메뉴 건너뛰기




Volumn 5, Issue , 2015, Pages

Nelfinavir and nelfinavir analogs block site-2 protease cleavage to inhibit castration-resistant prostate cancer

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 6; ATF6 PROTEIN, HUMAN; MBTPS2 PROTEIN, HUMAN; METALLOPROTEINASE; NELFINAVIR; PROTEIN BCL 2; PROTEIN PRECURSOR; RNA; SREBF1 PROTEIN, HUMAN; STEROL REGULATORY ELEMENT BINDING PROTEIN 1; TRANSCRIPTOME;

EID: 84928028956     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep09698     Document Type: Article
Times cited : (52)

References (31)
  • 1
    • 85028107326 scopus 로고    scopus 로고
    • Drug resistance in metastatic castrationresistant prostate cancer
    • Seruga, B., Ocana, A. & Tannock, I. F. Drug resistance in metastatic castrationresistant prostate cancer. Nat Rev Clin Oncol 8, 12-23 (2011).
    • (2011) Nat Rev Clin Oncol , vol.8 , pp. 12-23
    • Seruga, B.1    Ocana, A.2    Tannock, I.F.3
  • 2
    • 79957443342 scopus 로고    scopus 로고
    • Abiraterone and increased survival in metastatic prostate cancer
    • De Bono, J. S. et al. Abiraterone and increased survival in metastatic prostate cancer. N Engl J Med 364, 1995-2005 (2011).
    • (2011) N Engl J Med , vol.364 , pp. 1995-2005
    • De Bono, J.S.1
  • 3
    • 84866770294 scopus 로고    scopus 로고
    • Increased survival with enzalutamide in prostate cancer after chemotherapy
    • Scher, H. I. et al. Increased survival with enzalutamide in prostate cancer after chemotherapy. N Engl J Med 367, 1187-1197 (2012).
    • (2012) N Engl J Med , vol.367 , pp. 1187-1197
    • Scher, H.I.1
  • 4
    • 84866752804 scopus 로고    scopus 로고
    • Enzalutamide-A major advance in the treatment of metastatic prostate cancer
    • Vogelzang, N. J. Enzalutamide-A major advance in the treatment of metastatic prostate cancer. N Engl J Med 367, 1256-1257 (2012).
    • (2012) N Engl J Med , vol.367 , pp. 1256-1257
    • Vogelzang, N.J.1
  • 5
    • 34748912615 scopus 로고    scopus 로고
    • Fatty acid synthase and the lipogenic phenotype in cancer pathogenesis
    • Menendez, J. A. & Lupu, R. Fatty acid synthase and the lipogenic phenotype in cancer pathogenesis. Nat Rev Cancer 7, 763-777 (2007).
    • (2007) Nat Rev Cancer , vol.7 , pp. 763-777
    • Menendez, J.A.1    Lupu, R.2
  • 6
    • 0030941803 scopus 로고    scopus 로고
    • The SREBP pathway: Regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor
    • Brown, M. S. & Goldstein, J. L. The SREBP pathway: Regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor. Cell 89, 331-340 (1997).
    • (1997) Cell , vol.89 , pp. 331-340
    • Brown, M.S.1    Goldstein, J.L.2
  • 7
    • 33749356751 scopus 로고    scopus 로고
    • Androgen activation of the sterol regulatory element-binding protein pathway: Current insights
    • Heemers, H. V., Verhoeven, G. & Swinnen, J. V. Androgen activation of the sterol regulatory element-binding protein pathway: Current insights. Mol Endocrinol 20, 2265-2277 (2006).
    • (2006) Mol Endocrinol , vol.20 , pp. 2265-2277
    • Heemers, H.V.1    Verhoeven, G.2    Swinnen, J.V.3
  • 8
    • 0030298339 scopus 로고    scopus 로고
    • Sterol resistance in CHO cells traced to point mutation in SREBP cleavage-activating protein
    • Hua, X., Nohturfft, A., Goldstein, J. L. & Brown, M. S. Sterol resistance in CHO cells traced to point mutation in SREBP cleavage-activating protein. Cell 87, 415-426 (1996).
    • (1996) Cell , vol.87 , pp. 415-426
    • Hua, X.1    Nohturfft, A.2    Goldstein, J.L.3    Brown, M.S.4
  • 9
    • 0032489460 scopus 로고    scopus 로고
    • Cleavage of sterol regulatory element-binding proteins (SREBPs) at site-1 requires interaction with SREBP cleavage-activating protein. Evidence from in vivo competition studies
    • Sakai, J., Nohturfft, A.,Goldstein, J. L.&Brown, M. S. Cleavage of sterol regulatory element-binding proteins (SREBPs) at site-1 requires interaction with SREBP cleavage-activating protein. Evidence from in vivo competition studies. J Biol Chem 273, 5785-5793 (1998).
    • (1998) J Biol Chem , vol.273 , pp. 5785-5793
    • Sakai, J.1    Nohturfft, A.2    Goldstein, J.L.3    Brown, M.S.4
  • 10
    • 0037162719 scopus 로고    scopus 로고
    • Crucial step in cholesterol homeostasis: Sterols promote binding of SCAP to INSIG-1, amembrane protein that facilitates retention of SREBPs in ER
    • Yang, T. et al. Crucial step in cholesterol homeostasis: Sterols promote binding of SCAP to INSIG-1, amembrane protein that facilitates retention of SREBPs in ER. Cell 110, 489-500 (2002).
    • (2002) Cell , vol.110 , pp. 489-500
    • Yang, T.1
  • 11
    • 0034681260 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis: A control mechanism conserved from bacteria to humans
    • Brown, M. S., Ye, J., Rawson, R. B. & Goldstein, J. L. Regulated intramembrane proteolysis: A control mechanism conserved from bacteria to humans. Cell 100, 391-398 (2000).
    • (2000) Cell , vol.100 , pp. 391-398
    • Brown, M.S.1    Ye, J.2    Rawson, R.B.3    Goldstein, J.L.4
  • 12
    • 0030911517 scopus 로고    scopus 로고
    • Cleavage site for sterolregulated protease localized to a leu-Ser bond in the lumenal loop of sterol regulatory element-binding protein-2
    • Duncan, E. A., Brown, M. S., Goldstein, J. L. & Sakai, J. Cleavage site for sterolregulated protease localized to a leu-Ser bond in the lumenal loop of sterol regulatory element-binding protein-2. J Biol Chem 272, 12778-12785 (1997).
    • (1997) J Biol Chem , vol.272 , pp. 12778-12785
    • Duncan, E.A.1    Brown, M.S.2    Goldstein, J.L.3    Sakai, J.4
  • 13
    • 0031301274 scopus 로고    scopus 로고
    • Complementation cloning of S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs
    • Rawson, R. B. et al. Complementation cloning of S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs. Mol Cell 1, 47-57 (1997).
    • (1997) Mol Cell , vol.1 , pp. 47-57
    • Rawson, R.B.1
  • 14
    • 0043172415 scopus 로고    scopus 로고
    • The SREBP pathway-insights from Insigs and insects
    • Rawson, R. B. The SREBP pathway-insights from Insigs and insects. Nat Rev Mol Cell Biol 4, 631-640 (2003).
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 631-640
    • Rawson, R.B.1
  • 15
    • 34548189283 scopus 로고    scopus 로고
    • ATF6alpha optimizes long-term endoplasmic reticulum function to protect cells from chronic stress
    • Wu, J. et al. ATF6alpha optimizes long-term endoplasmic reticulum function to protect cells from chronic stress. Dev Cell 13, 351-364 (2007).
    • (2007) Dev Cell , vol.13 , pp. 351-364
    • Wu, J.1
  • 16
    • 57749170528 scopus 로고    scopus 로고
    • Anti-HIV drugs for cancer therapeutics: Back to the future? the Lancet
    • Chow,W. A., Jiang, C. & Guan, M. Anti-HIV drugs for cancer therapeutics: Back to the future? The Lancet. Oncology 10, 61-71 (2009).
    • (2009) Oncology , vol.10 , pp. 61-71
    • Chow, W.A.1    Jiang, C.2    Guan, M.3
  • 17
    • 33845603151 scopus 로고    scopus 로고
    • NFV, an HIV-1 protease inhibitor, induces growth arrest, reduced Akt signalling, apoptosis and docetaxel sensitisation in NSCLC cell lines
    • Yang, Y. et al. NFV, an HIV-1 protease inhibitor, induces growth arrest, reduced Akt signalling, apoptosis and docetaxel sensitisation in NSCLC cell lines. Br J Cancer 95, 1653-1662 (2006).
    • (2006) Br J Cancer , vol.95 , pp. 1653-1662
    • Yang, Y.1
  • 18
    • 33749472340 scopus 로고    scopus 로고
    • Nelfinavir down-regulates hypoxia-inducible factor 1alpha and VEGF expression and increases tumor oxygenation: Implications for radiotherapy
    • Pore, N. et al. Nelfinavir down-regulates hypoxia-inducible factor 1alpha and VEGF expression and increases tumor oxygenation: Implications for radiotherapy. Cancer research 66, 9252-9259 (2006).
    • (2006) Cancer Research , vol.66 , pp. 9252-9259
    • Pore, N.1
  • 19
    • 34249304804 scopus 로고    scopus 로고
    • Phosphatase and tensin homologue deficiency in glioblastoma confers resistance to radiation and temozolomide that is reversed by the protease inhibitor nelfinavir
    • Jiang, Z. et al. Phosphatase and tensin homologue deficiency in glioblastoma confers resistance to radiation and temozolomide that is reversed by the protease inhibitor nelfinavir. Cancer research 67, 4467-4473 (2007).
    • (2007) Cancer Research , vol.67 , pp. 4467-4473
    • Jiang, Z.1
  • 20
    • 23844434338 scopus 로고    scopus 로고
    • HIV-1 protease inhibitor induces growth arrest and apoptosis of human prostate cancer LNCaP cells in vitro and in vivo in conjunction with blockade of androgen receptor STAT3 and AKT signaling
    • Yang, Y. et al. HIV-1 protease inhibitor induces growth arrest and apoptosis of human prostate cancer LNCaP cells in vitro and in vivo in conjunction with blockade of androgen receptor STAT3 and AKT signaling. Cancer Sci 96, 425-433 (2005).
    • (2005) Cancer Sci , vol.96 , pp. 425-433
    • Yang, Y.1
  • 21
    • 33847064335 scopus 로고    scopus 로고
    • HIV protease inhibitor nelfinavir inhibits growth of human melanoma cells by induction of cell cycle arrest
    • Jiang, W. et al. HIV protease inhibitor nelfinavir inhibits growth of human melanoma cells by induction of cell cycle arrest. Cancer research 67, 1221-1227 (2007).
    • (2007) Cancer Research , vol.67 , pp. 1221-1227
    • Jiang, W.1
  • 22
    • 84867719417 scopus 로고    scopus 로고
    • Selective inhibition of HER2-positive breast cancer cells by the HIV protease inhibitor nelfinavir
    • Shim, J. S. et al. Selective inhibition of HER2-positive breast cancer cells by the HIV protease inhibitor nelfinavir. J Natl Cancer Inst 104, 1576-1590 (2012).
    • (2012) J Natl Cancer Inst , vol.104 , pp. 1576-1590
    • Shim, J.S.1
  • 23
    • 79955562721 scopus 로고    scopus 로고
    • Drug discovery using chemical systems biology: Weak inhibition of multiple kinases may contribute to the anticancer effect of nelfinavir
    • Xie, L., Evangelidis, T., Xie, L. & Bourne, P. E. Drug discovery using chemical systems biology: Weak inhibition of multiple kinases may contribute to the anticancer effect of nelfinavir. PLoS Comput Biol 7, e1002037 (2011).
    • (2011) PLoS Comput Biol , vol.7 , pp. e1002037
    • Xie, L.1    Evangelidis, T.2    Xie, L.3    Bourne, P.E.4
  • 24
    • 84862580422 scopus 로고    scopus 로고
    • Nelfinavir inhibits regulated intramembrane proteolysis of sterol regulatory element binding protein-1 and activating transcription factor 6 in castration-resistant prostate cancer
    • Guan, M., Fousek, K. & Chow,W. A.Nelfinavir inhibits regulated intramembrane proteolysis of sterol regulatory element binding protein-1 and activating transcription factor 6 in castration-resistant prostate cancer. The FEBS journal 279, 2399-2411 (2012).
    • (2012) The FEBS Journal , vol.279 , pp. 2399-2411
    • Guan, M.1    Fousek, K.2    Chow, W.A.3
  • 25
    • 36849037428 scopus 로고    scopus 로고
    • Structure of a site-2 protease family intramembrane metalloprotease
    • Feng, L. et al. Structure of a site-2 protease family intramembrane metalloprotease. Science 318, 1608-1612 (2007).
    • (2007) Science , vol.318 , pp. 1608-1612
    • Feng, L.1
  • 26
    • 65449136284 scopus 로고    scopus 로고
    • TopHat: Discovering splice junctions with RNA-Seq
    • Trapnell, C., Pachter, L.&Salzberg, S. L. TopHat: Discovering splice junctions with RNA-Seq. Bioinformatics 25, 1105-1111 (2009).
    • (2009) Bioinformatics , vol.25 , pp. 1105-1111
    • Trapnell, C.1    Pachter, L.2    Salzberg, S.L.3
  • 27
    • 0037150534 scopus 로고    scopus 로고
    • Biochemistry Intramembrane proteases-mixing oil and water
    • Wolfe, M. S. & Selkoe, D. J. Biochemistry. Intramembrane proteases-mixing oil and water. Science 296, 2156-2157 (2002).
    • (2002) Science , vol.296 , pp. 2156-2157
    • Wolfe, M.S.1    Selkoe, D.J.2
  • 28
    • 34548063171 scopus 로고    scopus 로고
    • HIV protease inhibitors block the zinc metalloproteinase ZMPSTE24 and lead to an accumulation of prelamin A in cells
    • Coffinier, C. et al. HIV protease inhibitors block the zinc metalloproteinase ZMPSTE24 and lead to an accumulation of prelamin A in cells. Proc Natl Acad Sci U S A 104, 13432-13437 (2007).
    • (2007) Proc Natl Acad Sci U.S.A. , vol.104 , pp. 13432-13437
    • Coffinier, C.1
  • 29
    • 35348814977 scopus 로고    scopus 로고
    • HIV protease inhibitors and nuclear lamin processing: Getting the right bells and whistles
    • Clarke, S. G. HIV protease inhibitors and nuclear lamin processing: Getting the right bells and whistles. Proc Natl Acad Sci U S A 104, 13857-13858 (2007).
    • (2007) Proc Natl Acad Sci U.S.A. , vol.104 , pp. 13857-13858
    • Clarke, S.G.1
  • 30
    • 64149125961 scopus 로고    scopus 로고
    • IFAP syndrome is caused by deficiency in MBTPS2, an intramembrane zinc metalloprotease essential for cholesterol homeostasis and ER stress response
    • Oeffner, F. et al. IFAP syndrome is caused by deficiency in MBTPS2, an intramembrane zinc metalloprotease essential for cholesterol homeostasis and ER stress response. Am J Hum Genet 84, 459-467 (2009).
    • (2009) Am J Hum Genet , vol.84 , pp. 459-467
    • Oeffner, F.1
  • 31
    • 0034613175 scopus 로고    scopus 로고
    • Promoter analysis of the mouse sterol regulatory element-binding protein-1c gene
    • Amemiya-Kudo, M. et al. Promoter analysis of the mouse sterol regulatory element-binding protein-1c gene. J Biol Chem 275, 31078-31085 (2000).
    • (2000) J Biol Chem , vol.275 , pp. 31078-31085
    • Amemiya-Kudo, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.