메뉴 건너뛰기




Volumn 5, Issue 6, 2014, Pages 1609-1620

TBX2 represses CST6 resulting in uncontrolled legumain activity to sustain breast cancer proliferation: A novel cancer-selective target pathway with therapeutic opportunities

Author keywords

Breast cancer; CST6; LGMN; TBX2

Indexed keywords

CATHEPSIN; CYSTATIN M; EARLY GROWTH RESPONSE FACTOR 1; LEGUMAIN; SMALL INTERFERING RNA; TRANSCRIPTION FACTOR T BET; CST6 PROTEIN, HUMAN; CYSTEINE PROTEINASE; MESSENGER RNA; T BOX TRANSCRIPTION FACTOR; T-BOX DOMAIN PROTEIN 2;

EID: 84904261428     PISSN: None     EISSN: 19492553     Source Type: Journal    
DOI: 10.18632/oncotarget.1707     Document Type: Article
Times cited : (35)

References (45)
  • 3
    • 1642396456 scopus 로고    scopus 로고
    • Tbx2 directly represses the expression of the p21(WAF1) cyclin-dependent kinase inhibitor
    • Prince S, Carreira S, Vance KW, Abrahams A and Goding CR. Tbx2 directly represses the expression of the p21(WAF1) cyclin-dependent kinase inhibitor. Cancer Res. 2004; 64(5):1669-1674.
    • (2004) Cancer Res , vol.64 , Issue.5 , pp. 1669-1674
    • Prince, S.1    Carreira, S.2    Vance, K.W.3    Abrahams, A.4    Goding, C.R.5
  • 4
    • 16844387097 scopus 로고    scopus 로고
    • Tbx2 is overexpressed and plays an important role in maintaining proliferation and suppression of senescence in melanomas
    • Vance KW, Carreira S, Brosch G and Goding CR. Tbx2 is overexpressed and plays an important role in maintaining proliferation and suppression of senescence in melanomas. Cancer Res. 2005; 65(6):2260-2268.
    • (2005) Cancer Res , vol.65 , Issue.6 , pp. 2260-2268
    • Vance, K.W.1    Carreira, S.2    Brosch, G.3    Goding, C.R.4
  • 5
    • 64649094528 scopus 로고    scopus 로고
    • Expression of TBX2 promotes anchorage-independent growth and survival in the p53-negative SW13 adrenocortical carcinoma
    • Ismail A and Bateman A. Expression of TBX2 promotes anchorage-independent growth and survival in the p53-negative SW13 adrenocortical carcinoma. Cancer Lett. 2009.
    • (2009) Cancer Lett
    • Ismail, A.1    Bateman, A.2
  • 8
    • 84863005397 scopus 로고    scopus 로고
    • NCI's provocative questions on cancer: some answers to ignite discussion
    • Blagosklonny MV. NCI's provocative questions on cancer: some answers to ignite discussion. Oncotarget. 2(12):1352-1367.
    • Oncotarget , vol.2 , Issue.12 , pp. 13521367
    • Blagosklonny, M.V.1
  • 10
    • 0031030180 scopus 로고    scopus 로고
    • Identification, cloning, and characterization of cystatin M, a novel cysteine proteinase inhibitor, down-regulated in breast cancer
    • Sotiropoulou G, Anisowicz A and Sager R. Identification, cloning, and characterization of cystatin M, a novel cysteine proteinase inhibitor, down-regulated in breast cancer. J Biol Chem. 1997; 272(2):903-910.
    • (1997) J Biol Chem , vol.272 , Issue.2 , pp. 903-910
    • Sotiropoulou, G.1    Anisowicz, A.2    Sager, R.3
  • 11
    • 33748041100 scopus 로고    scopus 로고
    • Epigenetic silencing of the tumor suppressor cystatin M occurs during breast cancer progression
    • Ai L, Kim WJ, Kim TY, Fields CR, Massoll NA, Robertson KD and Brown KD. Epigenetic silencing of the tumor suppressor cystatin M occurs during breast cancer progression. Cancer Res. 2006; 66(16):7899-7909.
    • (2006) Cancer Res , vol.66 , Issue.16 , pp. 7899-7909
    • Ai, L.1    Kim, W.J.2    Kim, T.Y.3    Fields, C.R.4    Massoll, N.A.5    Robertson, K.D.6    Brown, K.D.7
  • 15
    • 68349160753 scopus 로고    scopus 로고
    • Frequent loss of cystatin E/M expression implicated in the progression of prostate cancer
    • Pulukuri SM, Gorantla B, Knost JA and Rao JS. Frequent loss of cystatin E/M expression implicated in the progression of prostate cancer. Oncogene. 2009; 28(31):2829-2838.
    • (2009) Oncogene , vol.28 , Issue.31 , pp. 2829-2838
    • Pulukuri, S.M.1    Gorantla, B.2    Knost, J.A.3    Rao, J.S.4
  • 16
    • 73149115274 scopus 로고    scopus 로고
    • expression is reduced in gastric carcinoma and is associated with promoter hypermethylation
    • Chen X, Cao X, Dong W, Xia M, Luo S, Fan Q and Xie J. Cystatin M. expression is reduced in gastric carcinoma and is associated with promoter hypermethylation. Biochem Biophys Res Commun. 2009; 391(1):1070-1074.
    • (2009) Biochem Biophys Res Commun , vol.391 , Issue.1 , pp. 1070-1074
    • Chen, X.1    Cao, X.2    Dong, W.3    Xia, M.4    Luo, S.5    Fan, Q.6    Xie, J.7    Cystatin, M.8
  • 19
    • 16844367758 scopus 로고    scopus 로고
    • Legumain expression in relation to clinicopathologic and biological variables in colorectal cancer
    • Murthy RV, Arbman G, Gao J, Roodman GD and Sun XF. Legumain expression in relation to clinicopathologic and biological variables in colorectal cancer. Clin Cancer Res. 2005; 11(6):2293-2299.
    • (2005) Clin Cancer Res , vol.11 , Issue.6 , pp. 2293-2299
    • Murthy, R.V.1    Arbman, G.2    Gao, J.3    Roodman, G.D.4    Sun, X.F.5
  • 21
    • 0030883558 scopus 로고    scopus 로고
    • Inhibition of autophagy abrogates tumour necrosis factor alpha induced apoptosis in human T-lymphoblastic leukaemic cells
    • Jia L, Dourmashkin RR, Allen PD, Gray AB, Newland AC and Kelsey SM. Inhibition of autophagy abrogates tumour necrosis factor alpha induced apoptosis in human T-lymphoblastic leukaemic cells. Br J Haematol. 1997; 98(3):673-685.
    • (1997) Br J Haematol , vol.98 , Issue.3 , pp. 673-685
    • Jia, L.1    Dourmashkin, R.R.2    Allen, P.D.3    Gray, A.B.4    Newland, A.C.5    Kelsey, S.M.6
  • 22
    • 33744915019 scopus 로고    scopus 로고
    • Cystatin M/E is a high affinity inhibitor of cathepsin V and cathepsin L by a reactive site that is distinct from the legumain-binding site A novel clue for the role of cystatin M/E in epidermal cornification.
    • Cheng T, Hitomi K, van Vlijmen-Willems IM, de Jongh GJ, Yamamoto K, Nishi K, Watts C, Reinheckel T, Schalkwijk J and Zeeuwen PL. Cystatin M/E is a high affinity inhibitor of cathepsin V and cathepsin L by a reactive site that is distinct from the legumain-binding site. A novel clue for the role of cystatin M/E in epidermal cornification. J Biol Chem. 2006; 281(23):15893-15899.
    • (2006) J Biol Chem. , vol.281 , Issue.23 , pp. 15893-15899
    • Cheng, T.1    Hitomi, K.2    van Vlijmen-Willems, I.M.3    de Jongh, G.J.4    Yamamoto, K.5    Nishi, K.6    Watts, C.7    Reinheckel, T.8    Schalkwijk, J.9    Zeeuwen, P.L.10
  • 23
    • 63049116236 scopus 로고    scopus 로고
    • Glycosylation directs targeting and activation of cystatin f from intracellular and extracellular sources
    • Colbert JD, Plechanovova A and Watts C. Glycosylation directs targeting and activation of cystatin f from intracellular and extracellular sources. Traffic. 2009; 10(4):425-437.
    • (2009) Traffic , vol.10 , Issue.4 , pp. 425-437
    • Colbert, J.D.1    Plechanovova, A.2    Watts, C.3
  • 27
    • 69249129052 scopus 로고    scopus 로고
    • Methylation profiles of 22 candidate genes in breast cancer using high-throughput MALDI-TOF mass array
    • Radpour R, Kohler C, Haghighi MM, Fan AX, Holzgreve W and Zhong XY. Methylation profiles of 22 candidate genes in breast cancer using high-throughput MALDI-TOF mass array. Oncogene. 2009; 28(33):2969-2978.
    • (2009) Oncogene , vol.28 , Issue.33 , pp. 2969-2978
    • Radpour, R.1    Kohler, C.2    Haghighi, M.M.3    Fan, A.X.4    Holzgreve, W.5    Zhong, X.Y.6
  • 29
    • 39649104991 scopus 로고    scopus 로고
    • DNMT3b overexpression contributes to a hypermethylator phenotype in human breast cancer cell lines
    • Roll JD, Rivenbark AG, Jones WD and Coleman WB. DNMT3b overexpression contributes to a hypermethylator phenotype in human breast cancer cell lines. Mol Cancer. 2008; 7:15.
    • (2008) Mol Cancer , vol.7 , pp. 15
    • Roll, J.D.1    Rivenbark, A.G.2    Jones, W.D.3    Coleman, W.B.4
  • 31
    • 0038243036 scopus 로고    scopus 로고
    • Overexpression of legumain in tumors is significant for invasion/metastasis and a candidate enzymatic target for prodrug therapy
    • Liu C, Sun C, Huang H, Janda K and Edgington T. Overexpression of legumain in tumors is significant for invasion/metastasis and a candidate enzymatic target for prodrug therapy. Cancer Res. 2003; 63(11):2957-2964.
    • (2003) Cancer Res , vol.63 , Issue.11 , pp. 2957-2964
    • Liu, C.1    Sun, C.2    Huang, H.3    Janda, K.4    Edgington, T.5
  • 32
    • 84897925851 scopus 로고    scopus 로고
    • Expression of legumain correlates with prognosis and metastasis in gastric carcinoma
    • Guo P, Zhu Z, Sun Z, Wang Z, Zheng X and Xu H. Expression of legumain correlates with prognosis and metastasis in gastric carcinoma. PLoS One. 2013; 8(9):e73090.
    • (2013) PLoS One , vol.8 , Issue.9
    • Guo, P.1    Zhu, Z.2    Sun, Z.3    Wang, Z.4    Zheng, X.5    Xu, H.6
  • 34
    • 0034937132 scopus 로고    scopus 로고
    • Activation of progelatinase A by mammalian legumain, a recently discovered cysteine proteinase
    • Chen JM, Fortunato M, Stevens RA and Barrett AJ. Activation of progelatinase A by mammalian legumain, a recently discovered cysteine proteinase. Biol Chem. 2001; 382(5):777-783.
    • (2001) Biol Chem , vol.382 , Issue.5 , pp. 777-783
    • Chen, J.M.1    Fortunato, M.2    Stevens, R.A.3    Barrett, A.J.4
  • 36
    • 84859562694 scopus 로고    scopus 로고
    • Targeting autophagy addiction in cancer
    • Mancias JD and Kimmelman AC. Targeting autophagy addiction in cancer. Oncotarget. 2(12):1302-1306.
    • Oncotarget , vol.2 , Issue.12 , pp. 13021306
    • Mancias, J.D.1    Kimmelman, A.C.2
  • 37
    • 0347358966 scopus 로고    scopus 로고
    • Aza-peptide epoxides: potent and selective inhibitors of Schistosoma mansoni and pig kidney legumains (asparaginyl endopeptidases)
    • James KE, Gotz MG, Caffrey CR, Hansell E, Carter W, Barrett AJ, McKerrow JH and Powers JC. Aza-peptide epoxides: potent and selective inhibitors of Schistosoma mansoni and pig kidney legumains (asparaginyl endopeptidases). Biol Chem. 2003; 384(12):1613-1618.
    • (2003) Biol Chem , vol.384 , Issue.12 , pp. 1613-1618
    • James, K.E.1    Gotz, M.G.2    Caffrey, C.R.3    Hansell, E.4    Carter, W.5    Barrett, A.J.6    McKerrow, J.H.7    Powers, J.C.8
  • 38
    • 84862818465 scopus 로고    scopus 로고
    • Synthesis and evaluation of aza-peptidyl inhibitors of the lysosomal asparaginyl endopeptidase, legumain
    • Lee J and Bogyo M. Synthesis and evaluation of aza-peptidyl inhibitors of the lysosomal asparaginyl endopeptidase, legumain. Bioorganic & medicinal chemistry letters. 2012; 22(3):1340-1343.
    • (2012) Bioorganic & medicinal chemistry letters , vol.22 , Issue.3 , pp. 1340-1343
    • Lee, J.1    Bogyo, M.2
  • 39
    • 78650532605 scopus 로고    scopus 로고
    • The Legumain Protease-Activated Auristatin Prodrugs Suppress Tumor Growth and Metastasis without Toxicity
    • Bajjuri KM, Liu Y, Liu C and Sinha SC. The Legumain Protease-Activated Auristatin Prodrugs Suppress Tumor Growth and Metastasis without Toxicity. ChemMedChem. 2012; 6(1):54-59.
    • (2012) ChemMedChem , vol.6 , Issue.1 , pp. 54-59
    • Bajjuri, K.M.1    Liu, Y.2    Liu, C.3    Sinha, S.C.4
  • 40
    • 63749126402 scopus 로고    scopus 로고
    • A novel antitumor prodrug platform designed to be cleaved by the endoprotease legumain
    • Stern L, Perry R, Ofek P, Many A, Shabat D and Satchi-Fainaro R. A novel antitumor prodrug platform designed to be cleaved by the endoprotease legumain. Bioconjug Chem. 2009; 20(3):500-510.
    • (2009) Bioconjug Chem , vol.20 , Issue.3 , pp. 500-510
    • Stern, L.1    Perry, R.2    Ofek, P.3    Many, A.4    Shabat, D.5    Satchi-Fainaro, R.6
  • 41
  • 42
    • 82255191976 scopus 로고    scopus 로고
    • Synthetic enzyme inhibitor: a novel targeting ligand for nanotherapeutic drug delivery inhibiting tumor growth without systemic toxicity
    • Liao D, Liu Z, Wrasidlo W, Chen T, Luo Y, Xiang R and Reisfeld RA. Synthetic enzyme inhibitor: a novel targeting ligand for nanotherapeutic drug delivery inhibiting tumor growth without systemic toxicity. Nanomedicine. 7(6):665-673.
    • Nanomedicine , vol.7 , Issue.6 , pp. 665673
    • Liao, D.1    Liu, Z.2    Wrasidlo, W.3    Chen, T.4    Luo, Y.5    Xiang, R.6    Reisfeld, R.A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.