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Volumn 34, Issue 8, 2015, Pages

Anti‑tumor activities and apoptotic mechanism of ribosome‑inactivating proteins

Author keywords

Anti tumor; Apoptosis; Cancer; Ribosome inactivating protein (RIP)

Indexed keywords

ANTINEOPLASTIC AGENT; DEATH RECEPTOR; PLANT PROTEIN; RIBOSOME INACTIVATING PROTEIN;

EID: 84939863147     PISSN: 1000467X     EISSN: 1944446X     Source Type: Journal    
DOI: 10.1186/s40880-015-0030-x     Document Type: Review
Times cited : (35)

References (89)
  • 1
    • 0023219950 scopus 로고
    • N-glycosidase activity of ricin A-chain. Mechanism of action of the toxic lectin ricin on eukaryotic ribosomes
    • Endo Y, Tsurugi K. RNA, N-glycosidase activity of ricin A-chain. Mechanism of action of the toxic lectin ricin on eukaryotic ribosomes. J Biol Chem. 1987;262:8128–30.
    • (1987) J Biol Chem , vol.262 , pp. 8128-8130
    • Endo, Y.1    Tsurugi, K.2
  • 3
    • 84863519513 scopus 로고    scopus 로고
    • Ribosome-inactivating proteins: Current status and biomedical applications
    • Puri M, Kaur I, Perugini MA, Gupta RC. Ribosome-inactivating proteins: current status and biomedical applications. Drug Discov Today. 2012;17:774–83.
    • (2012) Drug Discov Today , vol.17 , pp. 774-783
    • Puri, M.1    Kaur, I.2    Perugini, M.A.3    Gupta, R.C.4
  • 5
    • 84866050965 scopus 로고    scopus 로고
    • Trichosanthin inhibits breast cancer cell proliferation in both cell lines and nude mice by promotion of apoptosis
    • e41592
    • Fang EF, Zhang CZ, Zhang L, Wong JH, Chan YS, Pan WL, et al. Trichosanthin inhibits breast cancer cell proliferation in both cell lines and nude mice by promotion of apoptosis. PLoS One. 2012;7:e41592.
    • (2012) Plos One , vol.7
    • Fang, E.F.1    Zhang, C.Z.2    Zhang, L.3    Wong, J.H.4    Chan, Y.S.5    Pan, W.L.6
  • 6
    • 0034090956 scopus 로고    scopus 로고
    • Inhibition of MDA-MB-231 human breast tumor xenografts and HER2 expression by anti-tumor agents GAP31 and MAP30
    • Lee-Huang S, Huang PL, Sun Y, Chen HC, Kung HF, Huang PL, et al. Inhibition of MDA-MB-231 human breast tumor xenografts and HER2 expression by anti-tumor agents GAP31 and MAP30. Anticancer Res. 2000;20:653–9.
    • (2000) Anticancer Res , vol.20 , pp. 653-659
    • Lee-Huang, S.1    Huang, P.L.2    Sun, Y.3    Chen, H.C.4    Kung, H.F.5    Huang, P.L.6
  • 8
    • 84880905289 scopus 로고    scopus 로고
    • Antitumor activity of a humanized, bivalent immunotoxin targeting fn14-positive solid tumors
    • Zhou H, Hittelman WN, Yagita H, Cheung LH, Martin SS, Winkles JA, et al. Antitumor activity of a humanized, bivalent immunotoxin targeting fn14-positive solid tumors. Cancer Res. 2013;73:4439–50.
    • (2013) Cancer Res , vol.73 , pp. 4439-4450
    • Zhou, H.1    Hittelman, W.N.2    Yagita, H.3    Cheung, L.H.4    Martin, S.S.5    Winkles, J.A.6
  • 9
    • 84939815986 scopus 로고    scopus 로고
    • Expression of ERα and ERβ and its diagnostic value for breast cancer
    • (in Chinese)
    • Wan J, Zhou L. Expression of ERα and ERβ and its diagnostic value for breast cancer. Guangxi Yixue. 2011;33:1449–51 (in Chinese).
    • (2011) Guangxi Yixue , vol.33 , pp. 1449-1451
    • Wan, J.1    Zhou, L.2
  • 10
    • 84874373257 scopus 로고    scopus 로고
    • Differential inhibitory potencies and mechanisms of the type I ribosome inactivating protein marmorin on estrogen receptor (ER)-positive and ER-negative breast cancer cells
    • Pan WL, Wong JH, Fang EF, Chan YS, Ye XJ, Ng TB. Differential inhibitory potencies and mechanisms of the type I ribosome inactivating protein marmorin on estrogen receptor (ER)-positive and ER-negative breast cancer cells. Biochim Biophys Acta. 2013;1833:987–96.
    • (2013) Biochim Biophys Acta , vol.1833 , pp. 987-996
    • Pan, W.L.1    Wong, J.H.2    Fang, E.F.3    Chan, Y.S.4    Ye, X.J.5    Ng, T.B.6
  • 11
    • 84918542197 scopus 로고    scopus 로고
    • PEGylation alleviates the non-specific toxicities of alpha-Momorcharin and preserves its antitumor efficacy in vivo
    • Epub ahead of print
    • Deng NH, Wang L, He QC, Zheng JC, Meng Y, Meng YF et al. PEGylation alleviates the non-specific toxicities of alpha-Momorcharin and preserves its antitumor efficacy in vivo. Drug Deliv. 2014 [Epub ahead of print].
    • (2014) Drug Deliv
    • Deng, N.H.1    Wang, L.2    He, Q.C.3    Zheng, J.C.4    Meng, Y.5    Meng, Y.F.6
  • 12
    • 78049466464 scopus 로고    scopus 로고
    • Mechanism of trichosanthin against human leukemia/lymphoma cells in vitro
    • (in Chinese)
    • Wang YY, Ouyang DY, Zheng YT. Mechanism of trichosanthin against human leukemia/lymphoma cells in vitro. Zhongguo Shi Yan Xue Ye Xue Za Zhi. 2007;15:729–32 (in Chinese).
    • (2007) Zhongguo Shi Yan Xue Ye Xue Za Zhi , vol.15 , pp. 729-732
    • Wang, Y.Y.1    Ouyang, D.Y.2    Zheng, Y.T.3
  • 13
    • 51749083943 scopus 로고    scopus 로고
    • Atomic resolution structure of cucurmosin, a novel type 1 ribosome-inactivating protein from the sarcocarp of Cucurbita moschata
    • Hou X, Meehan EJ, Xie J, Huang M, Chen M, Chen L. Atomic resolution structure of cucurmosin, a novel type 1 ribosome-inactivating protein from the sarcocarp of Cucurbita moschata. J Struct Biol. 2008;164:81–7.
    • (2008) J Struct Biol , vol.164 , pp. 81-87
    • Hou, X.1    Meehan, E.J.2    Xie, J.3    Huang, M.4    Chen, M.5    Chen, L.6
  • 14
    • 84891513359 scopus 로고    scopus 로고
    • Effects of cucurmosin combined with common chemotherapeutics on proliferation and apoptosis of NB4 cells
    • (in Chinese)
    • Xie JM, Liu M, Liu TB, Chen MH, Yang AQ, Yang P. Effects of cucurmosin combined with common chemotherapeutics on proliferation and apoptosis of NB4 cells. Zhongguo Shi Yan Xue Ye Xue Za Zhi. 2012;20:1327–31 (in Chinese).
    • (2012) Zhongguo Shi Yan Xue Ye Xue Za Zhi , vol.20 , pp. 1327-1331
    • Xie, J.M.1    Liu, M.2    Liu, T.B.3    Chen, M.H.4    Yang, A.Q.5    Yang, P.6
  • 15
    • 80054871337 scopus 로고    scopus 로고
    • A cytotoxic type-2 ribosome inactivating protein (From leafless mistletoe) lacking sugar binding activity
    • Das MK, Sharma RS, Mishra V. A cytotoxic type-2 ribosome inactivating protein (from leafless mistletoe) lacking sugar binding activity. Int J Biol Macromol. 2011;49:1096–103.
    • (2011) Int J Biol Macromol , vol.49 , pp. 1096-1103
    • Das, M.K.1    Sharma, R.S.2    Mishra, V.3
  • 16
    • 71549169552 scopus 로고    scopus 로고
    • Construction and characterization of novel, recombinant immunotoxins targeting the Her2/neu oncogene product: In vitro and in vivo studies
    • Cao Y, Marks JD, Marks JW, Cheung LH, Kim S, Rosenblum MG. Construction and characterization of novel, recombinant immunotoxins targeting the Her2/neu oncogene product: in vitro and in vivo studies. Cancer Res. 2009;69:8987–95.
    • (2009) Cancer Res , vol.69 , pp. 8987-8995
    • Cao, Y.1    Marks, J.D.2    Marks, J.W.3    Cheung, L.H.4    Kim, S.5    Rosenblum, M.G.6
  • 18
    • 84875219244 scopus 로고    scopus 로고
    • The TWEAK receptor Fn14 is a therapeutic target in melanoma: Immunotoxins targeting Fn14 receptor for malignant melanoma treatment
    • Zhou H, Ekmekcioglu S, Marks JW, Mohamedali KA, Asrani K, Phillips KK, et al. The TWEAK receptor Fn14 is a therapeutic target in melanoma: immunotoxins targeting Fn14 receptor for malignant melanoma treatment. J Invest Dermatol. 2013;133:1052–62.
    • (2013) J Invest Dermatol , vol.133 , pp. 1052-1062
    • Zhou, H.1    Ekmekcioglu, S.2    Marks, J.W.3    Mohamedali, K.A.4    Asrani, K.5    Phillips, K.K.6
  • 19
    • 84875233141 scopus 로고    scopus 로고
    • Phase 1 study of an anti-CD33 immunotoxin, humanized monoclonal antibody M195 conjugated to recombinant gelonin (HUM-195/rGEL), in patients with advanced myeloid malignancies
    • Borthakur G, Rosenblum MG, Talpaz M, Daver N, Ravandi F, Faderl S, et al. Phase 1 study of an anti-CD33 immunotoxin, humanized monoclonal antibody M195 conjugated to recombinant gelonin (HUM-195/rGEL), in patients with advanced myeloid malignancies. Haematologica. 2013;98:217–21.
    • (2013) Haematologica , vol.98 , pp. 217-221
    • Borthakur, G.1    Rosenblum, M.G.2    Talpaz, M.3    Daver, N.4    Ravandi, F.5    Faderl, S.6
  • 20
    • 79959654218 scopus 로고    scopus 로고
    • Immunotoxins and other conjugates containing saporin-s6 for cancer therapy
    • Polito L, Bortolotti M, Pedrazzi M, Bolognesi A. Immunotoxins and other conjugates containing saporin-s6 for cancer therapy. Toxins. 2011;3:697–720.
    • (2011) Toxins , vol.3 , pp. 697-720
    • Polito, L.1    Bortolotti, M.2    Pedrazzi, M.3    Bolognesi, A.4
  • 21
    • 84880840297 scopus 로고    scopus 로고
    • Efficacy and toxicity of a CD22-targeted antibody-saporin conjugate in a xenograft model of non-Hodgkin’s lymphoma
    • Kato J, O’Donnell RT, Abuhay M, Tuscano JM. Efficacy and toxicity of a CD22-targeted antibody-saporin conjugate in a xenograft model of non-Hodgkin’s lymphoma. Oncoimmunology. 2012;1:1469–75.
    • (2012) Oncoimmunology , vol.1 , pp. 1469-1475
    • Kato, J.1    O’Donnell, R.T.2    Abuhay, M.3    Tuscano, J.M.4
  • 22
    • 0029586776 scopus 로고
    • Preclinical studies with the anti-CD19-saporin immunotoxin BU12-SAPORIN for the treatment of human-B-cell tumours
    • Flavell DJ, Flavell SU, Boehm DA, Emery L, Noss A, Ling NR, et al. Preclinical studies with the anti-CD19-saporin immunotoxin BU12-SAPORIN for the treatment of human-B-cell tumours. Br J Cancer. 1995;72:1373–9.
    • (1995) Br J Cancer , vol.72 , pp. 1373-1379
    • Flavell, D.J.1    Flavell, S.U.2    Boehm, D.A.3    Emery, L.4    Noss, A.5    Ling, N.R.6
  • 23
    • 0028147457 scopus 로고
    • Effectiveness  of HB2 (Anti-CD7)—saporin immunotoxin in an in vivo model of human T-cell leukaemia developed in severe combined immunodeficient mice
    • Morland BJ, Barley J, Boehm D, Flavell SU, Ghaleb N, Kohler JA, et al. Effectiveness  of HB2 (anti-CD7)—saporin immunotoxin in an in vivo model of human T-cell leukaemia developed in severe combined immunodeficient mice. Br J Cancer. 1994;69:279–85.
    • (1994) Br J Cancer , vol.69 , pp. 279-285
    • Morland, B.J.1    Barley, J.2    Boehm, D.3    Flavell, S.U.4    Ghaleb, N.5    Kohler, J.A.6
  • 24
    • 0035103315 scopus 로고    scopus 로고
    • Therapy of human T-cell acute lymphoblastic leukaemia with a combination  of anti-CD7 and anti-CD38-SAPORIN immunotoxins is significantly better than therapy with each individual immunotoxin
    • Flavell DJ, Boehm DA, Noss A, Warnes SL, Flavell SU. Therapy of human T-cell acute lymphoblastic leukaemia with a combination  of anti-CD7 and anti-CD38-SAPORIN immunotoxins is significantly better than therapy with each individual immunotoxin. Br J Cancer. 2001;84:571–8.
    • (2001) Br J Cancer , vol.84 , pp. 571-578
    • Flavell, D.J.1    Boehm, D.A.2    Noss, A.3    Warnes, S.L.4    Flavell, S.U.5
  • 25
    • 84867292358 scopus 로고    scopus 로고
    • Fusion toxin BLyS-gelonin inhibits growth of malignant human B cell lines in vitro and  in vivo
    • e47361
    • Luster TA, Mukherjee I, Carrell JA, Cho YH, Gill J, Kelly L, et al. Fusion toxin BLyS-gelonin inhibits growth of malignant human B cell lines in vitro and  in vivo. PLoS One. 2012;7:e47361.
    • (2012) Plos One , vol.7
    • Luster, T.A.1    Mukherjee, I.2    Carrell, J.A.3    Cho, Y.H.4    Gill, J.5    Kelly, L.6
  • 26
    • 84864148562 scopus 로고    scopus 로고
    • The therapeutic effects of rGel/BLyS fusion toxin in in vitro and in vivo models of mantle cell lymphoma
    • Lyu MA, Pham LV, Sung B, Tamayo AT, Ahn KS, Hittelman WN, et al. The therapeutic effects of rGel/BLyS fusion toxin in in vitro and in vivo models of mantle cell lymphoma. Biochem Pharmacol. 2012;84:451–8.
    • (2012) Biochem Pharmacol , vol.84 , pp. 451-458
    • Lyu, M.A.1    Pham, L.V.2    Sung, B.3    Tamayo, A.T.4    Ahn, K.S.5    Hittelman, W.N.6
  • 27
    • 84864036834 scopus 로고    scopus 로고
    • The MAP30 protein from bitter gourd (Momordica charantia) seeds promotes apoptosis in  liver cancer cells in vitro and in vivo
    • Fang EF, Zhang CZ, Wong JH, Shen JY, Li CH, Ng TB. The MAP30 protein from bitter gourd (Momordica charantia) seeds promotes apoptosis in  liver cancer cells in vitro and in vivo. Cancer Lett. 2012;324:66–74.
    • (2012) Cancer Lett , vol.324 , pp. 66-74
    • Fang, E.F.1    Zhang, C.Z.2    Wong, J.H.3    Shen, J.Y.4    Li, C.H.5    Ng, T.B.6
  • 28
    • 84855215420 scopus 로고    scopus 로고
    • Anti-proliferative effects of cucurmosin on human hepatoma HepG2 cells
    • Xie J, Que W, Liu H, Liu M, Yang A, Chen M. Anti-proliferative effects of cucurmosin on human hepatoma HepG2 cells. Mol Med Rep. 2012;5:196–201.
    • (2012) Mol Med Rep , vol.5 , pp. 196-201
    • Xie, J.1    Que, W.2    Liu, H.3    Liu, M.4    Yang, A.5    Chen, M.6
  • 29
    • 84902260115 scopus 로고    scopus 로고
    • Abrus agglutinin suppresses human hepatocellular carcinoma in vitro and in vivo by inducing caspase-mediated cell death
    • Mukhopadhyay S, Panda PK, Das DN, Sinha N, Behera B, Maiti TK, et al. Abrus agglutinin suppresses human hepatocellular carcinoma in vitro and in vivo by inducing caspase-mediated cell death. Acta Pharmacol Sin. 2014;35:814–24.
    • (2014) Acta Pharmacol Sin , vol.35 , pp. 814-824
    • Mukhopadhyay, S.1    Panda, P.K.2    Das, D.N.3    Sinha, N.4    Behera, B.5    Maiti, T.K.6
  • 30
    • 4043133131 scopus 로고    scopus 로고
    • Ribosome-inactivating proteins
    • Stirpe F. Ribosome-inactivating proteins. Toxicon. 2004;44:371–83.
    • (2004) Toxicon , vol.44 , pp. 371-383
    • Stirpe, F.1
  • 31
    • 0038268159 scopus 로고    scopus 로고
    • Inhibition of Bid-induced apoptosis by Bcl-2. TBid insertion, Bax translocation, and Bax/Bak oligomerization suppressed
    • Yi X, Yin XM, Dong Z. Inhibition of Bid-induced apoptosis by Bcl-2. tBid insertion, Bax translocation, and Bax/Bak oligomerization suppressed. J  Biol Chem. 2003;278:16992–9.
    • (2003) J  Biol Chem , vol.278 , pp. 16992-16999
    • Yi, X.1    Yin, X.M.2    Dong, Z.3
  • 33
    • 34347364663 scopus 로고    scopus 로고
    • Trichosanthin induced apoptosis in HL-60 cells via mitochondrial and endoplasmic reticulum stress signaling pathways
    • Li J, Xia X, Ke Y, Nie H, Smith MA, Zhu X. Trichosanthin induced apoptosis in HL-60 cells via mitochondrial and endoplasmic reticulum stress signaling pathways. Biochim Biophys Acta. 2007;1770:1169–80.
    • (2007) Biochim Biophys Acta , vol.1770 , pp. 1169-1180
    • Li, J.1    Xia, X.2    Ke, Y.3    Nie, H.4    Smith, M.A.5    Zhu, X.6
  • 34
    • 1842767259 scopus 로고    scopus 로고
    • Mitochondrial regulation of apoptotic cell death
    • Orrenius S. Mitochondrial regulation of apoptotic cell death. Toxicol Lett. 2004;149:19–23.
    • (2004) Toxicol Lett , vol.149 , pp. 19-23
    • Orrenius, S.1
  • 35
    • 84862907973 scopus 로고    scopus 로고
    • Momordica Charantia lectin, a type II ribosome inactivating protein, exhibits antitumor activity toward human nasopharyngeal carcinoma cells in vitro and in vivo
    • Fang EF, Zhang CZ, Ng TB, Wong JH, Pan WL, Ye XJ, et al. Momordica Charantia lectin, a type II ribosome inactivating protein, exhibits antitumor activity toward human nasopharyngeal carcinoma cells in vitro and in vivo. Cancer Prev Res (Phila). 2012;5:109–21.
    • (2012) Cancer Prev Res (Phila) , vol.5 , pp. 109-121
    • Fang, E.F.1    Zhang, C.Z.2    Ng, T.B.3    Wong, J.H.4    Pan, W.L.5    Ye, X.J.6
  • 36
    • 84878650130 scopus 로고    scopus 로고
    • Anti-tumor action of trichosanthin, a type 1 ribosome-inactivating protein, employed in traditional  Chinese medicine: A mini review
    • Sha O, Niu J, Ng TB, Cho EY, Fu X, Jiang W. Anti-tumor action of trichosanthin, a type 1 ribosome-inactivating protein, employed in traditional  Chinese medicine: a mini review. Cancer Chemother Pharmacol. 2013;71:1387–93.
    • (2013) Cancer Chemother Pharmacol , vol.71 , pp. 1387-1393
    • Sha, O.1    Niu, J.2    Ng, T.B.3    Cho, E.Y.4    Fu, X.5    Jiang, W.6
  • 37
    • 84939793013 scopus 로고    scopus 로고
    • Experimental study of trichosanthin’s effect on Hela cells proliferation
    • (in Chinese)
    • Huang YL, Huang LM, Hui Y, Lu H. Experimental study of trichosanthin’s effect on Hela cells proliferation. Lishizhen Med Materia Medica Res. 2007;18:280–1 (in Chinese).
    • (2007) Lishizhen Med Materia Medica Res , vol.18 , pp. 280-281
    • Huang, Y.L.1    Huang, L.M.2    Hui, Y.3    Lu, H.4
  • 38
    • 83055174684 scopus 로고    scopus 로고
    • Effect of recombinant  trichosanthin on proliferation of human cevical cancer Caski cells
    • (in Chinese)
    • Peng P, Huang L, Wang Y, You C, Cao W, Song H, et al. Effect of recombinant  trichosanthin on proliferation of human cevical cancer Caski cells. Zhongguo Zhong Yao Za Zhi. 2011;36:2539–42 (in Chinese).
    • (2011) Zhongguo Zhong Yao Za Zhi , vol.36 , pp. 2539-2542
    • Peng, P.1    Huang, L.2    Wang, Y.3    You, C.4    Cao, W.5    Song, H.6
  • 39
    • 74449085278 scopus 로고    scopus 로고
    • Low-density lipoprotein receptor-related protein 1 is an essential receptor for trichosanthin in 2 choriocarcinoma cell lines
    • Jiao Y, Liu W. Low-density lipoprotein receptor-related protein 1 is an essential receptor for trichosanthin in 2 choriocarcinoma cell lines. Biochem Biophys Res Commun. 2010;391:1579–84.
    • (2010) Biochem Biophys Res Commun , vol.391 , pp. 1579-1584
    • Jiao, Y.1    Liu, W.2
  • 40
    • 77955088992 scopus 로고    scopus 로고
    • Multi-chaperonepeptide-rich mixture from colo-carcinoma cells elicits potent anticancer immunity
    • Huang CX, Zhao JG, Li ZY, Li D, Xia DJ, Wang QQ, et al. Multi-chaperonepeptide-rich mixture from colo-carcinoma cells elicits potent anticancer immunity. Cancer Epidemiol. 2010;34:494–500.
    • (2010) Cancer Epidemiol , vol.34 , pp. 494-500
    • Huang, C.X.1    Zhao, J.G.2    Li, Z.Y.3    Li, D.4    Xia, D.J.5    Wang, Q.Q.6
  • 41
    • 77951616651 scopus 로고    scopus 로고
    • Cloning of trichosanthin gene and its induction effects on the apoptpsis of colorectal carcinoma LoVo cell
    • (in Chinese)
    • Gao DF, Wang BQ, Cao GM, Zhang XL. Cloning of trichosanthin gene and its induction effects on the apoptpsis of colorectal carcinoma LoVo cell. Fudan Xuebao 2010;37:157–61 (in Chinese).
    • (2010) Fudan Xuebao , vol.37 , pp. 157-161
    • Gao, D.F.1    Wang, B.Q.2    Cao, G.M.3    Zhang, X.L.4
  • 42
    • 84900793700 scopus 로고    scopus 로고
    • A novel extraction of trichosanthin from Trichosanthes kirilowii roots using three-phase partitioning and its in vitro anticancer activity
    • Mondal A. A novel extraction of trichosanthin from Trichosanthes kirilowii roots using three-phase partitioning and its in vitro anticancer activity. Pharm Biol. 2014;52:677–80.
    • (2014) Pharm Biol , vol.52 , pp. 677-680
    • Mondal, A.1
  • 43
  • 44
    • 79960038809 scopus 로고    scopus 로고
    • Trichosanthin enhances anti-tumor immune response in a murine Lewis lung cancer model by boosting the interaction between TSLC1 and CRTAM
    • Cai Y, Xiong S, Zheng Y, Luo F, Jiang P, Chu Y. Trichosanthin enhances anti-tumor immune response in a murine Lewis lung cancer model by boosting the interaction between TSLC1 and CRTAM. Cell Mol Immunol. 2011;8:359–67.
    • (2011) Cell Mol Immunol , vol.8 , pp. 359-367
    • Cai, Y.1    Xiong, S.2    Zheng, Y.3    Luo, F.4    Jiang, P.5    Chu, Y.6
  • 45
    • 0031598069 scopus 로고    scopus 로고
    • Effect of trichosanthin of cell cycle and apoptosis of murine melanoma cells
    • (in Chinese)
    • Bi L, Li H, Zhang Y. Effect of trichosanthin of cell cycle and apoptosis of murine melanoma cells. Zhongguo Zhong Xi Yi Jie He Za Zhi. 1998;18:35–7 (in Chinese).
    • (1998) Zhongguo Zhong Xi Yi Jie He Za Zhi , vol.18 , pp. 35-37
    • Bi, L.1    Li, H.2    Zhang, Y.3
  • 46
    • 84885826676 scopus 로고    scopus 로고
    • Effect of trichosanthin on apoptosis and telomerase activity of nasopharyngeal carcinomas in nude mice
    • Kang M, Ou H, Wang R, Liu W, Mao Y, Tang A. Effect of trichosanthin on apoptosis and telomerase activity of nasopharyngeal carcinomas in nude mice. J BUON. 2013;18:675–82.
    • (2013) J BUON , vol.18 , pp. 675-682
    • Kang, M.1    Ou, H.2    Wang, R.3    Liu, W.4    Mao, Y.5    Tang, A.6
  • 47
    • 84861581996 scopus 로고    scopus 로고
    • Trichosanthin down-regulates Notch signaling and inhibits proliferation of the nasopharyngeal carcinoma cell line CNE2 in vitro
    • Liu F, Wang B, Wang Z, Yu S. Trichosanthin down-regulates Notch signaling and inhibits proliferation of the nasopharyngeal carcinoma cell line CNE2 in vitro. Fitoterapia. 2012;83:838–42.
    • (2012) Fitoterapia , vol.83 , pp. 838-842
    • Liu, F.1    Wang, B.2    Wang, Z.3    Yu, S.4
  • 48
    • 69849097035 scopus 로고    scopus 로고
    • Mechanism of trichosanthin inducing apoptosis of mouse prostatic cancer RM-1 cells in vitro
    • (in Chinese)
    • Shi Z, Shan SD, Yuan T, Gui YP, Cao CH, Zhang JF. Mechanism of trichosanthin inducing apoptosis of mouse prostatic cancer RM-1 cells in vitro. Zhong Yao Cai. 2009;32:239–42 (in Chinese).
    • (2009) Zhong Yao Cai , vol.32 , pp. 239-242
    • Shi, Z.1    Shan, S.D.2    Yuan, T.3    Gui, Y.P.4    Cao, C.H.5    Zhang, J.F.6
  • 49
    • 67651095933 scopus 로고    scopus 로고
    • Induced apoptotic action of recombinant trichosanthin in human stomach adenocarcinoma MCG803 cells
    • Xu J, Gao DF, Yan GL, Fan JM. Induced apoptotic action of recombinant trichosanthin in human stomach adenocarcinoma MCG803 cells. Mol Biol Rep. 2009;36:1559–64.
    • (2009) Mol Biol Rep , vol.36 , pp. 1559-1564
    • Xu, J.1    Gao, D.F.2    Yan, G.L.3    Fan, J.M.4
  • 50
    • 77953821992 scopus 로고    scopus 로고
    • PEGylation of alphamomorcharin: Synthesis and characterization of novel anti-tumor conjugates with therapeutic potential
    • Bian X, Shen F, Chen Y, Wang B, Deng M, Meng Y. PEGylation of alphamomorcharin: synthesis and characterization of novel anti-tumor conjugates with therapeutic potential. Biotechnol Lett. 2010;32:883–90.
    • (2010) Biotechnol Lett , vol.32 , pp. 883-890
    • Bian, X.1    Shen, F.2    Chen, Y.3    Wang, B.4    Deng, M.5    Meng, Y.6
  • 51
    • 84899952397 scopus 로고    scopus 로고
    • Preferential cytotoxicity of the type I ribosome inactivating protein alpha-momorcharin on human nasopharyngeal carcinoma cells under normoxia and hypoxia
    • Pan WL, Wong JH, Fang EF, Chan YS, Ng TB, Cheung RC. Preferential cytotoxicity of the type I ribosome inactivating protein alpha-momorcharin on human nasopharyngeal carcinoma cells under normoxia and hypoxia. Biochem Pharmacol. 2014;89:329–39.
    • (2014) Biochem Pharmacol , vol.89 , pp. 329-339
    • Pan, W.L.1    Wong, J.H.2    Fang, E.F.3    Chan, Y.S.4    Ng, T.B.5    Cheung, R.C.6
  • 52
    • 84926180687 scopus 로고    scopus 로고
    • Expression of  Momordica charantia MAP30 and its anti-tumor effect on bladder cancer cells
    • Epub ahead of print
    • Hao L, Zhang ZG, Han CH, Zhao Y, Liang Q, Jiang B et al. Expression of  Momordica charantia MAP30 and its anti-tumor effect on bladder cancer cells. Minerva Urol Nefrol. 2014. [Epub ahead of print]
    • (2014) Minerva Urol Nefrol
    • Hao, L.1    Zhang, Z.G.2    Han, C.H.3    Zhao, Y.4    Liang, Q.5    Jiang, B.6
  • 54
    • 84939807758 scopus 로고    scopus 로고
    • Prokaryotic expression of MAP30 from Momordica charantia and its biological activity
    • (in Chinese)
    • Qiu HI, Rang J, Ding XZ, Hu SB, Zhang YM, Zhu DQ, et al. Prokaryotic expression of MAP30 from Momordica charantia and its biological activity. China Biotechnol. 2014;34:40–6 (in Chinese).
    • (2014) China Biotechnol. , vol.34 , pp. 40-46
    • Qiu, H.I.1    Rang, J.2    Ding, X.Z.3    Hu, S.B.4    Zhang, Y.M.5    Zhu, D.Q.6
  • 55
    • 84903891081 scopus 로고    scopus 로고
    • A novel method for simultaneous production of two ribosome-inactivating proteins, alpha-MMC and MAP30, from Momordica charantia L
    • e101998
    • Meng Y, Lin S, Liu S, Fan X, Li G, Meng Y. A novel method for simultaneous production of two ribosome-inactivating proteins, alpha-MMC and MAP30, from Momordica charantia L. PLoS One. 2014;9:e101998.
    • (2014) Plos One , vol.9
    • Meng, Y.1    Lin, S.2    Liu, S.3    Fan, X.4    Li, G.5    Meng, Y.6
  • 56
    • 84899589715 scopus 로고    scopus 로고
    • Effect of cucurmosin on chronic myeloid leukemia K562 cell line
    • in Chinese
    • Liu T, Liu H, Xie J, Hu J. Effect of cucurmosin on chronic myeloid leukemia K562 cell line. Zhongguo Shi Yan Xue Ye Xue Za Zhi. 2013;21:891–4 (in Chinese).
    • (2013) Zhongguo Shi Yan Xue Ye Xue Za Zhi , vol.8914 , pp. 21
    • Liu, T.1    Liu, H.2    Xie, J.3    Hu, J.4
  • 57
    • 84921691106 scopus 로고    scopus 로고
    • Inhibitory effect of pumpkin protein on expression of Notch signal in RPMI8226 myeloma cells
    • (in Chinese)
    • Liu T, Yang P, Xie Jie M, Hu J. Inhibitory effect of pumpkin protein on expression of Notch signal in RPMI8226 myeloma cells. Zhongguo Shi Yan Xue Ye Xue Za Zhi. 2014;22:1012–5 (in Chinese).
    • (2014) Zhongguo Shi Yan Xue Ye Xue Za Zhi , vol.22 , pp. 1012-1015
    • Liu, T.1    Yang, P.2    Xie Jie, M.3    Hu, J.4
  • 58
    • 84863011415 scopus 로고    scopus 로고
    • Cucurmosin induces apoptosis of BxPC-3 human pancreatic cancer cells via inactivation of the EGFR signaling pathway
    • Zhang B, Huang H, Xie J, Xu C, Chen M, Wang C, et al. Cucurmosin induces apoptosis of BxPC-3 human pancreatic cancer cells via inactivation of the EGFR signaling pathway. Oncol Rep. 2012;27:891–7.
    • (2012) Oncol Rep , vol.27 , pp. 891-897
    • Zhang, B.1    Huang, H.2    Xie, J.3    Xu, C.4    Chen, M.5    Wang, C.6
  • 59
    • 84880160471 scopus 로고    scopus 로고
    • Cucurmosin kills human pancreatic cancer SW-1990 cells in vitro and in vivo
    • Xie J, Wang C, Yang A, Zhang B, Yin Q, Huang H, et al. Cucurmosin kills human pancreatic cancer SW-1990 cells in vitro and in vivo. Anticancer Agents Med Chem. 2013;13:952–6.
    • (2013) Anticancer Agents Med Chem , vol.13 , pp. 952-956
    • Xie, J.1    Wang, C.2    Yang, A.3    Zhang, B.4    Yin, Q.5    Huang, H.6
  • 60
    • 84894462912 scopus 로고    scopus 로고
    • PANC-1 pancreatic cancer cell growth inhibited by cucurmosin alone and in combination with an epidermal growth factor receptor-targeted drug
    • Wang C, Yang A, Zhang B, Yin Q, Huang H, Chen M, et al. PANC-1 pancreatic cancer cell growth inhibited by cucurmosin alone and in combination with an epidermal growth factor receptor-targeted drug. Pancreas. 2014;43:291–7.
    • (2014) Pancreas , vol.43 , pp. 291-297
    • Wang, C.1    Yang, A.2    Zhang, B.3    Yin, Q.4    Huang, H.5    Chen, M.6
  • 61
    • 84884489356 scopus 로고    scopus 로고
    • Cucurmosin induces the apoptosis of human pancreatic cancer CFPAC-1 cells by inactivating the PDGFR-beta signalling pathway
    • Xie J, Wang C, Zhang B, Yang A, Yin Q, Huang H, et al. Cucurmosin induces the apoptosis of human pancreatic cancer CFPAC-1 cells by inactivating the PDGFR-beta signalling pathway. Pharmacol Rep. 2013;65:682–8. 
    • (2013) Pharmacol Rep , vol.65 , pp. 682-688
    • Xie, J.1    Wang, C.2    Zhang, B.3    Yang, A.4    Yin, Q.5    Huang, H.6
  • 62
    • 84926259268 scopus 로고    scopus 로고
    • Riproximin is a recently discovered type II ribosome inactivating protein with potential for treating cancer
    • Adwan H, Bayer H, Pervaiz A, Sagini M, Berger MR. Riproximin is a recently discovered type II ribosome inactivating protein with potential for treating cancer. Biotechnol Adv. 2014;32:1077–90.
    • (2014) Biotechnol Adv , vol.32 , pp. 1077-1090
    • Adwan, H.1    Bayer, H.2    Pervaiz, A.3    Sagini, M.4    Berger, M.R.5
  • 64
    • 0026573883 scopus 로고
    • Antitumor activity of basic fibroblast growth factor-saporin mitotoxin in vitro and in vivo
    • Beitz JG, Davol P, Clark JW, Kato J, Medina M, Frackelton AR Jr, et al. Antitumor activity of basic fibroblast growth factor-saporin mitotoxin in vitro and in vivo. Cancer Res. 1992;52:227–30.
    • (1992) Cancer Res , vol.52 , pp. 227-230
    • Beitz, J.G.1    Davol, P.2    Clark, J.W.3    Kato, J.4    Medina, M.5    Frackelton, A.R.6
  • 66
    • 1842740116 scopus 로고    scopus 로고
    • CEACAM6 as a novel target for indirect type 1 immunotoxin-based therapy in pancreatic adenocarcinoma
    • Duxbury MS, Ito H, Ashley SW, Whang EE. CEACAM6 as a novel target for indirect type 1 immunotoxin-based therapy in pancreatic adenocarcinoma. Biochem Biophys Res Commun. 2004;317:837–43.
    • (2004) Biochem Biophys Res Commun , vol.317 , pp. 837-843
    • Duxbury, M.S.1    Ito, H.2    Ashley, S.W.3    Whang, E.E.4
  • 67
    • 77956388275 scopus 로고    scopus 로고
    • Saporin toxinconjugated monoclonal antibody targeting prostate-specific membrane antigen has potent anticancer activity
    • Kuroda K, Liu H, Kim S, Guo M, Navarro V, Bander NH. Saporin toxinconjugated monoclonal antibody targeting prostate-specific membrane antigen has potent anticancer activity. Prostate. 2010;70:1286–94.
    • (2010) Prostate , vol.70 , pp. 1286-1294
    • Kuroda, K.1    Liu, H.2    Kim, S.3    Guo, M.4    Navarro, V.5    Bander, N.H.6
  • 68
    • 45549086918 scopus 로고    scopus 로고
    • Targeting CUB domain-containing protein 1 with a monoclonal antibody inhibits metastasis in a prostate cancer model
    • Siva AC, Wild MA, Kirkland RE, Nolan MJ, Lin B, Maruyama T, et al. Targeting CUB domain-containing protein 1 with a monoclonal antibody inhibits metastasis in a prostate cancer model. Cancer Res. 2008;68:3759–66.
    • (2008) Cancer Res , vol.68 , pp. 3759-3766
    • Siva, A.C.1    Wild, M.A.2    Kirkland, R.E.3    Nolan, M.J.4    Lin, B.5    Maruyama, T.6
  • 69
    • 79960124328 scopus 로고    scopus 로고
    • Development and characterization of a potent immunoconjugate targeting the Fn14 receptor on solid tumor cells
    • Zhou H, Marks JW, Hittelman WN, Yagita H, Cheung LH, Rosenblum MG,  et al. Development and characterization of a potent immunoconjugate targeting the Fn14 receptor on solid tumor cells. Mol Cancer Ther. 2011;10:1276–88.
    • (2011) Mol Cancer Ther , vol.10 , pp. 1276-1288
    • Zhou, H.1    Marks, J.W.2    Hittelman, W.N.3    Yagita, H.4    Cheung, L.H.5    Rosenblum, M.G.6
  • 70
    • 42249103255 scopus 로고    scopus 로고
    • Antitumor activity of fibroblast growth factor receptor 3-specific immunotoxins in a xenograft mouse model of bladder carcinoma is mediated by apoptosis
    • Martinez-Torrecuadrada JL, Cheung LH, Lopez-Serra P, Barderas R, Canamero M, Ferreiro S, et al. Antitumor activity of fibroblast growth factor receptor 3-specific immunotoxins in a xenograft mouse model of bladder carcinoma is mediated by apoptosis. Mol Cancer Ther. 2008;7:862–73.
    • (2008) Mol Cancer Ther , vol.7 , pp. 862-873
    • Martinez-Torrecuadrada, J.L.1    Cheung, L.H.2    Lopez-Serra, P.3    Barderas, R.4    Canamero, M.5    Ferreiro, S.6
  • 71
    • 84884524144 scopus 로고    scopus 로고
    • Targeted cytolysins synergistically potentiate cytoplasmic delivery of gelonin immunotoxin
    • Pirie CM, Liu DV, Wittrup KD. Targeted cytolysins synergistically potentiate cytoplasmic delivery of gelonin immunotoxin. Mol Cancer Ther. 2013;12:1774–82.
    • (2013) Mol Cancer Ther , vol.12 , pp. 1774-1782
    • Pirie, C.M.1    Liu, D.V.2    Wittrup, K.D.3
  • 72
    • 84883609896 scopus 로고    scopus 로고
    • Chemically and biologically synthesized CPP-modified gelonin for enhanced  anti-tumor activity
    • Shin MC, Zhang J, David AE, Trommer WE, Kwon YM, Min KA, et al. Chemically and biologically synthesized CPP-modified gelonin for enhanced  anti-tumor activity. J Control Release. 2013;172:169–78.
    • (2013) J Control Release , vol.172 , pp. 169-178
    • Shin, M.C.1    Zhang, J.2    David, A.E.3    Trommer, W.E.4    Kwon, Y.M.5    Min, K.A.6
  • 73
    • 12144291272 scopus 로고    scopus 로고
    • Bone marrow purging studies in acute myelogenous leukemia using the  recombinant anti-CD33 immunotoxin HuM195/rGel
    • Duzkale H, Pagliaro LC, Rosenblum MG, Varan A, Liu B, Reuben J, et al. Bone marrow purging studies in acute myelogenous leukemia using the  recombinant anti-CD33 immunotoxin HuM195/rGel. Biol Blood Marrow Transplant. 2003;9:364–72.
    • (2003) Biol Blood Marrow Transplant , vol.9 , pp. 364-372
    • Duzkale, H.1    Pagliaro, L.C.2    Rosenblum, M.G.3    Varan, A.4    Liu, B.5    Reuben, J.6
  • 74
    • 84864334668 scopus 로고    scopus 로고
    • In vitro and in vivo antitumor  activities of anti-EGFR single-chain variable fragment fused with  recombinant gelonin toxin
    • Zhou X, Qiu J, Wang Z, Huang N, Li X, Li Q, et al. In vitro and in vivo antitumor  activities of anti-EGFR single-chain variable fragment fused with  recombinant gelonin toxin. J Cancer Res Clin Oncol. 2012;138:1081–90.
    • (2012) J Cancer Res Clin Oncol , vol.138 , pp. 1081-1090
    • Zhou, X.1    Qiu, J.2    Wang, Z.3    Huang, N.4    Li, X.5    Li, Q.6
  • 75
    • 77951694051 scopus 로고    scopus 로고
    • The rGel/BLyS fusion toxin inhibits diffuse large B-cell lymphoma growth in vitro and in vivo
    • Lyu M-A, Rai D, Ahn KS, Sung B, Cheung LH, Marks JW, et al. The rGel/BLyS fusion toxin inhibits diffuse large B-cell lymphoma growth in vitro and in vivo. Neoplasia. 2010;12:366–75.
    • (2010) Neoplasia , vol.12 , pp. 366-375
    • Lyu, M.-A.1    Rai, D.2    Ahn, K.S.3    Sung, B.4    Cheung, L.H.5    Marks, J.W.6
  • 76
    • 0027269725 scopus 로고
    • Kinetic study of the cytotoxic effect of alpha-sarcin, a ribosome inactivating protein from Aspergillus giganteus, on tumour cell lines: Protein biosynthesis inhibition  and cell binding
    • Turnay J, Olmo N, Jimenez A, Lizarbe MA, Gavilanes JG. Kinetic study of the cytotoxic effect of alpha-sarcin, a ribosome inactivating protein from Aspergillus giganteus, on tumour cell lines: protein biosynthesis inhibition  and cell binding. Mol Cell Biochem. 1993;122:39–47.
    • (1993) Mol Cell Biochem , vol.122 , pp. 39-47
    • Turnay, J.1    Olmo, N.2    Jimenez, A.3    Lizarbe, M.A.4    Gavilanes, J.G.5
  • 77
    • 0026035077 scopus 로고
    • Biochemical, cytotoxic and pharmacokinetic properties of an immunotoxin composed of a mouse monoclonal antibody Fib75 and the ribosome-inactivating protein alpha-sarcin from Aspergillus giganteus
    • Wawrzynczak EJ, Henry RV, Cumber AJ, Parnell GD, Derbyshire EJ, Ulbrich N. Biochemical, cytotoxic and pharmacokinetic properties of an immunotoxin composed of a mouse monoclonal antibody Fib75 and the ribosome-inactivating protein alpha-sarcin from Aspergillus giganteus. Eur J Biochem. 1991;196:203–9.
    • (1991) Eur J Biochem , vol.196 , pp. 203-209
    • Wawrzynczak, E.J.1    Henry, R.V.2    Cumber, A.J.3    Parnell, G.D.4    Derbyshire, E.J.5    Ulbrich, N.6
  • 82
    • 84861607615 scopus 로고    scopus 로고
    • The effect of curcin from Jatropha curcas on apoptosis of mouse sarcoma-180 cells
    • Zhao Q, Wang W, Wang Y, Xu Y, Chen F. The effect of curcin from Jatropha curcas on apoptosis of mouse sarcoma-180 cells. Fitoterapia. 2012;83:849–52.
    • (2012) Fitoterapia , vol.83 , pp. 849-852
    • Zhao, Q.1    Wang, W.2    Wang, Y.3    Xu, Y.4    Chen, F.5
  • 83
    • 77955190717 scopus 로고    scopus 로고
    • Cloning and soluble expression of mature alpha-luffin from Luffa cylindrica and its antitumor activities in vitro
    • Liu L, Wang R, He W, He F, Huang G. Cloning and soluble expression of mature alpha-luffin from Luffa cylindrica and its antitumor activities in vitro. Acta Biochim Biophys Sin (Shanghai). 2010;42:585–92.
    • (2010) Acta Biochim Biophys Sin (Shanghai) , vol.42 , pp. 585-592
    • Liu, L.1    Wang, R.2    He, W.3    He, F.4    Huang, G.5
  • 84
    • 67650097017 scopus 로고    scopus 로고
    • Ribosomeinactivating  proteins isolated from dietary bitter melon induce apoptosis and inhibit histone deacetylase-1 selectively in premalignant and malignant prostate cancer cells
    • Xiong SD, Yu K, Liu XH, Yin LH, Kirschenbaum A, Yao S, et al. Ribosomeinactivating  proteins isolated from dietary bitter melon induce apoptosis and inhibit histone deacetylase-1 selectively in premalignant and malignant prostate cancer cells. Int J Cancer. 2009;125:774–82.
    • (2009) Int J Cancer , vol.125 , pp. 774-782
    • Xiong, S.D.1    Yu, K.2    Liu, X.H.3    Yin, L.H.4    Kirschenbaum, A.5    Yao, S.6
  • 85
    • 33845649761 scopus 로고    scopus 로고
    • Identification and characterization of riproximin, a new type II ribosome-inactivating protein with antineoplastic activity from Ximenia americana
    • Voss C, Eyol E, Frank M, von der Lieth CW, Berger MR. Identification and characterization of riproximin, a new type II ribosome-inactivating protein with antineoplastic activity from Ximenia americana. FASEB J. 2006;20:1194–6.
    • (2006) FASEB J , vol.20 , pp. 1194-1196
    • Voss, C.1    Eyol, E.2    Frank, M.3    Von Der Lieth, C.W.4    Berger, M.R.5
  • 86
    • 79953695935 scopus 로고    scopus 로고
    • Plant ribosome-inactivating proteins type II induce the unfolded protein response
    • Horrix C, Raviv Z, Flescher E, Voss C, Berger MR. Plant ribosome-inactivating proteins type II induce the unfolded protein response. Cell Mol Life Sci. 2011;68:1269–81.
    • (2011) Cell Mol Life Sci , vol.68 , pp. 1269-1281
    • Horrix, C.1    Raviv, Z.2    Flescher, E.3    Voss, C.4    Berger, M.R.5
  • 87
    • 43049176801 scopus 로고    scopus 로고
    • Molecular mechanisms of mistletoe plant extract-induced apoptosis in acute lymphoblastic leukemia in vivo and in vitro
    • Seifert G, Jesse P, Laengler A, Reindl T, Luth M, Lobitz S, et al. Molecular mechanisms of mistletoe plant extract-induced apoptosis in acute lymphoblastic leukemia in vivo and in vitro. Cancer Lett. 2008;264:218–28.
    • (2008) Cancer Lett , vol.264 , pp. 218-228
    • Seifert, G.1    Jesse, P.2    Laengler, A.3    Reindl, T.4    Luth, M.5    Lobitz, S.6
  • 88
    • 34248579289 scopus 로고    scopus 로고
    • Isolation and characterization of ribosome-inactivating proteins from Cucurbitaceae
    • Zhang D, Halaweish FT. Isolation and characterization of ribosome-inactivating proteins from Cucurbitaceae. Chem Biodivers. 2007;4:431–42.
    • (2007) Chem Biodivers , vol.4 , pp. 431-442
    • Zhang, D.1    Halaweish, F.T.2
  • 89
    • 0037044183 scopus 로고    scopus 로고
    • Targeting cancer cells with transferrin conjugates containing the non-toxic type 2 ribosome-inactivating proteins nigrin b or ebulin I
    • Citores L, Ferreras JM, Munoz R, Benitez J, Jimenez P, Girbes T. Targeting cancer cells with transferrin conjugates containing the non-toxic type 2 ribosome-inactivating proteins nigrin b or ebulin I. Cancer Lett. 2002;184:29–35.
    • (2002) Cancer Lett. , vol.184 , pp. 29-35
    • Citores, L.1    Ferreras, J.M.2    Munoz, R.3    Benitez, J.4    Jimenez, P.5    Girbes, T.6


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