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Volumn 29, Issue 7-8 SPEC. ISS., 2004, Pages 509-514

The role of Hsp90 in cell response to hyperthermia

Author keywords

Apoptosis Necrosis; Cell signaling; Heat shock protein 90 (Hsp90); Human SKOV3 and primary ovarian carcinoma cells; Hyperthermia; Inhibitors of Hsp90

Indexed keywords

BETA CATENIN; EPIDERMAL GROWTH FACTOR RECEPTOR 2; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; MITOGEN ACTIVATED PROTEIN KINASE 1; NOVOBIOCIN;

EID: 4744359868     PISSN: 03064565     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jtherbio.2004.08.078     Document Type: Conference Paper
Times cited : (16)

References (31)
  • 1
    • 0035866397 scopus 로고    scopus 로고
    • Geldanamycin abrogates ErbB2 association with proteasome-resistant beta-catenin in melanoma cells, increases beta-catenin-E-cadherin association, and decreases beta-catenin-sensitive transcription
    • P. Bonvini, W.G. An, A. Rosolen, P. Nguyen, J. Trepel, A. Garcia de Herreros, M. Dunach, and L.M. Neckers Geldanamycin abrogates ErbB2 association with proteasome-resistant beta-catenin in melanoma cells, increases beta-catenin-E-cadherin association, and decreases beta-catenin-sensitive transcription Cancer Res. 61 2001 1671 1677
    • (2001) Cancer Res. , vol.61 , pp. 1671-1677
    • Bonvini, P.1    An, W.G.2    Rosolen, A.3    Nguyen, P.4    Trepel, J.5    Garcia De Herreros, A.6    Dunach, M.7    Neckers, L.M.8
  • 2
    • 1942485334 scopus 로고    scopus 로고
    • 17-(Allylamino)-17-demethoxygeldanamycin activity in human melanoma models
    • A.M. Burger, H.H. Fiebig, S.F. Stinson, and E.A. Sausville 17-(Allylamino)-17-demethoxygeldanamycin activity in human melanoma models Anticancer Drugs 15 2004 377 387
    • (2004) Anticancer Drugs , vol.15 , pp. 377-387
    • Burger, A.M.1    Fiebig, H.H.2    Stinson, S.F.3    Sausville, E.A.4
  • 3
    • 1942431966 scopus 로고    scopus 로고
    • The achilles heel of ErbB-2/HER2: Regulation by the Hsp90 chaperone machine and potential for pharmacological intervention
    • A. Citri, B.S. Kochupurakkal, and Y. Yarden The achilles heel of ErbB-2/HER2 regulation by the Hsp90 chaperone machine and potential for pharmacological intervention Cell Cycle 3 2004 51 60
    • (2004) Cell Cycle , vol.3 , pp. 51-60
    • Citri, A.1    Kochupurakkal, B.S.2    Yarden, Y.3
  • 4
    • 0034652115 scopus 로고    scopus 로고
    • Survival function of ERK1/2 as IL-3-activated, staurosporine-resistant Bcl2 kinases
    • X. Deng, P. Ruvalo, B. Carr, and W.S.J. May Survival function of ERK1/2 as IL-3-activated, staurosporine-resistant Bcl2 kinases Proc. Natl. Acad. Sci. USA 97 2000 1578 1583
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1578-1583
    • Deng, X.1    Ruvalo, P.2    Carr, B.3    May, W.S.J.4
  • 6
    • 0034903094 scopus 로고    scopus 로고
    • Aurintricarboxylic acid decreases proliferative potential of SKOV3 and MCF7 human carcinoma cells
    • V. Fraifeld, R. Seidman, O. Sagi, and M. Wolfson Aurintricarboxylic acid decreases proliferative potential of SKOV3 and MCF7 human carcinoma cells Anticancer Res. 21 2001 1975 1978
    • (2001) Anticancer Res. , vol.21 , pp. 1975-1978
    • Fraifeld, V.1    Seidman, R.2    Sagi, O.3    Wolfson, M.4
  • 7
    • 0036090023 scopus 로고    scopus 로고
    • Invited review: Interplay between molecular chaperones and signaling pathways in survival of heat shock
    • V.L. Gabai, and M.Y. Sherman Invited review interplay between molecular chaperones and signaling pathways in survival of heat shock J. Appl. Physiol. 92 2002 1743 1748
    • (2002) J. Appl. Physiol. , vol.92 , pp. 1743-1748
    • Gabai, V.L.1    Sherman, M.Y.2
  • 8
    • 0043237338 scopus 로고    scopus 로고
    • Intracellular HSP72 detection in HL60 cells using a flow cytometry system based on microfluidic analysis
    • E. Gottwald, B. Lahni, G. Ludke, T. Preckel, and C. Buhlmann Intracellular HSP72 detection in HL60 cells using a flow cytometry system based on microfluidic analysis Biotechniques 35 2003 358 367
    • (2003) Biotechniques , vol.35 , pp. 358-367
    • Gottwald, E.1    Lahni, B.2    Ludke, G.3    Preckel, T.4    Buhlmann, C.5
  • 10
    • 0026040203 scopus 로고
    • Inhibition of heat shock protein synthesis and protein glycosylation by stepdown heating
    • K.J. Henle, and W.A. Nagle Inhibition of heat shock protein synthesis and protein glycosylation by stepdown heating Exp. Cell Res. 196 1991 184 191
    • (1991) Exp. Cell Res. , vol.196 , pp. 184-191
    • Henle, K.J.1    Nagle, W.A.2
  • 11
    • 0034869582 scopus 로고    scopus 로고
    • Heat acclimation: Phenotypic plasticity and cues to the underlying molecular mechanisms
    • M. Horowitz Heat acclimation phenotypic plasticity and cues to the underlying molecular mechanisms J. Thermal Biol. 26 2001 357 363
    • (2001) J. Thermal Biol. , vol.26 , pp. 357-363
    • Horowitz, M.1
  • 12
    • 0036180660 scopus 로고    scopus 로고
    • From molecular and cellular to integrative heat defense during exposure to chronic heat
    • M. Horowitz From molecular and cellular to integrative heat defense during exposure to chronic heat Comp. Biochem. Physiol. A Mol. Integr. Physiol. 131 2002 475 483
    • (2002) Comp. Biochem. Physiol. a Mol. Integr. Physiol. , vol.131 , pp. 475-483
    • Horowitz, M.1
  • 13
    • 0035138956 scopus 로고    scopus 로고
    • The effects of KNK437, a novel inhibitor of heat shock protein synthesis, on the acquisition of thermotolerance in a murine transplantable tumor in vivo
    • M. Koishi, S. Yokota, T. Mae, Y. Nishimura, S. Kanamori, N. Horii, K. Shibuya, K. Sasai, and M. Hiraoka The effects of KNK437, a novel inhibitor of heat shock protein synthesis, on the acquisition of thermotolerance in a murine transplantable tumor in vivo Clin. Cancer Res. 7 2001 215 219
    • (2001) Clin. Cancer Res. , vol.7 , pp. 215-219
    • Koishi, M.1    Yokota, S.2    Mae, T.3    Nishimura, Y.4    Kanamori, S.5    Horii, N.6    Shibuya, K.7    Sasai, K.8    Hiraoka, M.9
  • 14
    • 0034711270 scopus 로고    scopus 로고
    • The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone
    • M.G. Marcu, A. Chadli, I. Bouhouche, M. Catelli, and L.M. Neckers The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone J. Biol. Chem. 275 2000 37181 37186
    • (2000) J. Biol. Chem. , vol.275 , pp. 37181-37186
    • Marcu, M.G.1    Chadli, A.2    Bouhouche, I.3    Catelli, M.4    Neckers, L.M.5
  • 15
    • 0031852375 scopus 로고    scopus 로고
    • Role of the heat-shock response in the life and death of proteins
    • A. Mathew, and R.I. Morimoto Role of the heat-shock response in the life and death of proteins Ann. NY Acad. Sci. 851 1998 99 111
    • (1998) Ann. NY Acad. Sci. , vol.851 , pp. 99-111
    • Mathew, A.1    Morimoto, R.I.2
  • 17
    • 0035313040 scopus 로고    scopus 로고
    • Lipopolysaccharide activates Akt in human alveolar macrophages resulting in nuclear accumulation and transcriptional activity of β-catenin
    • M.M. Monick, A.B. Carter, P.K. Robeff, D.M. Flaherty, M.W. Peterson, and G.W. Hunninghake Lipopolysaccharide activates Akt in human alveolar macrophages resulting in nuclear accumulation and transcriptional activity of β-catenin J. Immunol. 166 2001 4713 4720
    • (2001) J. Immunol. , vol.166 , pp. 4713-4720
    • Monick, M.M.1    Carter, A.B.2    Robeff, P.K.3    Flaherty, D.M.4    Peterson, M.W.5    Hunninghake, G.W.6
  • 19
    • 0037099046 scopus 로고    scopus 로고
    • Chaperoning signaling pathways: Molecular chaperones as stress-sensing 'heat shock' proteins
    • E.A. Nollen, and R.I. Morimoto Chaperoning signaling pathways molecular chaperones as stress-sensing 'heat shock' proteins J. Cell Sci. 115 2002 2809 2816
    • (2002) J. Cell Sci. , vol.115 , pp. 2809-2816
    • Nollen, E.A.1    Morimoto, R.I.2
  • 20
    • 85047682789 scopus 로고    scopus 로고
    • Taxol-induced apoptosis in human SKOV3 ovarian and MCF7 breast carcinoma cells is caspase-3 and caspase-9 independent
    • R. Ofir, R. Seidman, T. Rabinski, M. Krup, V. Yavelsky, Y. Weinstein, and M. Wolfson Taxol-induced apoptosis in human SKOV3 ovarian and MCF7 breast carcinoma cells is caspase-3 and caspase-9 independent Cell Death Differ. 9 2002 636 642
    • (2002) Cell Death Differ. , vol.9 , pp. 636-642
    • Ofir, R.1    Seidman, R.2    Rabinski, T.3    Krup, M.4    Yavelsky, V.5    Weinstein, Y.6    Wolfson, M.7
  • 21
    • 0004565467 scopus 로고
    • Hyperthermia
    • V.T. DeVita Jr. S. Hellman S.A. Rosenberg J.B. Lippincott Company Philadelphia
    • J.R. Oleson Hyperthermia V.T. DeVita Jr. S. Hellman S.A. Rosenberg Cancer Principles and Practice of Oncology 1993 J.B. Lippincott Company Philadelphia 2725 2733
    • (1993) Cancer: Principles and Practice of Oncology , pp. 2725-2733
    • Oleson, J.R.1
  • 22
    • 0030982641 scopus 로고    scopus 로고
    • The role of the hsp90-based chaperone system in signal transduction by nuclear receptors and receptors signaling via MAP kinase
    • W.B. Pratt The role of the hsp90-based chaperone system in signal transduction by nuclear receptors and receptors signaling via MAP kinase Annu. Rev. Pharmacol. Toxicol. 37 1997 297 326
    • (1997) Annu. Rev. Pharmacol. Toxicol. , vol.37 , pp. 297-326
    • Pratt, W.B.1
  • 23
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • W.B. Pratt, and D.O. Toft Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery Exp. Biol. Med. (Maywood) 228 2003 111 133
    • (2003) Exp. Biol. Med. (Maywood) , vol.228 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 25
    • 0036339108 scopus 로고    scopus 로고
    • ErbB2 overexpression in an ovarian cancer cell line confers sensitivity to the HSP90 inhibitor geldanamycin
    • V. Smith, S. Hobbs, W. Court, S. Eccles, P. Workman, and L.R. Kelland ErbB2 overexpression in an ovarian cancer cell line confers sensitivity to the HSP90 inhibitor geldanamycin Anticancer Res. 22 2002 1993 1999
    • (2002) Anticancer Res. , vol.22 , pp. 1993-1999
    • Smith, V.1    Hobbs, S.2    Court, W.3    Eccles, S.4    Workman, P.5    Kelland, L.R.6
  • 26
    • 0033119801 scopus 로고    scopus 로고
    • Beta-catenin regulates expression of cyclin D1 in colon carcinoma cells
    • O. Tetsu, and F. McCormick Beta-catenin regulates expression of cyclin D1 in colon carcinoma cells Nature 398 1999 422 426
    • (1999) Nature , vol.398 , pp. 422-426
    • Tetsu, O.1    McCormick, F.2
  • 27
    • 0037458627 scopus 로고    scopus 로고
    • Disruption of HSP90 function reverts tumor necrosis factor-induced necrosis to apoptosis
    • T. Vanden Berghe, M. Kalai, G. van Loo, W. Declercq, and P. Vandenabeele Disruption of HSP90 function reverts tumor necrosis factor-induced necrosis to apoptosis J. Biol. Chem. 278 2003 5622 5629
    • (2003) J. Biol. Chem. , vol.278 , pp. 5622-5629
    • Vanden Berghe, T.1    Kalai, M.2    Van Loo, G.3    Declercq, W.4    Vandenabeele, P.5
  • 28
    • 0028823892 scopus 로고
    • Mitogen and stress response pathways: MAP kinase cascades and phosphatase regulation in mammals and yeast
    • A.J. Waskiewicz, and J.A. Cooper Mitogen and stress response pathways MAP kinase cascades and phosphatase regulation in mammals and yeast Curr. Opin. Cell Biol. 7 1995 798 805
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 798-805
    • Waskiewicz, A.J.1    Cooper, J.A.2
  • 29
    • 0033567869 scopus 로고    scopus 로고
    • An essential role for mitogen-activated protein kinases, ERKs, in preventing heat-induced cell death
    • W. Woessmann, Y.H. Meng, and N.F. Mivechi An essential role for mitogen-activated protein kinases, ERKs, in preventing heat-induced cell death J. Cell Biochem. 74 1999 648 662
    • (1999) J. Cell Biochem. , vol.74 , pp. 648-662
    • Woessmann, W.1    Meng, Y.H.2    Mivechi, N.F.3
  • 30
    • 1142273472 scopus 로고    scopus 로고
    • Altered states: Selectively drugging the Hsp90 cancer chaperone
    • P. Workman Altered states selectively drugging the Hsp90 cancer chaperone Trends Mol. Med. 10 2004 47 51
    • (2004) Trends Mol. Med. , vol.10 , pp. 47-51
    • Workman, P.1
  • 31
    • 0037908648 scopus 로고    scopus 로고
    • Inactivation of dual-specificity phosphatases is involved in the regulation of extracellular signal-regulated kinases by heat shock and hsp72
    • J. Yaglom, C. O'Callaghan-Sunol, V. Gabai, and M.Y. Sherman Inactivation of dual-specificity phosphatases is involved in the regulation of extracellular signal-regulated kinases by heat shock and hsp72 Mol. Cell. Biol. 23 2003 3813 3824
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 3813-3824
    • Yaglom, J.1    O'Callaghan-Sunol, C.2    Gabai, V.3    Sherman, M.Y.4


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