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Volumn 1850, Issue 2, 2015, Pages 401-410

Psammaplin A induces Sirtuin 1-dependent autophagic cell death in doxorubicin-resistant MCF-7/adr human breast cancer cells and xenografts

Author keywords

Autophagy; Breast cancer; Doxorubicin; Drug resistant; SIRT1

Indexed keywords

AUTOPHAGY RELATED PROTEIN; DAMAGE REGULATED AUTOPHAGY MODULATOR; DOXORUBICIN; HYDROLASE INHIBITOR; MEMBRANE PROTEIN; NATURAL PRODUCT; NICOTINAMIDE; PROTEIN P53; PSAMMAPLIN A; SALERMIDE; SIRTINOL; SIRTUIN 1; UNCLASSIFIED DRUG; ANTINEOPLASTIC ANTIBIOTIC; DISULFIDE; DRAM1 PROTEIN, HUMAN; SIRT1 PROTEIN, HUMAN; TP53 PROTEIN, HUMAN; TYROSINE;

EID: 84913601119     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2014.11.007     Document Type: Article
Times cited : (36)

References (63)
  • 2
    • 4143050290 scopus 로고    scopus 로고
    • The interaction between FOXO and SIRT1: Ttipping the balance towards survival
    • M.E. Giannakou, and L. Partridge The interaction between FOXO and SIRT1: tipping the balance towards survival Trends Cell Biol. 14 2004 408 412
    • (2004) Trends Cell Biol. , vol.14 , pp. 408-412
    • Giannakou, M.E.1    Partridge, L.2
  • 3
    • 34249083199 scopus 로고    scopus 로고
    • Sirtuins in mammals: Insights into their biological function
    • S. Michan, and D. Sinclair Sirtuins in mammals: insights into their biological function Biochem. J. 404 2007 1 13
    • (2007) Biochem. J. , vol.404 , pp. 1-13
    • Michan, S.1    Sinclair, D.2
  • 5
  • 6
    • 0034193776 scopus 로고    scopus 로고
    • Sir2 links chromatin silencing, metabolism, and aging
    • L. Guarente Sir2 links chromatin silencing, metabolism, and aging Genes Dev. 14 2000 1021 1026
    • (2000) Genes Dev. , vol.14 , pp. 1021-1026
    • Guarente, L.1
  • 7
    • 10844236451 scopus 로고    scopus 로고
    • Nutrient availability regulates SIRT1 through a forkhead-dependent pathway
    • S. Nemoto, M.M. Fergusson, and T. Finkel Nutrient availability regulates SIRT1 through a forkhead-dependent pathway Science 306 2004 2105 2108
    • (2004) Science , vol.306 , pp. 2105-2108
    • Nemoto, S.1    Fergusson, M.M.2    Finkel, T.3
  • 8
    • 34249683635 scopus 로고    scopus 로고
    • Cross-talk between aging and cancer: The epigenetic language
    • M.F. Fraga, R. Agrelo, and M. Esteller Cross-talk between aging and cancer: the epigenetic language Ann. N. Y. Acad. Sci. 1100 2007 60 74
    • (2007) Ann. N. Y. Acad. Sci. , vol.1100 , pp. 60-74
    • Fraga, M.F.1    Agrelo, R.2    Esteller, M.3
  • 9
    • 53349091778 scopus 로고    scopus 로고
    • SIRT1 contributes in part to cisplatin resistance in cancer cells by altering mitochondrial metabolism
    • X.J. Liang, T. Finkel, D.W. Shen, J.J. Yin, A. Aszalos, and M.M. Gottesman SIRT1 contributes in part to cisplatin resistance in cancer cells by altering mitochondrial metabolism Mol. Cancer Res. 6 2008 1499 1506
    • (2008) Mol. Cancer Res. , vol.6 , pp. 1499-1506
    • Liang, X.J.1    Finkel, T.2    Shen, D.W.3    Yin, J.J.4    Aszalos, A.5    Gottesman, M.M.6
  • 10
    • 58849158388 scopus 로고    scopus 로고
    • How does SIRT1 affect metabolism, senescence and cancer?
    • C.L. Brooks, and W. Gu How does SIRT1 affect metabolism, senescence and cancer? Nat. Rev. Cancer 9 2009 123 128
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 123-128
    • Brooks, C.L.1    Gu, W.2
  • 11
    • 65549120715 scopus 로고    scopus 로고
    • Modes of p53 regulation
    • J.P. Kruse, and W. Gu Modes of p53 regulation Cell 137 2009 609 622
    • (2009) Cell , vol.137 , pp. 609-622
    • Kruse, J.P.1    Gu, W.2
  • 12
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2alpha promotes cell survival under stress
    • J. Luo, A.Y. Nikolaev, S. Imai, D. Chen, F. Su, A. Shiloh, L. Guarente, and W. Gu Negative control of p53 by Sir2alpha promotes cell survival under stress Cell 107 2001 137 148
    • (2001) Cell , vol.107 , pp. 137-148
    • Luo, J.1    Nikolaev, A.Y.2    Imai, S.3    Chen, D.4    Su, F.5    Shiloh, A.6    Guarente, L.7    Gu, W.8
  • 14
    • 70349442548 scopus 로고    scopus 로고
    • The first 30 years of p53: Growing ever more complex
    • A.J. Levine, and M. Oren The first 30 years of p53: growing ever more complex Nat. Rev. Cancer 9 2009 749 758
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 749-758
    • Levine, A.J.1    Oren, M.2
  • 16
    • 0033992478 scopus 로고    scopus 로고
    • P53 and human cancer: The first ten thousand mutations
    • P. Hainaut, and M. Hollstein p53 and human cancer: the first ten thousand mutations Adv. Cancer Res. 77 2000 81 137
    • (2000) Adv. Cancer Res. , vol.77 , pp. 81-137
    • Hainaut, P.1    Hollstein, M.2
  • 17
    • 78649833334 scopus 로고    scopus 로고
    • P53-dependent regulation of autophagy protein LC3 supports cancer cell survival under prolonged starvation
    • R. Scherz-Shouval, H. Weidberg, C. Gonen, S. Wilder, Z. Elazar, and M. Oren p53-dependent regulation of autophagy protein LC3 supports cancer cell survival under prolonged starvation Proc. Natl. Acad. Sci. U. S. A. 107 2010 18511 18516
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 18511-18516
    • Scherz-Shouval, R.1    Weidberg, H.2    Gonen, C.3    Wilder, S.4    Elazar, Z.5    Oren, M.6
  • 20
    • 79957895563 scopus 로고    scopus 로고
    • P53 signaling and autophagy in cancer: A revolutionary strategy could be developed for cancer treatment
    • X. Sui, L. Jin, X. Huang, S. Geng, C. He, and X. Hu p53 signaling and autophagy in cancer: a revolutionary strategy could be developed for cancer treatment Autophagy 7 2011 565 571
    • (2011) Autophagy , vol.7 , pp. 565-571
    • Sui, X.1    Jin, L.2    Huang, X.3    Geng, S.4    He, C.5    Hu, X.6
  • 23
    • 33846260837 scopus 로고    scopus 로고
    • DRAM links autophagy to p53 and programmed cell death
    • D. Crighton, S. Wilkinson, and K.M. Ryan DRAM links autophagy to p53 and programmed cell death Autophagy 3 2007 72 74
    • (2007) Autophagy , vol.3 , pp. 72-74
    • Crighton, D.1    Wilkinson, S.2    Ryan, K.M.3
  • 24
    • 77649171884 scopus 로고    scopus 로고
    • Novel histone deacetylase inhibitors in clinical trials as anti-cancer agents
    • J. Tan, S. Cang, Y. Ma, R.L. Petrillo, and D. Liu Novel histone deacetylase inhibitors in clinical trials as anti-cancer agents J. Hematol. Oncol. 3 2010 5
    • (2010) J. Hematol. Oncol. , vol.3 , pp. 5
    • Tan, J.1    Cang, S.2    Ma, Y.3    Petrillo, R.L.4    Liu, D.5
  • 26
    • 0029603564 scopus 로고
    • Cytotoxic compounds from a two-sponge association
    • J.H. Jung, C.J. Sim, and C.O. Lee Cytotoxic compounds from a two-sponge association J. Nat. Prod. 58 1995 1722 1726
    • (1995) J. Nat. Prod. , vol.58 , pp. 1722-1726
    • Jung, J.H.1    Sim, C.J.2    Lee, C.O.3
  • 27
    • 0032806308 scopus 로고    scopus 로고
    • Psammaplin A, a natural phenolic compound, has inhibitory effect on human topoisomerase II and is cytotoxic to cancer cells
    • D. Kim, I.S. Lee, J.H. Jung, C.O. Lee, and S.U. Choi Psammaplin A, a natural phenolic compound, has inhibitory effect on human topoisomerase II and is cytotoxic to cancer cells Anticancer Res. 19 1999 4085 4090
    • (1999) Anticancer Res. , vol.19 , pp. 4085-4090
    • Kim, D.1    Lee, I.S.2    Jung, J.H.3    Lee, C.O.4    Choi, S.U.5
  • 30
    • 48549092906 scopus 로고    scopus 로고
    • Decreased production of vascular endothelial growth factor in adriamycin-resistant breast cancer cells
    • J.A. Kim, K.B. Cho, M.R. Kim, B.C. Park, S.K. Kim, M.Y. Lee, and K.W. Kang Decreased production of vascular endothelial growth factor in adriamycin-resistant breast cancer cells Cancer Lett. 268 2008 225 232
    • (2008) Cancer Lett. , vol.268 , pp. 225-232
    • Kim, J.A.1    Cho, K.B.2    Kim, M.R.3    Park, B.C.4    Kim, S.K.5    Lee, M.Y.6    Kang, K.W.7
  • 31
    • 37349061341 scopus 로고    scopus 로고
    • A natural histone deacetylase inhibitor, Psammaplin A, induces cell cycle arrest and apoptosis in human endometrial cancer cells
    • M.Y. Ahn, J.H. Jung, Y.J. Na, and H.S. Kim A natural histone deacetylase inhibitor, Psammaplin A, induces cell cycle arrest and apoptosis in human endometrial cancer cells Gynecol. Oncol. 108 2008 27 33
    • (2008) Gynecol. Oncol. , vol.108 , pp. 27-33
    • Ahn, M.Y.1    Jung, J.H.2    Na, Y.J.3    Kim, H.S.4
  • 34
    • 27944504351 scopus 로고    scopus 로고
    • P62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • G. Bjorkoy, T. Lamark, A. Brech, H. Outzen, M. Perander, A. Overvatn, H. Stenmark, and T. Johansen p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death J. Cell Biol. 171 2005 603 614
    • (2005) J. Cell Biol. , vol.171 , pp. 603-614
    • Bjorkoy, G.1    Lamark, T.2    Brech, A.3    Outzen, H.4    Perander, M.5    Overvatn, A.6    Stenmark, H.7    Johansen, T.8
  • 36
    • 35348886043 scopus 로고    scopus 로고
    • Physiological functions of Atg6/Beclin 1: A unique autophagy-related protein
    • Y. Cao, and D.J. Klionsky Physiological functions of Atg6/Beclin 1: a unique autophagy-related protein Cell Res. 17 2007 839 849
    • (2007) Cell Res. , vol.17 , pp. 839-849
    • Cao, Y.1    Klionsky, D.J.2
  • 38
    • 27544434763 scopus 로고    scopus 로고
    • Tumor suppressor HIC1 directly regulates SIRT1 to modulate p53-dependent DNA-damage responses
    • W.Y. Chen, D.H. Wang, R.C. Yen, J. Luo, W. Gu, and S.B. Baylin Tumor suppressor HIC1 directly regulates SIRT1 to modulate p53-dependent DNA-damage responses Cell 123 2005 437 448
    • (2005) Cell , vol.123 , pp. 437-448
    • Chen, W.Y.1    Wang, D.H.2    Yen, R.C.3    Luo, J.4    Gu, W.5    Baylin, S.B.6
  • 41
    • 53249121556 scopus 로고    scopus 로고
    • Sirtuins - novel therapeutic targets to treat age-associated diseases
    • S. Lavu, O. Boss, P.J. Elliott, and P.D. Lambert Sirtuins - novel therapeutic targets to treat age-associated diseases Nat. Rev. Drug Discov. 7 2008 841 853
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 841-853
    • Lavu, S.1    Boss, O.2    Elliott, P.J.3    Lambert, P.D.4
  • 43
    • 33845396682 scopus 로고    scopus 로고
    • SIRT1 interacts with p73 and suppresses p73-dependent transcriptional activity
    • J.M. Dai, Z.Y. Wang, D.C. Sun, R.X. Lin, and S.Q. Wang SIRT1 interacts with p73 and suppresses p73-dependent transcriptional activity J. Cell. Physiol. 210 2007 161 166
    • (2007) J. Cell. Physiol. , vol.210 , pp. 161-166
    • Dai, J.M.1    Wang, Z.Y.2    Sun, D.C.3    Lin, R.X.4    Wang, S.Q.5
  • 47
    • 28544451205 scopus 로고    scopus 로고
    • Control of multidrug resistance gene mdr1 and cancer resistance to chemotherapy by the longevity gene sirt1
    • F. Chu, P.M. Chou, X. Zheng, B.L. Mirkin, and A. Rebbaa Control of multidrug resistance gene mdr1 and cancer resistance to chemotherapy by the longevity gene sirt1 Cancer Res. 65 2005 10183 10187
    • (2005) Cancer Res. , vol.65 , pp. 10183-10187
    • Chu, F.1    Chou, P.M.2    Zheng, X.3    Mirkin, B.L.4    Rebbaa, A.5
  • 51
    • 77749306550 scopus 로고    scopus 로고
    • Harmonic oscillations in homeostatic controllers: Dynamics of the p53 regulatory system
    • I.W. Jolma, X.Y. Ni, L. Rensing, and P. Ruoff Harmonic oscillations in homeostatic controllers: dynamics of the p53 regulatory system Biophys. J. 98 2010 743 752
    • (2010) Biophys. J. , vol.98 , pp. 743-752
    • Jolma, I.W.1    Ni, X.Y.2    Rensing, L.3    Ruoff, P.4
  • 52
    • 34848886914 scopus 로고    scopus 로고
    • Autophagosome formation: Core machinery and adaptations
    • Z. Xie, and D.J. Klionsky Autophagosome formation: core machinery and adaptations Nat. Cell Biol. 9 2007 1102 1109
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1102-1109
    • Xie, Z.1    Klionsky, D.J.2
  • 53
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • N. Mizushima, B. Levine, A.M. Cuervo, and D.J. Klionsky Autophagy fights disease through cellular self-digestion Nature 451 2008 1069 1075
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 54
    • 1842583789 scopus 로고    scopus 로고
    • Development by self-digestion: Molecular mechanisms and biological functions of autophagy
    • B. Levine, and D.J. Klionsky Development by self-digestion: molecular mechanisms and biological functions of autophagy Dev. Cell 6 2004 463 477
    • (2004) Dev. Cell , vol.6 , pp. 463-477
    • Levine, B.1    Klionsky, D.J.2
  • 57
  • 58
    • 66849087488 scopus 로고    scopus 로고
    • A novel player in the p53-mediated autophagy: Sestrin2
    • M. D'Amelio, and F. Cecconi A novel player in the p53-mediated autophagy: Sestrin2 Cell Cycle 8 2009 1467
    • (2009) Cell Cycle , vol.8 , pp. 1467
    • D'amelio, M.1    Cecconi, F.2
  • 60
    • 79551521179 scopus 로고    scopus 로고
    • Disruption of a Sirt1-dependent autophagy checkpoint in the prostate results in prostatic intraepithelial neoplasia lesion formation
    • M.J. Powell, M.C. Casimiro, C. Cordon-Cardo, X. He, W.S. Yeow, C. Wang, P.A. McCue, M.W. McBurney, and R.G. Pestell Disruption of a Sirt1-dependent autophagy checkpoint in the prostate results in prostatic intraepithelial neoplasia lesion formation Cancer Res. 71 2011 964 975
    • (2011) Cancer Res. , vol.71 , pp. 964-975
    • Powell, M.J.1    Casimiro, M.C.2    Cordon-Cardo, C.3    He, X.4    Yeow, W.S.5    Wang, C.6    Mccue, P.A.7    Mcburney, M.W.8    Pestell, R.G.9
  • 61
    • 78650691023 scopus 로고    scopus 로고
    • Deacetylation of FoxO by Sirt1 plays an essential role in mediating starvation-induced autophagy in cardiac myocytes
    • N. Hariharan, Y. Maejima, J. Nakae, J. Paik, R.A. Depinho, and J. Sadoshima Deacetylation of FoxO by Sirt1 plays an essential role in mediating starvation-induced autophagy in cardiac myocytes Circ. Res. 107 2010 1470 1482
    • (2010) Circ. Res. , vol.107 , pp. 1470-1482
    • Hariharan, N.1    Maejima, Y.2    Nakae, J.3    Paik, J.4    Depinho, R.A.5    Sadoshima, J.6
  • 62
    • 67349273985 scopus 로고    scopus 로고
    • SIRT1: Regulation of longevity via autophagy
    • A. Salminen, and K. Kaarniranta SIRT1: regulation of longevity via autophagy Cell. Signal. 21 2009 1356 1360
    • (2009) Cell. Signal. , vol.21 , pp. 1356-1360
    • Salminen, A.1    Kaarniranta, K.2


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