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Volumn 1833, Issue 5, 2013, Pages 987-996

Differential inhibitory potencies and mechanisms of the type I ribosome inactivating protein marmorin on estrogen receptor (ER)-positive and ER-negative breast cancer cells

Author keywords

Apoptosis; Breast cancer; Endoplasmic reticulum stress; Estrogen receptor ; Marmorin; Ribosome inactivating protein

Indexed keywords

CASPASE 12; CASPASE 8; CASPASE 9; DEATH RECEPTOR; ESTRADIOL; ESTROGEN RECEPTOR; ESTROGEN RECEPTOR ALPHA; INOSITOL; INOSITOL REQUIRING PROTEIN 1 ALPHA; MARMORIN; PROTEIN KINASE; PROTEIN KINASE RNA ACTIVATED LIKE ENDOPLASMIC RETICULUM KINASE; RIBOSOME INACTIVATING PROTEIN 2; UNCLASSIFIED DRUG;

EID: 84874373257     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2012.12.013     Document Type: Article
Times cited : (29)

References (43)
  • 2
    • 0036174231 scopus 로고    scopus 로고
    • Breast cancer risk in usual ductal hyperplasia is defined by estrogen
    • Shaaban A.M., Sloane J.P., West C.R., Foster C.S. Breast cancer risk in usual ductal hyperplasia is defined by estrogen. Am. J. Pathol. 2002, 160:597-604.
    • (2002) Am. J. Pathol. , vol.160 , pp. 597-604
    • Shaaban, A.M.1    Sloane, J.P.2    West, C.R.3    Foster, C.S.4
  • 3
    • 0032980947 scopus 로고    scopus 로고
    • Oestrogen receptor expression in the normal and pre-cancerous breast
    • Shoker B.S., Jarvis C., Sibson D.R., Walker C., Sloane J.P. Oestrogen receptor expression in the normal and pre-cancerous breast. J. Pathol. 1999, 188:237-244.
    • (1999) J. Pathol. , vol.188 , pp. 237-244
    • Shoker, B.S.1    Jarvis, C.2    Sibson, D.R.3    Walker, C.4    Sloane, J.P.5
  • 4
    • 23744447497 scopus 로고    scopus 로고
    • Integration of the extranuclear and nuclear actions of estrogen
    • Levin E.R. Integration of the extranuclear and nuclear actions of estrogen. Mol. Endocrinol. 2005, 19:1951-1959.
    • (2005) Mol. Endocrinol. , vol.19 , pp. 1951-1959
    • Levin, E.R.1
  • 6
    • 1042292612 scopus 로고    scopus 로고
    • Advances in estrogen receptor biology: prospects for improvements in targeted breast cancer therapy
    • Shao W., Brown M. Advances in estrogen receptor biology: prospects for improvements in targeted breast cancer therapy. Breast Cancer Res. 2004, 6:39-52.
    • (2004) Breast Cancer Res. , vol.6 , pp. 39-52
    • Shao, W.1    Brown, M.2
  • 8
    • 84055216977 scopus 로고    scopus 로고
    • Estrogen-mediated upregulation of Noxa Is associated with cell cycle progression in estrogen receptor-positive breast cancer cells
    • Liu W.S., Swetzig W.M., Medisetty R., Das G.M. Estrogen-mediated upregulation of Noxa Is associated with cell cycle progression in estrogen receptor-positive breast cancer cells. PLoS One 2011, 6.
    • (2011) PLoS One , vol.6
    • Liu, W.S.1    Swetzig, W.M.2    Medisetty, R.3    Das, G.M.4
  • 12
    • 79551576468 scopus 로고    scopus 로고
    • Mechanisms of endocrine resistance in breast cancer
    • Osborne C.K., Schiff R. Mechanisms of endocrine resistance in breast cancer. Annu. Rev. Med. 2011, 62:233-247.
    • (2011) Annu. Rev. Med. , vol.62 , pp. 233-247
    • Osborne, C.K.1    Schiff, R.2
  • 13
    • 4043074939 scopus 로고    scopus 로고
    • The history of ricin, abrin and related toxins
    • Olsnes S. The history of ricin, abrin and related toxins. Toxicon 2004, 44:361-370.
    • (2004) Toxicon , vol.44 , pp. 361-370
    • Olsnes, S.1
  • 14
    • 4043133131 scopus 로고    scopus 로고
    • Ribosome-inactivating proteins - Preface
    • Stirpe F. Ribosome-inactivating proteins - Preface. Mini Rev. Med. Chem. 2004, 4.
    • (2004) Mini Rev. Med. Chem. , vol.4
    • Stirpe, F.1
  • 16
    • 3042613317 scopus 로고    scopus 로고
    • Description, distribution, activity and phylogenetic relationship of ribosome-inactivating proteins in plants, fungi and bacteria
    • Girbes T., Ferreras J.M., Arias F.J., Stirpe F. Description, distribution, activity and phylogenetic relationship of ribosome-inactivating proteins in plants, fungi and bacteria. Mini Rev. Med. Chem. 2004, 4:461-476.
    • (2004) Mini Rev. Med. Chem. , vol.4 , pp. 461-476
    • Girbes, T.1    Ferreras, J.M.2    Arias, F.J.3    Stirpe, F.4
  • 17
    • 0035884010 scopus 로고    scopus 로고
    • First simultaneous isolation of a ribosome inactivating protein and an antifungal protein from a mushroom (Lyophyllum shimeji) together with evidence for synergism of their antifungal effects
    • Lam S.K., Ng T.B. First simultaneous isolation of a ribosome inactivating protein and an antifungal protein from a mushroom (Lyophyllum shimeji) together with evidence for synergism of their antifungal effects. Arch. Biochem. Biophys. 2001, 393:271-280.
    • (2001) Arch. Biochem. Biophys. , vol.393 , pp. 271-280
    • Lam, S.K.1    Ng, T.B.2
  • 18
    • 0034804852 scopus 로고    scopus 로고
    • Hypsin, a novel thermostable ribosome-inactivating protein with antifungal and antiproliferative activities from fruiting bodies of the edible mushroom Hypsizigus marmoreus
    • Lam S.K., Ng T.B. Hypsin, a novel thermostable ribosome-inactivating protein with antifungal and antiproliferative activities from fruiting bodies of the edible mushroom Hypsizigus marmoreus. Biochem. Biophys. Res. Commun. 2001, 285:1071-1075.
    • (2001) Biochem. Biophys. Res. Commun. , vol.285 , pp. 1071-1075
    • Lam, S.K.1    Ng, T.B.2
  • 19
    • 57249115911 scopus 로고    scopus 로고
    • Marmorin, a new ribosome inactivating protein with antiproliferative and HIV-1 reverse transcriptase inhibitory activities from the mushroom Hypsizigus marmoreus
    • Wong J.H., Wang H.X., Ng T.B. Marmorin, a new ribosome inactivating protein with antiproliferative and HIV-1 reverse transcriptase inhibitory activities from the mushroom Hypsizigus marmoreus. Appl. Microbiol. Biotechnol. 2008, 81:669-674.
    • (2008) Appl. Microbiol. Biotechnol. , vol.81 , pp. 669-674
    • Wong, J.H.1    Wang, H.X.2    Ng, T.B.3
  • 20
    • 3042515159 scopus 로고    scopus 로고
    • Cytotoxicity and toxicity to animals and humans of ribosome-inactivating proteins
    • Battelli M.G. Cytotoxicity and toxicity to animals and humans of ribosome-inactivating proteins. Mini Rev. Med. Chem. 2004, 4:513-521.
    • (2004) Mini Rev. Med. Chem. , vol.4 , pp. 513-521
    • Battelli, M.G.1
  • 22
    • 0343729921 scopus 로고    scopus 로고
    • Molecular mechanism of apoptosis induced by ricin in HeLa cells
    • Gan Y.H., Peng S.Q., Liu H.Y. Molecular mechanism of apoptosis induced by ricin in HeLa cells. Acta Pharmacol. Sin. 2000, 21:243-248.
    • (2000) Acta Pharmacol. Sin. , vol.21 , pp. 243-248
    • Gan, Y.H.1    Peng, S.Q.2    Liu, H.Y.3
  • 23
    • 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 M. Plant ribosome-inactivating proteins type II induce the unfolded protein response. Cell. Mol. Life Sci. 2011, 68:1269-1281.
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 1269-1281
    • Horrix, C.1    Raviv, Z.2    Flescher, E.3    Voss, C.4    Berger, M.5
  • 24
    • 0035877840 scopus 로고    scopus 로고
    • Abrin triggers cell death by inactivating a thiol-specific antioxidant protein
    • Shih S.F., Wu Y.H., Hung C.H., Yang H.Y., Lin J.Y. Abrin triggers cell death by inactivating a thiol-specific antioxidant protein. J. Biol. Chem. 2001, 276:21870-21877.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21870-21877
    • Shih, S.F.1    Wu, Y.H.2    Hung, C.H.3    Yang, H.Y.4    Lin, J.Y.5
  • 25
    • 51249107532 scopus 로고    scopus 로고
    • Ribosome inactivating protein saporin induces apoptosis through mitochondrial cascade, independent of translation inhibition
    • Sikriwal D., Ghosh P., Batra J.K. Ribosome inactivating protein saporin induces apoptosis through mitochondrial cascade, independent of translation inhibition. Int. J. Biochem. Cell Biol. 2008, 40:2880-2888.
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 2880-2888
    • Sikriwal, D.1    Ghosh, P.2    Batra, J.K.3
  • 26
    • 67650097017 scopus 로고    scopus 로고
    • Ribosome-inactivating proteins isolated from dietary bitter melon induce apoptosis and inhibit histone deacetylase-1 selectively in premalignant and malignant prostate cancer cells
    • Xiong S.D., Yu K., Liu X.H., Yin L.H., Kirschenbaum A., Yao S., Narla G., DiFeo A., Wu J.B., Yuan Y., Ho S.M., Lam Y.W., Levine A.C. Ribosome-inactivating 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, 125:774-782.
    • (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    Narla, G.7    DiFeo, A.8    Wu, J.B.9    Yuan, Y.10    Ho, S.M.11    Lam, Y.W.12    Levine, A.C.13
  • 27
    • 0036467549 scopus 로고    scopus 로고
    • Mechanisms involved in spontaneous and Viscum album agglutinin-I-induced human neutrophil apoptosis: viscum album agglutinin-I accelerates the loss of antiapoptotic Mcl-1 expression and the degradation of cytoskeletal paxillin and vimentin proteins via caspases
    • Lavastre V., Pelletier M., Saller R., Hostanska K., Girard D. Mechanisms involved in spontaneous and Viscum album agglutinin-I-induced human neutrophil apoptosis: viscum album agglutinin-I accelerates the loss of antiapoptotic Mcl-1 expression and the degradation of cytoskeletal paxillin and vimentin proteins via caspases. J. Immunol. 2002, 168:1419-1427.
    • (2002) J. Immunol. , vol.168 , pp. 1419-1427
    • Lavastre, V.1    Pelletier, M.2    Saller, R.3    Hostanska, K.4    Girard, D.5
  • 28
    • 0035340832 scopus 로고    scopus 로고
    • Reactive oxygen species involved in trichosanthin-induced apoptosis of human choriocarcinoma cells
    • Zhang C., Gong Y., Ma H., An C., Chen D., Chen Z.L. Reactive oxygen species involved in trichosanthin-induced apoptosis of human choriocarcinoma cells. Biochem. J. 2001, 355:653-661.
    • (2001) Biochem. J. , vol.355 , pp. 653-661
    • Zhang, C.1    Gong, Y.2    Ma, H.3    An, C.4    Chen, D.5    Chen, Z.L.6
  • 30
    • 77249112249 scopus 로고    scopus 로고
    • A lectin with anti-HIV-1 reverse transcriptase, antitumor, and nitric oxide inducing activities from seeds of Phaseolus vulgaris cv. extralong autumn purple bean
    • Fang E.F., Lin P., Wong J.H., Tsao S.W., Ng T.B. A lectin with anti-HIV-1 reverse transcriptase, antitumor, and nitric oxide inducing activities from seeds of Phaseolus vulgaris cv. extralong autumn purple bean. J. Agric. Food Chem. 2010, 58:2221-2229.
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 2221-2229
    • Fang, E.F.1    Lin, P.2    Wong, J.H.3    Tsao, S.W.4    Ng, T.B.5
  • 31
    • 82355187576 scopus 로고    scopus 로고
    • A new Phaseolus vulgaris lectin induces selective toxicity on human liver carcinoma Hep G2 cells
    • Fang E.F., Pan W.L., Wong J.H., Chan Y.S., Ye X.J., Ng T.B. A new Phaseolus vulgaris lectin induces selective toxicity on human liver carcinoma Hep G2 cells. Arch. Toxicol. 2011, 85:1551-1563.
    • (2011) Arch. Toxicol. , vol.85 , pp. 1551-1563
    • Fang, E.F.1    Pan, W.L.2    Wong, J.H.3    Chan, Y.S.4    Ye, X.J.5    Ng, T.B.6
  • 32
    • 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 E.F., Zhang C.Z., Ng T.B., Wong J.H., Pan W.L., Ye X.J., Chan Y.S., Fong W.P. 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, 5:109-121.
    • (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    Chan, Y.S.7    Fong, W.P.8
  • 33
    • 2942755868 scopus 로고    scopus 로고
    • Signaling the unfolded protein response from the endoplasmic reticulum
    • Zhang K., Kaufman R.J. Signaling the unfolded protein response from the endoplasmic reticulum. J. Biol. Chem. 2004, 279:25935-25938.
    • (2004) J. Biol. Chem. , vol.279 , pp. 25935-25938
    • Zhang, K.1    Kaufman, R.J.2
  • 34
    • 0036853914 scopus 로고    scopus 로고
    • Orchestrating the unfolded protein response in health and disease
    • Kaufman R.J. Orchestrating the unfolded protein response in health and disease. J. Clin. Invest. 2002, 110:1389-1398.
    • (2002) J. Clin. Invest. , vol.110 , pp. 1389-1398
    • Kaufman, R.J.1
  • 35
    • 0036856008 scopus 로고    scopus 로고
    • Translational control in the endoplasmic reticulum stress response
    • Ron D. Translational control in the endoplasmic reticulum stress response. J. Clin. Invest. 2002, 110:1383-1388.
    • (2002) J. Clin. Invest. , vol.110 , pp. 1383-1388
    • Ron, D.1
  • 36
    • 0036314984 scopus 로고    scopus 로고
    • Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response
    • Ma Y.J., Brewer J.W., Diehl J.A., Hendershot L.M. Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response. J. Mol. Biol. 2002, 318:1351-1365.
    • (2002) J. Mol. Biol. , vol.318 , pp. 1351-1365
    • Ma, Y.J.1    Brewer, J.W.2    Diehl, J.A.3    Hendershot, L.M.4
  • 38
    • 0035684276 scopus 로고    scopus 로고
    • Faslodex(TM) for the treatment of breast cancer
    • Smolnikar K. Faslodex(TM) for the treatment of breast cancer. Drugs Today (Barc.) 2001, 37:783-789.
    • (2001) Drugs Today (Barc.) , vol.37 , pp. 783-789
    • Smolnikar, K.1
  • 39
    • 0842281645 scopus 로고    scopus 로고
    • Cell death: critical control points
    • Danial N.N., Korsmeyer S.J. Cell death: critical control points. Cell 2004, 116:205-219.
    • (2004) Cell , vol.116 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 40
    • 0029938805 scopus 로고    scopus 로고
    • Stress-induced phosphorylation and activation of the transcription factor CHOP (GADD153) by p38 MAP kinase
    • Wang X.Z., Ron D. Stress-induced phosphorylation and activation of the transcription factor CHOP (GADD153) by p38 MAP kinase. Science 1996, 272:1347-1349.
    • (1996) Science , vol.272 , pp. 1347-1349
    • Wang, X.Z.1    Ron, D.2
  • 41
    • 17144417669 scopus 로고    scopus 로고
    • TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP pathway and is involved in cell death
    • Ohoka N., Yoshii S., Hattori T., Onozaki K., Hayashi H. TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP pathway and is involved in cell death. EMBO J. 2005, 24:1243-1255.
    • (2005) EMBO J. , vol.24 , pp. 1243-1255
    • Ohoka, N.1    Yoshii, S.2    Hattori, T.3    Onozaki, K.4    Hayashi, H.5
  • 43
    • 26844495642 scopus 로고    scopus 로고
    • Maspin overexpression modulates tumor cell apoptosis through the regulation of Bcl-2 family proteins
    • Zhang W.G., Shi H.Y., Zhang M. Maspin overexpression modulates tumor cell apoptosis through the regulation of Bcl-2 family proteins. BMC Cancer 2005, 5.
    • (2005) BMC Cancer , vol.5
    • Zhang, W.G.1    Shi, H.Y.2    Zhang, M.3


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