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Volumn 14, Issue 1, 2014, Pages

Panobinostat synergizes with bortezomib to induce endoplasmic reticulum stress and ubiquitinated protein accumulation in renal cancer cells

Author keywords

Bortezomib; Combination therapy; Endoplasmic reticulum stress; Histone acetylation; Panobinostat; Renal cancer; Ubiquitinated protein

Indexed keywords

ALPHA TUBULIN; BORTEZOMIB; PANOBINOSTAT; ANTINEOPLASTIC AGENT; BORONIC ACID DERIVATIVE; HISTONE; HISTONE DEACETYLASE INHIBITOR; HYDROXAMIC ACID; INDOLE DERIVATIVE; PYRAZINE DERIVATIVE; UBIQUITINATED PROTEIN;

EID: 84925234997     PISSN: None     EISSN: 14712490     Source Type: Journal    
DOI: 10.1186/1471-2490-14-71     Document Type: Article
Times cited : (28)

References (23)
  • 1
    • 79960066445 scopus 로고    scopus 로고
    • Proteostasis regulation at the endoplasmic reticulum: A new perturbation site for targeted cancer therapy
    • Liu Y, Ye Y: Proteostasis regulation at the endoplasmic reticulum: A new perturbation site for targeted cancer therapy. Cell Res 2011, 21:867-883.
    • (2011) Cell Res , vol.21 , pp. 867-883
    • Liu, Y.1    Ye, Y.2
  • 2
    • 79952264011 scopus 로고    scopus 로고
    • Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress
    • Tabas I, Ron D: Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress. Nat Cell Biol 2011, 13:184-190.
    • (2011) Nat Cell Biol , vol.13 , pp. 184-190
    • Tabas, I.1    Ron, D.2
  • 3
    • 4444311881 scopus 로고    scopus 로고
    • Simultaneous inhibition of hsp 90 and the proteasome promotes protein ubiquitination, causes endoplasmic reticulum-derived cytosolic vacuolization, and enhances antitumor activity
    • Mimnaugh EG, Xu W, Vos M, Yuan X, Isaacs JS, Bisht KS, Gius D, Neckers L: Simultaneous inhibition of hsp 90 and the proteasome promotes protein ubiquitination, causes endoplasmic reticulum-derived cytosolic vacuolization, and enhances antitumor activity. Mol Cancer Ther 2004, 3:551-566.
    • (2004) Mol Cancer Ther , vol.3 , pp. 551-566
    • Mimnaugh, E.G.1    Xu, W.2    Vos, M.3    Yuan, X.4    Isaacs, J.S.5    Bisht, K.S.6    Gius, D.7    Neckers, L.8
  • 4
    • 22844432021 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: A novel basis for antileukemia activity of histone deacetylase inhibitors
    • Bali P, Pranpat M, Bradner J, Balasis M, Fiskus W, Guo F, Rocha K, Kumaraswamy S, Boyapalle S, Atadja P, Seto E, Bhalla K: Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: A novel basis for antileukemia activity of histone deacetylase inhibitors. J Biol Chem 2005, 280:26729-26734.
    • (2005) J Biol Chem , vol.280 , pp. 26729-26734
    • Bali, P.1    Pranpat, M.2    Bradner, J.3    Balasis, M.4    Fiskus, W.5    Guo, F.6    Rocha, K.7    Kumaraswamy, S.8    Boyapalle, S.9    Atadja, P.10    Seto, E.11    Bhalla, K.12
  • 5
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman MH, Ciechanover A: The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev 2002, 82:373-428.
    • (2002) Physiol Rev , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 9
    • 79960197509 scopus 로고    scopus 로고
    • A phase II trial of panobinostat, a histone deacetylase inhibitor, in the treatment of patients with refractory metastatic renal cell carcinoma
    • Hainsworth JD, Infante JR, Spigel DR, Arrowsmith ER, Boccia RV, Burris HA: A phase II trial of panobinostat, a histone deacetylase inhibitor, in the treatment of patients with refractory metastatic renal cell carcinoma. Cancer Invest 2011, 29:451-455.
    • (2011) Cancer Invest , vol.29 , pp. 451-455
    • Hainsworth, J.D.1    Infante, J.R.2    Spigel, D.R.3    Arrowsmith, E.R.4    Boccia, R.V.5    Burris, H.A.6
  • 10
    • 33744832401 scopus 로고    scopus 로고
    • United States food and drug administration approval summary: Bortezomib for the treatment of progressive multiple myeloma after one prior therapy
    • Kane RC, Farrell AT, Sridhara R, Pazdur R: United States Food and Drug Administration approval summary: bortezomib for the treatment of progressive multiple myeloma after one prior therapy. Clin Cancer Res 2006, 12:2955-2960.
    • (2006) Clin Cancer Res , vol.12 , pp. 2955-2960
    • Kane, R.C.1    Farrell, A.T.2    Sridhara, R.3    Pazdur, R.4
  • 13
    • 84859455667 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid (SAHA) combined with bortezomib inhibits renal cancer growth by enhancing histone acetylation and protein ubiquitination synergistically
    • Sato A, Asano T, Ito K, Sumitomo M, Asano T: Suberoylanilide hydroxamic acid (SAHA) combined with bortezomib inhibits renal cancer growth by enhancing histone acetylation and protein ubiquitination synergistically. BJU Int 2012, 109:1258-1268.
    • (2012) BJU Int , vol.109 , pp. 1258-1268
    • Sato, A.1    Asano, T.2    Ito, K.3    Sumitomo, M.4    Asano, T.5
  • 14
    • 0034716887 scopus 로고    scopus 로고
    • Tripartite management of unfolded proteins in the endoplasmic reticulum
    • Mori K: Tripartite management of unfolded proteins in the endoplasmic reticulum. Cell 2000, 101:451-454.
    • (2000) Cell , vol.101 , pp. 451-454
    • Mori, K.1
  • 15
    • 15944366885 scopus 로고    scopus 로고
    • The ER chaperone and signaling regulator GRP78/BiP as a monitor of endoplasmic reticulum stress
    • Lee AS: The ER chaperone and signaling regulator GRP78/BiP as a monitor of endoplasmic reticulum stress. Methods 2005, 35:373-381.
    • (2005) Methods , vol.35 , pp. 373-381
    • Lee, A.S.1
  • 16
    • 77955044180 scopus 로고    scopus 로고
    • HSP72 protects cells from ER stress-induced apoptosis via enhancement of IRE1alpha-XBP1 signaling through a physical interaction
    • Gupta S, Deepti A, Deegan S, Lisbona F, Hetz C, Samali A: HSP72 protects cells from ER stress-induced apoptosis via enhancement of IRE1alpha-XBP1 signaling through a physical interaction. PLoS Biol 2010, 8:e1000410.
    • (2010) PLoS Biol , vol.8 , pp. e1000410
    • Gupta, S.1    Deepti, A.2    Deegan, S.3    Lisbona, F.4    Hetz, C.5    Samali, A.6
  • 17
    • 0035890070 scopus 로고    scopus 로고
    • Manipulation of oxidative protein folding and PDI redox state in mammalian cells
    • Mezghrani A, Fassio A, Benham A, Simmen T, Braakman I, Sitia R: Manipulation of oxidative protein folding and PDI redox state in mammalian cells. EMBO J 2001, 20:6288-6296.
    • (2001) EMBO J , vol.20 , pp. 6288-6296
    • Mezghrani, A.1    Fassio, A.2    Benham, A.3    Simmen, T.4    Braakman, I.5    Sitia, R.6
  • 18
    • 0023720121 scopus 로고
    • Defective co-Translational formation of disulphide bonds in protein disulphide-isomerase-deficient microsomes
    • Bulleid NJ, Freedman RB: Defective co-Translational formation of disulphide bonds in protein disulphide-isomerase-deficient microsomes. Nature 1988, 335:649-651.
    • (1988) Nature , vol.335 , pp. 649-651
    • Bulleid, N.J.1    Freedman, R.B.2
  • 22
    • 84869082464 scopus 로고    scopus 로고
    • Vorinostat and bortezomib synergistically cause ubiquitinated protein accumulation in prostate cancer cells
    • Sato A, Asano T, Ito K, Asano T: Vorinostat and bortezomib synergistically cause ubiquitinated protein accumulation in prostate cancer cells. J Urol 2012, 188:2410-2418.
    • (2012) J Urol , vol.188 , pp. 2410-2418
    • Sato, A.1    Asano, T.2    Ito, K.3    Asano, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.