메뉴 건너뛰기




Volumn 21, Issue 11, 2004, Pages 1085-1089

A drastic reduction in the basal level of heat-shock protein 90 in the brain of goldfish (Carassius auratus) after administration of geldanamycin

Author keywords

Brain; Geldanamycin; Goldfish; Heat shock; Heat shock protein

Indexed keywords

BENZOQUINONE DERIVATIVE; CHAPERONE; GELDANAMYCIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 72; HEAT SHOCK PROTEIN 90; HYDROCORTISONE; MACROCYCLIC LACTAM; QUINONE DERIVATIVE;

EID: 10944223838     PISSN: 02890003     EISSN: None     Source Type: Journal    
DOI: 10.2108/zsj.21.1085     Document Type: Article
Times cited : (8)

References (22)
  • 1
    • 0034777916 scopus 로고    scopus 로고
    • Destabilization of steroid receptors by heat shock protein 90-binding drugs: A ligand-independent approach to hormonal therapy of breast cancer
    • Bagatell R, Khan O, Paine-Murrieta G, Taylor CW, Akinaga S, Whitesell L (2001) Destabilization of steroid receptors by heat shock protein 90-binding drugs: A ligand-independent approach to hormonal therapy of breast cancer. Clin Cancer Res 7: 2076-2084
    • (2001) Clin Cancer Res , vol.7 , pp. 2076-2084
    • Bagatell, R.1    Khan, O.2    Paine-Murrieta, G.3    Taylor, C.W.4    Akinaga, S.5    Whitesell, L.6
  • 2
    • 0017184389 scopus 로고
    • A rapid sensitive method for the quantities of protein utilizing the principle of protein-dry binding
    • Bradford MM (1976) A rapid sensitive method for the quantities of protein utilizing the principle of protein-dry binding. Analyt Biochem 72: 248-254
    • (1976) Analyt Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0031193541 scopus 로고    scopus 로고
    • Induction of heat shock proteins by tyrosine kinase inhibitors in rat cardiomyocytes and myogenic cells confers protection against stimulated ischemia
    • Conde AG, Lau SS, Dillmann WH, Mestril R (1997) Induction of heat shock proteins by tyrosine kinase inhibitors in rat cardiomyocytes and myogenic cells confers protection against stimulated ischemia. J Mol Cell Cardiol 29: 1927-1938
    • (1997) J Mol Cell Cardiol , vol.29 , pp. 1927-1938
    • Conde, A.G.1    Lau, S.S.2    Dillmann, W.H.3    Mestril, R.4
  • 5
    • 0027969323 scopus 로고
    • Proof that Hsp70 is required for assembly of the glucocorticoid receptor into a heterocomplex with Hsp90
    • Hutchison KA, Dittmar KD, Czar MJ, Pratt WB (1994) Proof that Hsp70 is required for assembly of the glucocorticoid receptor into a heterocomplex with Hsp90. J Biol Chem 267: 5043-5049
    • (1994) J Biol Chem , vol.267 , pp. 5043-5049
    • Hutchison, K.A.1    Dittmar, K.D.2    Czar, M.J.3    Pratt, W.B.4
  • 6
    • 0000286857 scopus 로고    scopus 로고
    • Enhanced expression of stress protein 70 in the brains of goldfish, Carassius auratus, reared with bluegills, Lepomis macrochirus
    • Kagawa N, Ryo K, Mugiya Y (1999) Enhanced expression of stress protein 70 in the brains of goldfish, Carassius auratus, reared with bluegills, Lepomis macrochirus. Fish Physiol Biochem 21: 103-110
    • (1999) Fish Physiol Biochem , vol.21 , pp. 103-110
    • Kagawa, N.1    Ryo, K.2    Mugiya, Y.3
  • 7
    • 0034310262 scopus 로고    scopus 로고
    • Exposure of goldfish (Carassius auratus) to bluegills (Lepomis macrochirus) enhances expression of stress protein 70 mRNA in the brains and increases plasma cortisol levels
    • Kagawa N, Mugiya Y (2000) Exposure of goldfish (Carassius auratus) to bluegills (Lepomis macrochirus) enhances expression of stress protein 70 mRNA in the brains and increases plasma cortisol levels. Zool Sci 17: 1061-1066
    • (2000) Zool Sci , vol.17 , pp. 1061-1066
    • Kagawa, N.1    Mugiya, Y.2
  • 8
    • 0036629862 scopus 로고    scopus 로고
    • Brain HSP70 mRNA expression is linked with plasma cortisol levels in goldfish (Carassius auratus) exposed to a potential predator
    • Kagawa N, Mugiya Y (2002) Brain HSP70 mRNA expression is linked with plasma cortisol levels in goldfish (Carassius auratus) exposed to a potential predator. Zool Sci 19: 735-740
    • (2002) Zool Sci , vol.19 , pp. 735-740
    • Kagawa, N.1    Mugiya, Y.2
  • 9
    • 0035010054 scopus 로고    scopus 로고
    • Heat-shock factor-1, steroid hormones, and regulation of heat-shock protein expression in the heart
    • Knowlton AA, Sun L (2001) Heat-shock factor-1, steroid hormones, and regulation of heat-shock protein expression in the heart. Am J Physiol 280: H455-H464
    • (2001) Am J Physiol , vol.280
    • Knowlton, A.A.1    Sun, L.2
  • 10
    • 0035815652 scopus 로고    scopus 로고
    • Regulation of the atrial natriuretic peptide receptor by heat shock protein 90 complexes
    • Kumar R, Grammatikakis N, Chinkers M (2001) Regulation of the atrial natriuretic peptide receptor by heat shock protein 90 complexes. J Biol Chem 276: 11371-11375
    • (2001) J Biol Chem , vol.276 , pp. 11371-11375
    • Kumar, R.1    Grammatikakis, N.2    Chinkers, M.3
  • 11
    • 0036319568 scopus 로고    scopus 로고
    • Geldanamycin induces heat shock proteins in brain and protects against focal cerebral ischemia
    • Lu A, Ran R, Parmentier-Batteur S, Nee A, Sharp FR (2002) Geldanamycin induces heat shock proteins in brain and protects against focal cerebral ischemia. J Neurochem 81: 355-364
    • (2002) J Neurochem , vol.81 , pp. 355-364
    • Lu, A.1    Ran, R.2    Parmentier-Batteur, S.3    Nee, A.4    Sharp, F.R.5
  • 12
    • 0027135501 scopus 로고
    • The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins
    • Parsell DA, Lindquist S (1993) The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins. Annu Rev Genet 27: 437-496
    • (1993) Annu Rev Genet , vol.27 , pp. 437-496
    • Parsell, D.A.1    Lindquist, S.2
  • 13
    • 0027451956 scopus 로고
    • The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor
    • Pratt WB (1993) The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor. J Biol Chem 268: 21455-21458
    • (1993) J Biol Chem , vol.268 , pp. 21455-21458
    • Pratt, W.B.1
  • 15
    • 0032569851 scopus 로고    scopus 로고
    • Hsp90 as a capacitor for morphological evolution
    • Rutherford S, Lindquist S (1998) Hsp90 as a capacitor for morphological evolution. Nature 396: 336-342
    • (1998) Nature , vol.396 , pp. 336-342
    • Rutherford, S.1    Lindquist, S.2
  • 16
    • 0028786332 scopus 로고
    • Disruption of the raf-1-Hsp90 molecular complex results in destabilization of raf-1 and loss of raf-1-ras association
    • Schulte TW, Blagosklonny MV, Ingui C, Neckers L (1995) Disruption of the raf-1-Hsp90 molecular complex results in destabilization of raf-1 and loss of raf-1-ras association. J Biol Chem 270: 24585-24588
    • (1995) J Biol Chem , vol.270 , pp. 24585-24588
    • Schulte, T.W.1    Blagosklonny, M.V.2    Ingui, C.3    Neckers, L.4
  • 17
    • 0035363805 scopus 로고    scopus 로고
    • Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Hutingson's disease
    • Sittler A, Lurz R, Lueder G, Priller J, Hayer-Hartl MK, Hartl FU, Lehrach H, Wanker EE (2001) Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Hutingson's disease. Hum Mol Genet 10: 1307-1315
    • (2001) Hum Mol Genet , vol.10 , pp. 1307-1315
    • Sittler, A.1    Lurz, R.2    Lueder, G.3    Priller, J.4    Hayer-Hartl, M.K.5    Hartl, F.U.6    Lehrach, H.7    Wanker, E.E.8
  • 18
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
    • Stebbins CE, Russo AA, Schneider C, Rosen N, Hartl FU, Pavletich NP (1997) Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell 89: 239-250
    • (1997) Cell , vol.89 , pp. 239-250
    • Stebbins, C.E.1    Russo, A.A.2    Schneider, C.3    Rosen, N.4    Hartl, F.U.5    Pavletich, N.P.6
  • 19
    • 0028064940 scopus 로고
    • v-src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation
    • v-src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation. Proc Natl Acad Sci USA 91: 8324-8328
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    De Costa, B.3    Myers, C.E.4    Neckers, L.M.5
  • 20
    • 0029973294 scopus 로고    scopus 로고
    • Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells
    • Whitesell L, Cook P (1996) Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells. Mol Endocrinol 10: 705-712
    • (1996) Mol Endocrinol , vol.10 , pp. 705-712
    • Whitesell, L.1    Cook, P.2
  • 22
    • 0032555685 scopus 로고    scopus 로고
    • Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1
    • Zou J, Guo Y, Guettouche T, Smith DF, Voellmy R (1998) Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. Cell 94: 471-480
    • (1998) Cell , vol.94 , pp. 471-480
    • Zou, J.1    Guo, Y.2    Guettouche, T.3    Smith, D.F.4    Voellmy, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.