInfo":2510,"publishDate":2513,"publishYear":2511,"citationAnalyzeStatus":17,"lastCitationAnalyze":2244,"indexDatabases":2514,"openAccess":18,"references":18,"isForceReanalyzing":600},"ee21a682-05ad-4876-8140-f88422344514","2024-01-04T05:02:09.311+00:00","2026-07-27T17:47:07.787+00:00",[],"Promoter-methylation-of-tumor-suppressor-genes-in-pre-neoplastic-lesions-potential-marker-of-disease-recurrence",{"abstract":2248,"title":2250,"gsPaper":2252,"references":2254,"doi":2256},{"EN":2249},"Epigenetic alterations of specific genes have been reported to be related to colorectal cancer (CRC) transformation and would also appear to be involved in the early stages of colorectal carcinogenesis. Little data are available on the role of these alterations in determining a different risk of colorectal lesion recurrence. The aim of the present study was to verify whether epigenetic alterations present in pre-neoplastic colorectal lesions detected by colonoscopy can predict disease recurrence. A retrospective series of 78 adenomas were collected and classified as low (35) or high-risk (43) for recurrence according to National Comprehensive Cancer Network guidelines. Methylation alterations were analyzed by the methylation-specific multiplex ligation probe assay (MS-MLPA) which is capable of quantifying methylation levels simultaneously in 24 different gene promoters. MS-MLPA results were confirmed by pyrosequencing and immunohistochemistry. Higher levels of methylation were associated with disease recurrence. In particular, MLH1, ATM and FHIT gene promoters were found to be significantly hypermethylated in recurring adenomas. Unconditional logistic regression analysis used to evaluate the relative risk (RR) of recurrence showed that FHIT and MLH1 were independent variables with an RR of 35.30 (95% CI 4.15-300.06, P = 0.001) and 17.68 (95% CI 1.91-163.54, P = 0.011), respectively. Histopathological classification does not permit an accurate evaluation of the risk of recurrence of colorectal lesions. Conversely, results from our methylation analysis suggest that a classification based on molecular parameters could help to define the mechanisms involved in carcinogenesis and prove an effective method for identifying patients at high risk of recurrence.",{"EN":2251},"Promoter methylation of tumor suppressor genes in pre-neoplastic lesions; potential marker of disease recurrence",{"VOID":2253},"[\"6445607810913646243\"]",{"VOID":2255},"Jass JR: Classification of colorectal cancer based on correlation of clinical, morphological and molecular features. 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J Clin Oncol. 2009, 27: 3161-3168. 10.1200\u002FJCO.2008.18.2485.\nDi Domenico M, Santoro A, Ricciardi C, Iaccarino M, Iaccarino S, Freda M, Feola A, Sanguedolce F, Losito S, Pasquali D, Di Spiezio Sardo A, Bifulco G, Nappi C, Bufo P, Guida M, De Rosa G, Abbruzzese A, Caraglia M, Pannone G: Epigenetic fingerprint in endometrial carcinogenesis: the hypothesis of a uterine field cancerization. Cancer Biol Ther. 2011, 12: 447-457. 10.4161\u002Fcbt.12.5.15963.\nIssa JP: CpG island methylator phenotype in cancer. Nat Rev Cancer. 2004, 4: 988-993. 10.1038\u002Fnrc1507.\nRashid A, Issa JPJ: CpG island methylation in gastroenterologic neoplasia: a maturing field. Gastroenterology. 2004, 127: 1578-1588. 10.1053\u002Fj.gastro.2004.09.007.\nWeisenberger DJ, Siegmund KD, Campan M, Young J, Long TI, Faasse MA, Kang GH, Widschwendter M, Weener D, Buchanan D, Koh H, Simms L, Barker M, Leggett B, Levine J, Kim M, French AJ, Thibodeau SN, Jass J, Haile R, Laird PW: CpG island methylator phenotype underlies sporadic microsatellite instability and is tightly associated with BRAF mutation in colorectal cancer. Nat Genet. 2006, 38: 787-793. 10.1038\u002Fng1834.\nHinoue T, Weisenberger DJ, Pan F, Campan M, Kim M, Young J, Kim M, Young J, Whitehall VL, Leggett BA, Laird PW: Analysis of the association between CIMP and BRAF in colorectal cancer by DNA methylation profiling. PLoS One. 2009, 4: e 8357-10.1371\u002Fjournal.pone.0008357.\nJi W, Hernandez R, Zhang XY, Qu GZ, Frady A, Varela M, Ehrlich M: DNA demethylation and pericentromeric rearrangements of chromosome 1. Mutat Res. 1997, 379: 33-41. 10.1016\u002FS0027-5107(97)00088-2.\nGoel A, Nagasaka T, Arnold CN, Inoue T, Hamilton C, Niedzwiecki D, Compton C, Mayer RJ, Goldberg R, Bertagnolli MM, Boland CR: The CpG Island methylator phenotype and chromosomal instability are inversely correlated in sporadic colorectal cancer. Gastroenterology. 2007, 132: 127-138. 10.1053\u002Fj.gastro.2006.09.018.\nLeong KJ, Wei W, Tannahill LA, Caldwell GM, Jones CE, Morton DG, Matthews GM, Bach SP: Methylation profiling of rectal cancer identifies novel markers of early-stage disease. Br J Surg. 2011, 98: 724-734. 10.1002\u002Fbjs.7422.\nMoon JW, Lee SK, Lee JO, Kim N, Lee YW, Kim SJ, Kang HJ, Kim J, Kim HS, Park SH: Identification of novel hypermethylated genes and demethylating effect of vincristine in colorectal cancer. J Exp Clin Cancer Res. 2014, 33: 4-\nBardhan K, Liu K: Epigenetics and colorectal cancer pathogenesis. Cancers (Basel). 2013, 5: 676-713. 10.3390\u002Fcancers5020676.\nKane MF, Loda M, Gaida GM, Lipman J, Mishra R, Goldman H, Jessup JM, Kolodner R: Methylation of the hMLH1 promoter correlates with lack of expression of hMLH1 in sporadic colon tumors and mismatch repair-defective human tumor cell lines. Cancer Res. 1997, 57: 808-811.\nFu D, Calvo JA, Samson LD: Balancing repair and tolerance of DNA damage caused by alkylating agents. Nat Rev Cancer. 2012, 12: 104-120.\nLavin MF: Ataxia-telangiectasia: from a rare disorder to a paradigm for cell signalling and cancer. Nat Rev Mol Cell Biol. 2008, 9: 759-769. 10.1038\u002Fnrm2514.\nShiloh Y: ATM and related protein kinases: safeguarding genome integrity. Nat Rev Cancer. 2003, 3: 155-168. 10.1038\u002Fnrc1011.\nHuebner K, Saldivar JC, Sun J, Shibata H, Druck T: Hits, Fhits and Nits: beyond enzymatic function. Adv Enzyme Regul. 2011, 51: 208-217. 10.1016\u002Fj.advenzreg.2010.09.003.\nWali A: FHIT: doubts are clear now. Scientific World Journal. 2010, 10: 1142-1151. 10.1100\u002Ftsw.2010.110.\nAl-Temaimi RA, Jacob S, Al-Ali W, Thomas DA, Al-Mulla F: Reduced FHIT expression is associated with mismatch repair deficient and high CpG island methylator phenotype colorectal cancer. J Histochem Cytochem. 2013, 61: 627-638. 10.1369\u002F0022155413497367.\nPortela A, Esteller M: Epigenetic modifications and human disease. Nat Biotechnol. 2010, 28: 1057-1068. 10.1038\u002Fnbt.1685.\nHerreros-Villanueva M, Muñiz P, García-Girón C, Cavia-Saiz M, Del Corral MJ: TAp73 is one of the genes responsible for the lack of response to chemotherapy depending on B-Raf mutational status. J Transl Med. 2010, 8: 15-10.1186\u002F1479-5876-8-15.\nAllocati N, Di Ilio C, De Laurenzi V: p63\u002Fp73 in the control of cell cycle and cell death. Exp Cell Res. 2012, 318: 1285-1290. 10.1016\u002Fj.yexcr.2012.01.023.\nMurphy CG, Moynahan ME: BRCA gene structure and function in tumor suppression: a repair-centric perspective. 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acknowledging the game-changing results achieved in the treatment of metastatic melanoma with the use of immune checkpoint inhibitors (ICI), a large proportion of patients (40–60%) still fail to respond or relapse due to the development of resistance. Alterations in the expression of Human Leukocyte Antigen class I (HLA-I) molecules are considered to play a major role in clinical resistance to ICI. Cellular immunotherapy with HLA-independent CAR-redirected lymphocytes is a promising alternative in this challenging setting and dedicated translational models are needed. In this study, we propose an HLA-independent therapeutic strategy with Cytokine Induced Killer lymphocytes (CIK) genetically engineered with a Chimeric Antigen Receptor (CAR) targeting the tumor antigen CSPG4 as effector mechanism. We investigated the preclinical antitumor activity of CSPG4-CAR.CIK in vitro and in a xenograft murine model focusing on patient-derived melanoma cell lines (Mel) with defective expression of HLA-I molecules. We successfully generated CSPG4-CAR.CIK from patients with metastatic melanoma and reported their intense activity in vitro against a panel of CSPG4-expressing patient-derived Mel. The melanoma killing activity was intense, even at very low effector to target ratios, and not influenced by the expression level (high, low, defective) of HLA-I molecules on target cells. Furthermore, CAR.CIK conditioned medium was capable of upregulating the expression of HLA-I molecules on melanoma cells. A comparable immunomodulatory effect was replicated by treatment of Mel cells with exogenous IFN-γ and IFN-α. The antimelanoma activity of CSPG4-CAR.CIK was successfully confirmed in vivo, obtaining a significant tumor growth inhibition of an HLA-defective Mel xenograft in immunodeficient mice. In this study we reported the intense preclinical activity of CSPG4-CAR.CIK against melanoma, including those with low or defective HLA-I expression. Our findings support CSPG4 as a valuable CAR target in melanoma and provide translational rationale for clinical studies exploring CAR-CIK cellular immunotherapies within the challenging setting of patients not responsive or relapsing to immune checkpoint inhibitors.",{"EN":2525},"CSPG4 CAR-redirected Cytokine Induced Killer lymphocytes (CIK) as effective cellular immunotherapy for HLA class I defective melanoma",{"VOID":2527},"[\"10736409160449931721\"]",{"VOID":2529},"Lamba N, Ott PA, Iorgulescu JB. Use of first-line immune checkpoint inhibitors and association with overall survival among patients with metastatic melanoma in the anti-PD-1 era. JAMA Netw Open. 2022;5(8): e2225459.\nWolchok JD, Chiarion-Sileni V, Gonzalez R, Grob JJ, Rutkowski P, Lao CD, et al. Long-term outcomes with Nivolumab plus Ipilimumab or Nivolumab alone versus Ipilimumab in patients with advanced melanoma. J Clin Oncol. 2022;40(2):127-137.\nRobert C, Grob JJ, Stroyakovskiy D, Karaszewska B, Hauschild A, Levchenko E, et al. Five-year outcomes with Dabrafenib plus Trametinib in metastatic melanoma. N Engl J Med. 2019;381(7):626–36.\nLarkin J, Chiarion-Sileni V, Gonzalez R, Grob JJ, Rutkowski P, Lao CD, et al. Five-year survival with combined Nivolumab and Ipilimumab in advanced melanoma. N Engl J Med. 2019;381(16):1535–46.\nLim SY, Shklovskaya E, Lee JH, Pedersen B, Stewart A, Ming Z, et al. The molecular and functional landscape of resistance to immune checkpoint blockade in melanoma. Nat Commun. 2023;14(1):1516.\nLiu D, Jenkins RW, Sullivan RJ. Mechanisms of resistance to immune checkpoint blockade. Am J Clin Dermatol. 2019;20(1):41–54.\nSade-Feldman M, Jiao YJ, Chen JH, Rooney MS, Barzily-Rokni M, Eliane JP, et al. Resistance to checkpoint blockade therapy through inactivation of antigen presentation. Nat Commun. 2017;8(1):1136.\nZaretsky JM, Garcia-Diaz A, Shin DS, Escuin-Ordinas H, Hugo W, Hu-Lieskovan S, et al. Mutations associated with acquired resistance to PD-1 blockade in melanoma. N Engl J Med. 2016;375(9):819–29.\nHaslauer T, Greil R, Zaborsky N, Geisberger R. CAR T-cell therapy in hematological malignancies. Int J Mol Sci. 2021;22(16):8996.\nPatel U, Abernathy J, Savani BN, Oluwole O, Sengsayadeth S, Dholaria B. CAR T cell therapy in solid tumors: a review of current clinical trials. EJHaem. 2022;3(S1):24–31.\nAdusumilli PS, Zauderer MG, Rivière I, Solomon SB, Rusch VW, O’Cearbhaill RE, et al. A phase I trial of regional mesothelin-targeted car t-cell therapy in patients with malignant pleural disease, in combination with the anti–pd-1 agent pembrolizumab. Cancer Discov. 2021;11(11):2748–63.\nVentin M, Cattaneo G, Maggs L, Jia J, Arya S, Ferrone S, et al. B7-H3-targeted CAR T cell activity is enhanced by radiotherapy in solid cancers. Front Oncol. 2023;13:1193963.\nWang Y, Drum DL, Sun R, Zhang Y, Chen F, Sun F, et al. Stressed target cancer cells drive nongenetic reprogramming of CAR T cells and solid tumor microenvironment. Nat Commun. 2023;14(1):5727.\nGuo X, Zheng H, Luo W, Zhang Q, Liu J, Yao K. 5T4-specific chimeric antigen receptor modification promotes the immune efficacy of cytokine-induced killer cells against nasopharyngeal carcinoma stem cell-like cells. Sci Rep. 2017;7(1):4859.\nMerker M, Wagner J, Kreyenberg H, Heim C, Moser LM, Wels WS, et al. ERBB2-CAR-engineered cytokine-induced killer cells exhibit both CAR-mediated and innate immunity against high-risk Rhabdomyosarcoma. Front Immunol. 2020;11: 581468.\nHu Z. Tissue factor as a new target for CAR-NK cell immunotherapy of triple-negative breast cancer. Sci Rep. 2020;10(1):2815.\nZhang Q, Zhang H, Ding J, Liu H, Li H, Li H, et al. Combination therapy with EpCAM-CAR-NK-92 cells and regorafenib against human colorectal cancer models. J Immunol Res. 2018;2018:4263520.\nPan K, Farrukh H, Chittepu VCSR, Xu H, Pan CX, Zhu Z. CAR race to cancer immunotherapy: from CAR T, CAR NK to CAR macrophage therapy. J Exp Clin Cancer Res. 2022;41(1):119.\nGammaitoni L, Giraudo L, Macagno M, Leuci V, Mesiano G, Rotolo R, et al. Cytokine-induced killer cells kill chemo-surviving melanoma cancer stem cells. Clin Cancer Res. 2017;23(9):2277–88.\nSangiolo D, Mesiano G, Gammaitoni L, Leuci V, Todorovic M, Giraudo L, et al. Cytokine-induced killer cells eradicate bone and soft-tissue sarcomas. Cancer Res. 2014;74(1):119–29.\nCapellero S, Erriquez J, Melano C, Mesiano G, Genta S, Pisacane A, et al. Preclinical immunotherapy with cytokine-induced killer lymphocytes against epithelial ovarian cancer. Sci Rep. 2020;10(1):6478.\nIaia I, Gammaitoni L, Cattaneo G, Giraudo L, Donini C, Fiorino E, et al. Recruitment, infiltration and cytotoxicity of hla-independent killer lymphocytes in three-dimensional melanoma models. Cancers (Basel). 2021;13(10):2302.\nZhao Q, Zhang H, Li Y, Liu J, Hu X, Fan L. Anti-tumor effects of CIK combined with oxaliplatin in human oxaliplatin-resistant gastric cancer cells in vivo and in vitro. J Exp Clin Cancer Res. 2010;29(1):118.\nDiefenbach A, Jamieson AM, Liu SD, Shastri N, Raulet DH. Ligands for the murine NKG2D receptor: expression by tumor cells and activation of NK cells and macrophages. Nat Immunol. 2000;1(2):119–26.\nSangiolo D, Martinuzzi E, Todorovic M, Vitaggio K, Vallario A, Jordaney N, et al. Alloreactivity and anti-tumor activity segregate within two distinct subsets of cytokine-induced killer (CIK) cells: Implications for their infusion across major HLA barriers. Int Immunol. 2008;20(7):841–8.\nZhang Y, Schmidt-Wolf IGH. Ten-year update of the international registry on cytokine-induced killer cells in cancer immunotherapy. J Cell Physiol. 2020;235(12):9291–303.\nLi H, Huang L, Liu L, Wang X, Zhang Z, Yue D, et al. Selective effect of cytokine-induced killer cells on survival of patients with early-stage melanoma. Cancer Immunol, Immunother. 2017;66(3):299–308.\nMagnani CF, Gaipa G, Lussana F, Belotti D, Gritti G, Napolitano S, et al. Sleeping beauty–engineered CAR T cells achieve antileukemic activity without severe toxicities. J Clin Invest. 2020;130(11):6021–33.\nCircosta P, Donini C, Gallo S, Giraudo L, Gammaitoni L, Rotolo R, et al. Full chimaeric CAR. CIK from patients engrafted after allogeneic haematopoietic cell transplant: Feasibility, anti-leukaemic potential and alloreactivity across major human leukocyte antigen barriers. Br J Haematol. 2023;200(1):64–9.\nBiondi M, Tettamanti S, Galimberti S, Cerina B, Tomasoni C, Piazza R, et al. Selective homing of CAR-CIK cells to the bone marrow niche enhances control of the acute myeloid leukemia burden. Blood. 2023;141(21):2587–98.\nLeuci V, Donini C, Grignani G, Rotolo R, Mesiano G, Fiorino E, et al. CSPG4-specific CAR. CIK lymphocytes as a novel therapy for the treatment of multiple soft-tissue sarcoma histotypes. Clin Cancer Res. 2020;26(23):6321–34.\nLeuci V, Casucci GM, Grignani G, Rotolo R, Rossotti U, Vigna E, et al. CD44v6 as innovative sarcoma target for CAR-redirected CIK cells. Oncoimmunology. 2018;7(5): e1423167.\nWang X, Wang Y, Yu L, Sakakura K, Visus C, Schwab JH, et al. CSPG4 in cancer: multiple roles. Curr Mol Med. 2010;10(4):419–29.\nWang Y, Geldres C, Ferrone S, Dotti G. Chondroitin sulfate proteoglycan 4 as a target for chimeric antigen receptor-based T-cell immunotherapy of solid tumors. Expert Opin Ther Targets. 2015;19(10):1339–50.\nIlieva KM, Cheung A, Mele S, Chiaruttini G, Crescioli S, Griffin M, et al. Chondroitin sulfate proteoglycan 4 and its potential as an antibody immunotherapy target across different tumor types. Front Immunol. 2018;8:1911.\nPellegatta S, Savoldo B, Di Ianni N, Corbetta C, Chen Y, Patané M, et al. Constitutive and TNFα-inducible expression of chondroitin sulfate proteoglycan 4 in glioblastoma and neurospheres: Implications for CAR-T cell therapy. Sci Transl Med. 2018;10(430):eaa02731.\nGammaitoni L, Giraudo L, Leuci V, Todorovic M, Mesiano G, Picciotto F, et al. Effective activity of cytokine-induced killer cells against autologous metastatic melanoma including cells with stemness features. Clin Cancer Res. 2013;19(16):4347–58.\nSnahnicanova Z, Kasubova I, Kalman M, Grendar M, Mikolajcik P, Gabonova E, et al. Genetic and epigenetic analysis of the beta-2-microglobulin gene in microsatellite instable colorectal cancer. Clin Exp Med. 2020;20(1):87–95.\nLazaro A, Tu B, Yang R, Xiao Y, Kariyawasam K, Ng J, et al. Human leukocyte antigen (HLA) typing by DNA sequencing. Methods Mol Biol. 2013;1034:161–95.\nRolih V, Barutello G, Iussich S, De Maria R, Quaglino E, Buracco P, et al. CSPG4: a prototype oncoantigen for translational immunotherapy studies. 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activator protein-1 (AP-1) family of transcription factors modulate a diverse range of cellular signalling pathways into outputs which can be oncogenic or anti-oncogenic. The transcription of relevant genes is controlled by the cellular context, and in particular by the dimeric composition of AP-1. Here, we describe the evidence linking cJun in particular to a range of cancers. This includes correlative studies of protein levels in patient tumour samples and mechanistic understanding of the role of cJun in cancer cell models. This develops an understanding of cJun as a focal point of cancer-altered signalling which has the potential for therapeutic antagonism. Significant work has produced a range of small molecules and peptides which have been summarised here and categorised according to the binding surface they target within the cJun-DNA complex. We highlight the importance of selectively targeting a single AP-1 family member to antagonise known oncogenic function and avoid antagonism of anti-oncogenic function.",{"EN":3039},"Selective antagonism of cJun for cancer therapy",{"VOID":3041},"[\"1783795648653740657\"]",{"VOID":3043},"Vierbuchen T, Ling E, Cowley CJ, Couch CH, Wang X, Harmin DA, et al. AP-1 Transcription Factors and the BAF Complex Mediate Signal-Dependent Enhancer Selection. Mol Cell. 2017;68(6):1067–82 e12.\nMüller R, Bravo R, Burckhardt J, Curran T. Induction of c-fos gene and protein by growth factors precedes activation of c-myc. Nature. 1984;312(5996):716–20.\nEckert RL, Adhikary G, Young CA, Jans R, Crish JF, Xu W, et al. AP1 transcription factors in epidermal differentiation and skin cancer. J Skin Cancer. 2013;2013:537028.\nAngel P, Karin M. The role of Jun, Fos and the AP-1 complex in cell-proliferation and transformation. Biochim Biophys Acta. 1991;1072(2-3):129–57.\nLam CF, Yeung HT, Lam YM, Ng RK. Reactive oxygen species activate differentiation gene transcription of acute myeloid leukemia cells via the JNK\u002Fc-JUN signaling pathway. Leuk Res. 2018;68:112–9.\nReiner J, Ye F, Kashikar ND, Datta PK. STRAP regulates c-Jun ubiquitin-mediated proteolysis and cellular proliferation. Biochem Biophys Res Commun. 2011;407(2):372–7.\nChinenov Y, Kerppola TK. Close encounters of many kinds: Fos-Jun interactions that mediate transcription regulatory specificity. Oncogene. 2001;20(19):2438–52.\nShaulian E, Karin M. AP-1 in cell proliferation and survival. Oncogene. 2001;20(19):2390–400.\nVartanian R, Masri J, Martin J, Cloninger C, Holmes B, Artinian N, et al. AP-1 regulates cyclin D1 and c-MYC transcription in an AKT-dependent manner in response to mTOR inhibition: role of AIP4\u002FItch-mediated JUNB degradation. Mol Cancer Res. 2011;9(1):115–30.\nHarwood FG, Kasibhatla S, Petak I, Vernes R, Green DR, Houghton JA. Regulation of FasL by NF-kappaB and AP-1 in Fas-dependent thymineless death of human colon carcinoma cells. J Biol Chem. 2000;275(14):10023–9.\nKim KW, Cho ML, Kim HR, Ju JH, Park MK, Oh HJ, et al. Up-regulation of stromal cell-derived factor 1 (CXCL12) production in rheumatoid synovial fibroblasts through interactions with T lymphocytes: role of interleukin-17 and CD40L-CD40 interaction. Arthritis Rheum. 2007;56(4):1076–86.\nVleugel MM, Greijer AE, Bos R, van der Wall E, van Diest PJ. c-Jun activation is associated with proliferation and angiogenesis in invasive breast cancer. Hum Pathol. 2006;37(6):668–74.\nSmith LM, Wise SC, Hendricks DT, Sabichi AL, Bos T, Reddy P, et al. cJun overexpression in MCF-7 breast cancer cells produces a tumorigenic, invasive and hormone resistant phenotype. Oncogene. 1999;18(44):6063–70.\nWang H, Birkenbach M, Hart J. Expression of Jun family members in human colorectal adenocarcinoma. Carcinogenesis. 2000;21(7):1313–7.\nBossy-Wetzel E, Bravo R, Hanahan D. Transcription factors junB and c-jun are selectively up-regulated and functionally implicated in fibrosarcoma development. Genes Dev. 1992;6(12A):2340–51.\nBlau L, Knirsh R, Ben-Dror I, Oren S, Kuphal S, Hau P, et al. Aberrant expression of c-Jun in glioblastoma by internal ribosome entry site (IRES)-mediated translational activation. Proc Natl Acad Sci U S A. 2012;109(42):E2875–84.\nMathas S, Hinz M, Anagnostopoulos I, Krappmann D, Lietz A, Jundt F, et al. Aberrantly expressed c-Jun and JunB are a hallmark of Hodgkin lymphoma cells, stimulate proliferation and synergize with NF-kappa B. EMBO J. 2002;21(15):4104–13.\nSzabo E, Riffe ME, Steinberg SM, Birrer MJ, Linnoila RI. Altered cJUN expression: an early event in human lung carcinogenesis. Cancer Res. 1996;56(2):305–15.\nRangatia J, Vangala RK, Singh SM, Peer Zada AA, Elsässer A, Kohlmann A, et al. Elevated c-Jun expression in acute myeloid leukemias inhibits C\u002FEBPalpha DNA binding via leucine zipper domain interaction. Oncogene. 2003;22(30):4760–4.\nHuhe M, Liu S, Zhang Y, Zhang Z, Chen Z. Expression levels of transcription factors c-Fos and c-Jun and transmembrane protein HAb18G\u002FCD147 in urothelial carcinoma of the bladder. Mol Med Rep. 2017;15(5):2991–3000.\nSundqvist A, Morikawa M, Ren J, Vasilaki E, Kawasaki N, Kobayashi M, et al. JUNB governs a feed-forward network of TGFβ signaling that aggravates breast cancer invasion. Nucleic Acids Res. 2018;46(3):1180–95.\nPrusty BK, Das BC. Constitutive activation of transcription factor AP-1 in cervical cancer and suppression of human papillomavirus (HPV) transcription and AP-1 activity in HeLa cells by curcumin. Int J Cancer. 2005;113(6):951–60.\nAsting AG, Carén H, Andersson M, Lönnroth C, Lagerstedt K, Lundholm K. COX-2 gene expression in colon cancer tissue related to regulating factors and promoter methylation status. BMC Cancer. 2011;11:238.\nHyakusoku H, Sano D, Takahashi H, Hatano T, Isono Y, Shimada S, et al. JunB promotes cell invasion, migration and distant metastasis of head and neck squamous cell carcinoma. J Exp Clin Cancer Res. 2016;35:6.\nThomsen MK, Bakiri L, Hasenfuss SC, Wu H, Morente M, Wagner EF. Loss of JUNB\u002FAP-1 promotes invasive prostate cancer. Cell Death Differ. 2015;22(4):574–82.\nElliott B, Millena AC, Matyunina L, Zhang M, Zou J, Wang G, et al. Essential role of JunD in cell proliferation is mediated via MYC signaling in prostate cancer cells. Cancer Lett. 2019;448:155–67.\nMillena AC, Vo BT, Khan SA. JunD Is Required for Proliferation of Prostate Cancer Cells and Plays a Role in Transforming Growth Factor-β (TGF-β)-induced Inhibition of Cell Proliferation. J Biol Chem. 2016;291(34):17964–76.\nLu C, Shen Q, DuPré E, Kim H, Hilsenbeck S, Brown PH. cFos is critical for MCF-7 breast cancer cell growth. Oncogene. 2005;24(43):6516–24.\nJin SP, Kim JH, Kim MA, Yang HK, Lee HE, Lee HS, et al. Prognostic significance of loss of c-fos protein in gastric carcinoma. Pathol Oncol Res. 2007;13(4):284–9.\nMuhammad N, Bhattacharya S, Steele R, Phillips N, Ray RB. Involvement of c-Fos in the Promotion of Cancer Stem-like Cell Properties in Head and Neck Squamous Cell Carcinoma. Clin Cancer Res. 2017;23(12):3120–8.\nMahner S, Baasch C, Schwarz J, Hein S, Wölber L, Jänicke F, et al. C-Fos expression is a molecular predictor of progression and survival in epithelial ovarian carcinoma. Br J Cancer. 2008;99(8):1269–75.\nGuo JC, Li J, Zhao YP, Zhou L, Cui QC, Zhou WX, et al. Expression of c-fos was associated with clinicopathologic characteristics and prognosis in pancreatic cancer. PLoS One. 2015;10(3):e0120332.\nSaez E, Rutberg SE, Mueller E, Oppenheim H, Smoluk J, Yuspa SH, et al. c-fos is required for malignant progression of skin tumors. Cell. 1995;82(5):721–32.\nGupta S, Kumar P, Kaur H, Sharma N, Saluja D, Bharti AC, et al. Selective participation of c-Jun with Fra-2\u002Fc-Fos promotes aggressive tumor phenotypes and poor prognosis in tongue cancer. Sci Rep. 2015;5:16811.\nMilde-Langosch K, Kappes H, Riethdorf S, Löning T, Bamberger AM. FosB is highly expressed in normal mammary epithelia, but down-regulated in poorly differentiated breast carcinomas. Breast Cancer Res Treat. 2003;77(3):265–75.\nTang C, Jiang Y, Shao W, Shi W, Gao X, Qin W, et al. Abnormal expression of FOSB correlates with tumor progression and poor survival in patients with gastric cancer. Int J Oncol. 2016;49(4):1489–96.\nTing CH, Lee KY, Wu SM, Feng PH, Chan YF, Chen YC, et al. FOSB-PCDHB13 Axis Disrupts the Microtubule Network in Non-Small Cell Lung Cancer. Cancers. 2019;11(1):107. https:\u002F\u002Fdoi.org\u002F10.3390\u002Fcancers11010107.\nKataoka F, Tsuda H, Arao T, Nishimura S, Tanaka H, Nomura H, et al. EGRI and FOSB gene expressions in cancer stroma are independent prognostic indicators for epithelial ovarian cancer receiving standard therapy. Genes Chromosomes Cancer. 2012;51(3):300–12.\nKim JH, Lee JY, Lee KT, Lee JK, Lee KH, Jang KT, et al. RGS16 and FosB underexpressed in pancreatic cancer with lymph node metastasis promote tumor progression. Tumour Biol. 2010;31(5):541–8.\nBelguise K, Kersual N, Galtier F, Chalbos D. FRA-1 expression level regulates proliferation and invasiveness of breast cancer cells. Oncogene. 2005;24(8):1434–44.\nIskit S, Schlicker A, Wessels L, Peeper DS. Fra-1 is a key driver of colon cancer metastasis and a Fra-1 classifier predicts disease-free survival. Oncotarget. 2015;6(41):43146–61.\nLi L, Zhang W, Zhao S, Sun M. FOS-like antigen 1 is a prognostic biomarker in hepatocellular carcinoma. Saudi J Gastroenterol. 2019;25(6):369–76.\nZhong G, Chen X, Fang X, Wang D, Xie M, Chen Q. 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J Biol Chem. 2007;282(8):5101–5.",{"VOID":3045},"10.1186\u002Fs13046-020-01686-9","2024-05-16T21:52:57.301+00:00","https:\u002F\u002Fjeccr.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs13046-020-01686-9",[3049,3066,3081,3096],{"id":3050,"sortIndex":19,"researcher":18,"roles":3051,"affiliations":3052,"properties":3061,"displayName":3063,"givenName":18,"familyName":18},"7a23984f-ccd5-4c3d-b666-a33d7ac45a8b",[624],[3053],{"id":3054,"sortIndex":19,"affiliation":3055,"properties":18},"889dd7a9-ece3-4f2a-a3a9-7b85c1662349",{"id":3054,"createTime":18,"updateTime":18,"relativeEntities":3056,"slug":18,"properties":3057,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":3060,"statistic":18},[],{"title":3058},{"VI":3059},"Department of Biology & Biochemistry, University of Bath, Bath, UK",[],{"title":3062,"gsAuthor":3064},{"VI":3063},"Andrew Brennan",{"VOID":3065},"[\"K6jTzx8AAAAJ\"]",{"id":3067,"sortIndex":207,"researcher":18,"roles":3068,"affiliations":3069,"properties":3078,"displayName":3080,"givenName":18,"familyName":18},"1c15b508-0e3d-49d3-bbb3-0c88ea821276",[624],[3070],{"id":3071,"sortIndex":19,"affiliation":3072,"properties":18},"4c5c0d89-9c1e-4513-82b7-44b8ae792a52",{"id":3071,"createTime":18,"updateTime":18,"relativeEntities":3073,"slug":18,"properties":3074,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":3077,"statistic":18},[],{"title":3075},{"VI":3076},"School of Biosciences, University of Kent, Canterbury, UK",[],{"title":3079},{"VI":3080},"James T. Leech",{"id":3082,"sortIndex":136,"researcher":18,"roles":3083,"affiliations":3084,"properties":3091,"displayName":3093,"givenName":18,"familyName":18},"3b76eb07-9288-455a-951e-419d49c30295",[624],[3085],{"id":3071,"sortIndex":19,"affiliation":3086,"properties":18},{"id":3071,"createTime":18,"updateTime":18,"relativeEntities":3087,"slug":18,"properties":3088,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":3090,"statistic":18},[],{"title":3089},{"VI":3076},[],{"title":3092,"gsAuthor":3094},{"VI":3093},"Neil M. 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We compared the presence and participation of platelets in the TME of two tumors characterized by highly different TME, PyMT AT-3 mammary tumors and B16F1 melanoma. We show that whereas firmly adherent platelets continuously line tumor vessels of both AT-3 and B16F1 tumors, abundant extravascular stromal clusters of platelets from thrombopoietin-independent origin were present only in AT-3 mammary tumors. We further show that platelets influence the angiogenic and inflammatory profiles of AT-3 and B16F1 tumors, though with very different outcomes according to tumor type. Whereas thrombocytopenia increased bleeding in both tumor types, it further caused severe endothelial degeneration associated with massive vascular leakage, tumor swelling, and increased infiltration of cytotoxic cells, only in AT-3 tumors. These results indicate that while platelets are integral components of solid tumors, their localization and origin in the TME, as well as their impact on its shaping, are tumor type-dependent.",{"EN":3173},"The localization, origin, and impact of platelets in the tumor microenvironment are tumor type-dependent",{"VOID":3175},"[\"16562716324603653017\"]",{"EN":3177},"",{"VOID":3179},"Gasic GJ, Gasic TB, Stewart CC. Antimetastatic effects associated with platelet reduction. Proc Natl Acad Sci U S A. 1968;61:46.\nLabelle M, Begum S, Hynes RO. Direct signaling between platelets and Cancer cells induces an epithelial-mesenchymal-like Transition and promotes metastasis. Cancer Cell. 2011;20:576–90.\nNieswandt B, Hafner M, Echtenacher B, Männel DN. Lysis of tumor cells by natural killer cells in mice is impeded by platelets. Cancer Res. 1999;59:1295–300.\nKim YJ, Borsig L, Varki NM, Varki A. P-selectin deficiency attenuates tumor growth and metastasis. 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Clin Cancer Res. 2015;21:602–10.\nPlantureux L, Mege D, Crescence L, Carminita E, Robert S, Cointe S, et al. The interaction of platelets with colorectal cancer cells inhibits tumor growth but promotes metastasis. Cancer Res. 2020;80:291–303.\nVolz J, Mammadova-Bach E, Gil-Pulido J, Nandigama R, Remer K, Sorokin L, et al. Inhibition of platelet GPVI induces intratumor hemorrhage and increases efficacy of chemotherapy in mice. Blood. 2019;133:2696–706.\nCho MS, Bottsford-Miller J, Vasquez HG, Stone R, Zand B, Kroll MH, et al. Platelets increase the proliferation of ovarian cancer cells. Blood. 2012;120:4869–72.\nMichael Jv, Wurtzel JGT, Mao GF, Rao AK, Kolpakov MA, Sabri A, et al. Platelet microparticles infiltrating solid tumors transfer miRNAs that suppress tumor growth. Blood. 2017;130:567–80.\nEgan K, Crowley D, Smyth P, O’Toole S, Spillane C, Martin C et al. Platelet adhesion and Degranulation Induce Pro-survival and Pro-angiogenic Signalling in Ovarian Cancer cells. 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PLoS ONE. 2021;16.",{"VOID":3181},"10.1186\u002Fs13046-024-03001-2","2024-06-25T04:21:00.519+00:00","https:\u002F\u002Fjeccr.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs13046-024-03001-2",[3185,3200,3215,3228,3241,3254,3273,3286,3299,3312,3325,3338,3351,3364,3379,3394,3409,3422],{"id":3186,"sortIndex":19,"researcher":18,"roles":3187,"affiliations":3188,"properties":3197,"displayName":3199,"givenName":18,"familyName":18},"ca286142-7718-4a01-a169-a7104ecf4b3b",[624],[3189],{"id":3190,"sortIndex":19,"affiliation":3191,"properties":18},"9ae26b8c-bcab-4905-acbe-dab13d132293",{"id":3190,"createTime":18,"updateTime":18,"relativeEntities":3192,"slug":18,"properties":3193,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":3196,"statistic":18},[],{"title":3194},{"VI":3195},"Faculté de Pharmacie de Paris, Université Paris Cité, Inserm UMR-S 1144 -Optimisation Thérapeutique en Neuropsychopharmacologie, 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curcumin has been reported to down-regulate the expression of WT1 in leukemic cells. However, the molecular mechanism underlying the down-regulation of WT1 by curcumin is not completely delineated. The purpose of this present study is to identify a new miRNA-mediated mechanism which plays an important role in the anti-proliferation effects of curcumin in leukemic cells. K562 and HL-60 cells were treated with different concentrations of curcumin for 24 and 48 hours, the level of miR-15a\u002F16-1 and WT1 were detected by qRT-PCR and Western blotting. WT1 expression and cell proliferation were detected by Western blotting and CCK-8, after curcumin treated-K562 and HL-60 cells were transfected with anti-miR-15a\u002F16-1 oligonucleotides. We found that pure curcumin upregulated the expression of miR-15a\u002F16-1 and downregulated the expression of WT1 in leukemic cells and primary acute myeloid leukemia (AML) cells. Overexpression of miR-15a\u002F16-1 deduced the protein level of WT1 in leukemic cells, but downregulation of WT1 by siRNA-WT1 could not increase the expression of miR-15a\u002F16-1 in leukemic cells. These results reveal that curcumin induced-upregulation of miR-15a\u002F16-1 is an early event upstream to downregulation of WT1. Furthermore, anti-miR-15a\u002F16-1 oligonucleotides (AMO) partly reversed the downregulation of WT1 induced by pure curcumin in leukemic cells and AMO promoted the growth of curcumin treated-K562 and HL-60 cells. Thus, these data suggest for the first time that pure curcumin downregulated the expression of WT1 partly by upregulating the expression of miR-15a\u002F16-1 in leukemic cells. miR-15a\u002F16-1 mediated WT1 downregulation plays an important role in the anti-proliferation effect of curcumin in leukemic cells.",{"EN":3497},"Pure curcumin decreases the expression of WT1 by upregulation of miR-15a and miR-16-1 in leukemic cells",{"VOID":3499},"[\"5631557204233825312\"]",{"VOID":3501},"Kreidberg JA, Sariola H, Loring JM, Maeda M, Pelletier J, Housman D, Jaenisch R: WT-1 is required for early kidney development. Cell. 1993, 74: 679-691. 10.1016\u002F0092-8674(93)90515-R.\nBergmann L, Miething C, Maurer U, Brieger J, Karakas T, Weidmann E, Hoelzer D: High levels of Wilms' tumor gene (wt1) mRNA in acute myeloid leukemias are associated with a worse long-term outcome. Blood. 1997, 90: 1217-1225.\nGlienke W, Maute L, Koehl U, Esser R, Milz E, Bergmann L: Effective treatment of leukemic cell lines with wt1 siRNA. Leukemia. 2007, 21: 2164-2170. 10.1038\u002Fsj.leu.2404878.\nDame C, Kirschner KM, Bartz KV, Wallach T, Hussels CS, Scholz H: Wilms tumor suppressor, Wt1, is a transcriptional activator of the erythropoietin gene. Blood. 2006, 107: 4282-4290. 10.1182\u002Fblood-2005-07-2889.\nMorrison AA, Viney RL, Ladomery MR: The post-transcriptional roles of WT1, a multifunctional zinc-finger protein. Biochim Biophys Acta. 2008, 1785: 55-62.\nKuttan R, Bhanumathy P, Nirmala K, George MC: Potential anticancer activity of turmeric (Curcuma longa). Cancer Lett. 1985, 29: 197-202. 10.1016\u002F0304-3835(85)90159-4.\nBharti AC, Donato N, Singh S, Aggarwal BB: Curcumin (diferuloylmethane) down-regulates the constitutive activation of nuclear factor-kappa B and IkappaBalpha kinase in human multiple myeloma cells, leading to suppression of proliferation and induction of apoptosis. Blood. 2003, 101: 1053-1062. 10.1182\u002Fblood-2002-05-1320.\nGlienke W, Maute L, Wicht J, Bergmann L: Wilms' tumour gene 1 (WT1) as a target in curcumin treatment of pancreatic cancer cells. Eur J Cancer. 2009, 45: 874-880. 10.1016\u002Fj.ejca.2008.12.030.\nAnuchapreeda S, Tima S, Duangrat C, Limtrakul P: Effect of pure curcumin, demethoxycurcumin, and bisdemethoxycurcumin on WT1 gene expression in leukemic cell lines. Cancer Chemother Pharmacol. 2008, 62: 585-594. 10.1007\u002Fs00280-007-0642-1.\nBartel DP: MicroRNAs: genomics, biogenesis, mechanism, and function. Cell. 2004, 16: 281-297.\nLim LP: Microarray analysis shows that some microRNAs downregulate large numbers of target mRNAs. Nature. 2005, 433: 769-773. 10.1038\u002Fnature03315.\nSun M, Estrov Z, Ji Y, Coombes KR, Harris DH, Kurzrock R: Curcumin (diferuloylmethane) alters the expression profiles of microRNAs in human pancreatic cancer cells. Mol Cancer Ther. 2008, 7: 464-473. 10.1158\u002F1535-7163.MCT-07-2272.\nYang J, Cao Y, Sun J, Zhang Y: Curcumin reduces the expression of Bcl-2 by upregulating miR-15a and miR-16 in MCF-7 cells. Med Oncol. 2010, 27: 1114-1118. 10.1007\u002Fs12032-009-9344-3.\nLivak KJ, Schmittgen TD: Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods. 2001, 25: 402-408. 10.1006\u002Fmeth.2001.1262.\nCilloni D, Gottardi E, De Micheli D, Serra A, Volpe G, Messa F, Rege-Cambrin G, Guerrasio A, Divona M, Lo Coco F, Saglio G: Quantitative assessment of WT1 expression by real time quantitative PCR may be a useful tool for monitoring minimal residual disease in acute leukemia patients. Leukemia. 2002, 16: 2115-2121. 10.1038\u002Fsj.leu.2402675.\nBeillard E, Pallisgaard N, van der Velden VH, Bi W, Dee R, van der Schoot E, Delabesse E, Macintyre E, Gottardi E, Saglio G, Watzinger F, Lion T, van Dongen JJ, Hokland P, Gabert J: Evaluation of candidate control genes for diagnosis and residual disease detection in leukemic patients using 'real-time' quantitative reverse-transcriptase polymerase chain reaction (RQ-PCR) - a Europe against cancer program. Leukemia. 2003, 17: 2474-2486. 10.1038\u002Fsj.leu.2403136.\nAnuchapreeda S, Thanarattanakorn P, Sittipreechacharn S, Chanarat P, Limtrakul P: Curcumin inhibits WT1 gene expression in human leukemic K562 cells. Acta Pharmacol Sin. 2006, 27: 360-366. 10.1111\u002Fj.1745-7254.2006.00291.x.\nCalin GA, Cimmino A, Fabbri M, Ferracin M, Wojcik SE, Shimizu M, Taccioli C, Zanesi N, Garzon R, Aqeilan RI, Alder H, Volinia S, Rassenti L, Liu X, Liu CG, Kipps TJ, Negrini M, Croce CM: MiR-15a and miR-16-1 cluster functions in human leukemia. Proc Natl Acad Sci USA. 2008, 105: 5166-5171. 10.1073\u002Fpnas.0800121105.\nGao SM, Xing CY, Chen CQ, Lin SS, Dong PH, Yu FJ: miR-15a and miR-16-1 inhibit the proliferation of leukemic cells by down-regulating WT1 protein level. J Exp Clin Cancer Res. 2011, 30: 110-10.1186\u002F1756-9966-30-110.\nOstergaard M, Olesen LH, Hasle H, Kjeldsen E, Hokland P: WT1 gene expression: an excellent tool for monitoring minimal residual disease in 70% of acute myeloid leukaemia patients - results from a single-centre study. Br J Haematol. 2004, 125: 590-600. 10.1111\u002Fj.1365-2141.2004.04952.x.\nSemsri S, Krig SR, Kotelawala L, Sweeney CA, Anuchapreeda S: Inhibitory mechanism of pure curcumin on Wilms' tumor 1 (WT1) gene expression through the PKCalpha signaling pathway in leukemic K562 cells. FEBS Lett. 2011, 585: 2235-2242. 10.1016\u002Fj.febslet.2011.05.043.\nKaddar T, Rouault JP, Chien WW, Chebel A, Gadoux M, Salles G, Ffrench M, Magaud JP: Two new miR-16 targets: caprin-1 and HMGA1, proteins implicated in cell proliferation. Biol Cell. 2009, 101: 511-524. 10.1042\u002FBC20080213.\nDavis CD, Ross SA: Evidence for dietary regulation of microRNA expression in cancer cells. 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