메뉴 건너뛰기




Volumn 88, Issue 7, 2003, Pages 3346-3353

The heat shock protein 90-binding geldanamycin inhibits cancer cell proliferation, down-regulates oncoproteins, and inhibits epidermal growth factor-induced invasion in thyroid cancer cell lines

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR; EPIDERMAL GROWTH FACTOR RECEPTOR; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; ONCOPROTEIN; PROTEIN P53; RAF PROTEIN; RAF1 PROTEIN; UNCLASSIFIED DRUG;

EID: 0038637205     PISSN: 0021972X     EISSN: None     Source Type: Journal    
DOI: 10.1210/jc.2002-020340     Document Type: Article
Times cited : (57)

References (50)
  • 1
    • 0032535770 scopus 로고    scopus 로고
    • A National Cancer Data Base report on 53, 856 cases of thyroid carcinoma treated in the U.S., 1985-1995
    • Hundahl SA, Fleming ID, Fremgen AM, Menck HR 1998 A National Cancer Data Base report on 53, 856 cases of thyroid carcinoma treated in the U.S., 1985-1995. Cancer 83:2638-2648
    • (1998) Cancer , vol.83 , pp. 2638-2648
    • Hundahl, S.A.1    Fleming, I.D.2    Fremgen, A.M.3    Menck, H.R.4
  • 2
    • 0035875896 scopus 로고    scopus 로고
    • Completely resected anaplastic thyroid carcinoma combined with adjuvant chemotherapy and irradiation is associated with prolonged survival
    • Haigh PI, Ituarte PH, Wu HS, Treseler PA, Posner MD, Quivey JM, Duh Q-Y, Clark OH 2001 Completely resected anaplastic thyroid carcinoma combined with adjuvant chemotherapy and irradiation is associated with prolonged survival. Cancer 91:2335-2342
    • (2001) Cancer , vol.91 , pp. 2335-2342
    • Haigh, P.I.1    Ituarte, P.H.2    Wu, H.S.3    Treseler, P.A.4    Posner, M.D.5    Quivey, J.M.6    Duh, Q.-Y.7    Clark, O.H.8
  • 3
    • 0027954495 scopus 로고
    • Heat-shock proteins as molecular chaperones
    • Becker J, Craig EA 1994 Heat-shock proteins as molecular chaperones. Eur J Biochem 219:11-23
    • (1994) Eur J Biochem , vol.219 , pp. 11-23
    • Becker, J.1    Craig, E.A.2
  • 4
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl FU 1996 Molecular chaperones in cellular protein folding. Nature 381:571-579
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 5
    • 0033724701 scopus 로고    scopus 로고
    • Chaperones in cell cycle regulation and mitogenic signal transduction: A review
    • Helmbrecht K, Zeise E, Rensing L 2000 Chaperones in cell cycle regulation and mitogenic signal transduction: a review. Cell Prolif 33:341-365
    • (2000) Cell Prolif , vol.33 , pp. 341-365
    • Helmbrecht, K.1    Zeise, E.2    Rensing, L.3
  • 6
    • 0029849363 scopus 로고    scopus 로고
    • Expression and roles of heat shock proteins in human breast cancer
    • Yano M, Naito Z, Tanaka S, Asano G 1996 Expression and roles of heat shock proteins in human breast cancer. Jpn J Cancer Res 87:908-915
    • (1996) Jpn J Cancer Res , vol.87 , pp. 908-915
    • Yano, M.1    Naito, Z.2    Tanaka, S.3    Asano, G.4
  • 8
    • 0026664393 scopus 로고
    • High constitutive expression of heat shock protein 90 alpha in human acute leukemia cells
    • Yufu Y, Nishimura J, Nawata H 1992 High constitutive expression of heat shock protein 90 alpha in human acute leukemia cells. Leukemia Res 16:597-605
    • (1992) Leukemia Res , vol.16 , pp. 597-605
    • Yufu, Y.1    Nishimura, J.2    Nawata, H.3
  • 9
    • 0026749295 scopus 로고
    • Unusual expression and localization of heat-shock proteins in human tumor cells
    • Ferrarini M, Heltai S, Zocchi MR, Rugarli C 1992 Unusual expression and localization of heat-shock proteins in human tumor cells. Int J Cancer 51:613-619
    • (1992) Int J Cancer , vol.51 , pp. 613-619
    • Ferrarini, M.1    Heltai, S.2    Zocchi, M.R.3    Rugarli, C.4
  • 11
    • 0029670034 scopus 로고    scopus 로고
    • p185erbB2 binds to GRP94 in vivo. Dissociation of the p185erbB2/GRP94 heterocomplex by benzoquinone ansamycins precedes depletion of p185erbB2
    • Chavany C, Mimnaugh E, Miller P, Bitton R, Nguyen P, Trepel J, Whitesell L, Schnur R, Moyer J, Neckers L 1996 p185erbB2 binds to GRP94 in vivo. Dissociation of the p185erbB2/GRP94 heterocomplex by benzoquinone ansamycins precedes depletion of p185erbB2. J Biol Chem 271:4974-4977
    • (1996) J Biol Chem , vol.271 , pp. 4974-4977
    • Chavany, C.1    Mimnaugh, E.2    Miller, P.3    Bitton, R.4    Nguyen, P.5    Trepel, J.6    Whitesell, L.7    Schnur, R.8    Moyer, J.9    Neckers, L.10
  • 12
    • 0029145215 scopus 로고
    • Geldanamycin selectively destabilizes and conformationally alters mutated p53
    • Blagosklonny MV, Toretsky J, Neckers L 1995 Geldanamycin selectively destabilizes and conformationally alters mutated p53. Oncogene 11:933-939
    • (1995) Oncogene , vol.11 , pp. 933-939
    • Blagosklonny, M.V.1    Toretsky, J.2    Neckers, L.3
  • 13
    • 0028068908 scopus 로고
    • Binding of benzoquinoid ansamycins to p100 correlates with their ability to deplete the erbB2 gene product p185
    • Miller P, Schnur RC, Barbacci E, Moyer MP, Moyer JD 1994 Binding of benzoquinoid ansamycins to p100 correlates with their ability to deplete the erbB2 gene product p185. Biochem Biophys Res Commun 201:1313-1319
    • (1994) Biochem Biophys Res Commun , vol.201 , pp. 1313-1319
    • Miller, P.1    Schnur, R.C.2    Barbacci, E.3    Moyer, M.P.4    Moyer, J.D.5
  • 14
    • 0028064940 scopus 로고
    • Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation
    • Whitesell L, Mimnaugh EG, De Costa B, Myers CE, Neckers LM 1994 Inhibition of heat shock protein HSP90-pp60v-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
  • 18
    • 0004954085 scopus 로고
    • Culture of hormone-dependent functional epithelial cells from rat thyroids
    • Ambesi-Impiombato FS, Parks LA, Coon HG 1980 Culture of hormone-dependent functional epithelial cells from rat thyroids. Proc Natl Acad Sci USA 77:3455-3459
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 3455-3459
    • Ambesi-Impiombato, F.S.1    Parks, L.A.2    Coon, H.G.3
  • 19
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • Mosmann T 1983 Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J Immunol Methods 65:55-63
    • (1983) J Immunol Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 24
    • 0033502429 scopus 로고    scopus 로고
    • Geldanamycin as a potential anti-cancer agent: Its molecular target and biochemical activity
    • Neckers L, Schulte TW, Mimnaugh E 1999 Geldanamycin as a potential anti-cancer agent: its molecular target and biochemical activity. Invest New Drugs 17:361-373
    • (1999) Invest New Drugs , vol.17 , pp. 361-373
    • Neckers, L.1    Schulte, T.W.2    Mimnaugh, E.3
  • 25
    • 0032058966 scopus 로고    scopus 로고
    • Autoantibodies to the 90kDa heat shock protein and poor survival in breast cancer patients
    • Conroy SE, Sasieni PD, Fentiman I, Latchman DS 1998 Autoantibodies to the 90kDa heat shock protein and poor survival in breast cancer patients [Letter]. Eur J Cancer 34:942-943
    • (1998) Eur J Cancer , vol.34 , pp. 942-943
    • Conroy, S.E.1    Sasieni, P.D.2    Fentiman, I.3    Latchman, D.S.4
  • 26
    • 0033988478 scopus 로고    scopus 로고
    • Antibodies to heat shock protein 90 in osteosarcoma patients correlate with response to neoadjuvant chemotherapy
    • Trieb K, Gerth R, Holzer G, Grohs JG, Berger P, Kotz R 2000 Antibodies to heat shock protein 90 in osteosarcoma patients correlate with response to neoadjuvant chemotherapy. Br J Cancer 82:85-87
    • (2000) Br J Cancer , vol.82 , pp. 85-87
    • Trieb, K.1    Gerth, R.2    Holzer, G.3    Grohs, J.G.4    Berger, P.5    Kotz, R.6
  • 27
    • 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
  • 28
    • 0030987132 scopus 로고    scopus 로고
    • An atypical topoisomerase II from Archaea with implications for meiotic recombination
    • Bergerat A, de Massy B, Gadelle D, Varoutas PC, Nicolas A, Forterre P 1997 An atypical topoisomerase II from Archaea with implications for meiotic recombination. Nature 386:414-417
    • (1997) Nature , vol.386 , pp. 414-417
    • Bergerat, A.1    De Massy, B.2    Gadelle, D.3    Varoutas, P.C.4    Nicolas, A.5    Forterre, P.6
  • 30
    • 0032959590 scopus 로고    scopus 로고
    • Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin
    • Roe SM, Prodromou C, O'Brien R, Ladbury JE, Piper PW, Pearl LH 1999 Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin. J Med Chem 42:260-266
    • (1999) J Med Chem , vol.42 , pp. 260-266
    • Roe, S.M.1    Prodromou, C.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 32
    • 0035872442 scopus 로고    scopus 로고
    • Inhibition of signal transduction by the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin results in cytostasis and apoptosis
    • Hostein I, Robertson D, DiStefano F, Workman P, Clarke PA 2001 Inhibition of signal transduction by the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin results in cytostasis and apoptosis. Cancer Res 61:4003-4009
    • (2001) Cancer Res , vol.61 , pp. 4003-4009
    • Hostein, I.1    Robertson, D.2    DiStefano, F.3    Workman, P.4    Clarke, P.A.5
  • 33
    • 0023883930 scopus 로고
    • Reversal of transformed phenotypes by herbimycin A in src oncogene expressed rat fibroblasts
    • Murakami Y, Mizuno S, Hori M, Uehara Y 1988 Reversal of transformed phenotypes by herbimycin A in src oncogene expressed rat fibroblasts. Cancer Res 48:1587-1590
    • (1988) Cancer Res , vol.48 , pp. 1587-1590
    • Murakami, Y.1    Mizuno, S.2    Hori, M.3    Uehara, Y.4
  • 34
    • 0024467122 scopus 로고
    • Irreversible inhibition of v-src tyrosine kinase activity by herbimycin A and its abrogation by sulfhydryl compounds
    • Uehara Y, Fukazawa H, Murakami Y, Mizuno S 1989 Irreversible inhibition of v-src tyrosine kinase activity by herbimycin A and its abrogation by sulfhydryl compounds. Biochem Biophys Res Commun 163:803-809
    • (1989) Biochem Biophys Res Commun , vol.163 , pp. 803-809
    • Uehara, Y.1    Fukazawa, H.2    Murakami, Y.3    Mizuno, S.4
  • 35
    • 0027410497 scopus 로고
    • The MAP kinase cascade is essential for diverse signal transduction pathways
    • Nishida E, Gotoh Y 1993 The MAP kinase cascade is essential for diverse signal transduction pathways. Trends Biochem Sci 18:128-131
    • (1993) Trends Biochem Sci , vol.18 , pp. 128-131
    • Nishida, E.1    Gotoh, Y.2
  • 37
    • 0033604576 scopus 로고    scopus 로고
    • Isotype-specific functions of Raf kinases
    • Hagemann C, Rapp UR 1999 Isotype-specific functions of Raf kinases. Exp Cell Res 253:34-46
    • (1999) Exp Cell Res , vol.253 , pp. 34-46
    • Hagemann, C.1    Rapp, U.R.2
  • 38
    • 0029977448 scopus 로고    scopus 로고
    • Antitumor activity of a phosphorothioate antisense oligodeoxynucleotide targeted against C-raf kinase
    • Monia BP, Johnston JF, Geiger T, Muller M, Fabbro D 1996 Antitumor activity of a phosphorothioate antisense oligodeoxynucleotide targeted against C-raf kinase. Nat Med 2:668-675
    • (1996) Nat Med , vol.2 , pp. 668-675
    • Monia, B.P.1    Johnston, J.F.2    Geiger, T.3    Muller, M.4    Fabbro, D.5
  • 39
    • 0034254678 scopus 로고    scopus 로고
    • Depletion of Raf-1 protooncogene by geldanamycin causes apoptosis in human luteinized granulosa cells
    • Khan SM, Oliver RH, Dauffenbach LM, Yeh J 2000 Depletion of Raf-1 protooncogene by geldanamycin causes apoptosis in human luteinized granulosa cells. Fertil Steril 74:359-365
    • (2000) Fertil Steril , vol.74 , pp. 359-365
    • Khan, S.M.1    Oliver, R.H.2    Dauffenbach, L.M.3    Yeh, J.4
  • 41
    • 0031054517 scopus 로고    scopus 로고
    • The hsp90-binding antibiotic geldanamycin decreases Raf levels and epidermal growth factor signaling without disrupting formation of signaling complexes or reducing the specific enzymatic activity of Raf kinase
    • Stancato LF, Silverstein AM, Owens-Grillo JK, Chow YH, Jove R, Pratt WB 1997 The hsp90-binding antibiotic geldanamycin decreases Raf levels and epidermal growth factor signaling without disrupting formation of signaling complexes or reducing the specific enzymatic activity of Raf kinase. J Biol Chem 272:4013-4020
    • (1997) J Biol Chem , vol.272 , pp. 4013-4020
    • Stancato, L.F.1    Silverstein, A.M.2    Owens-Grillo, J.K.3    Chow, Y.H.4    Jove, R.5    Pratt, W.B.6
  • 43
    • 0032897474 scopus 로고    scopus 로고
    • Benzoquinoid ansamycins (herbimycin A and geldanamycin) interfere with the maturation of growth factor receptor tyrosine kinases
    • Sakagami M, Morrison P, Welch WJ 1999 Benzoquinoid ansamycins (herbimycin A and geldanamycin) interfere with the maturation of growth factor receptor tyrosine kinases. Cell Stress Chaperones 4:19-28
    • (1999) Cell Stress Chaperones , vol.4 , pp. 19-28
    • Sakagami, M.1    Morrison, P.2    Welch, W.J.3
  • 44
    • 0028894184 scopus 로고
    • Epidermal growth factor (EGF)- and transforming growth factor α-stimulated invasion and growth of follicular thyroid cancer cells can be blocked by antagonism to the EGF receptor and tyrosine kinase in vitro
    • Hölting T, Siperstein AE, Clark OH, Duh Q-Y 1995 Epidermal growth factor (EGF)- and transforming growth factor α-stimulated invasion and growth of follicular thyroid cancer cells can be blocked by antagonism to the EGF receptor and tyrosine kinase in vitro. Eur J Endocrinol 132:229-235
    • (1995) Eur J Endocrinol , vol.132 , pp. 229-235
    • Hölting, T.1    Siperstein, A.E.2    Clark, O.H.3    Duh, Q.-Y.4
  • 45
    • 0028874675 scopus 로고
    • Oncoproteins and tumor progression in papillary thyroid carcinoma: Presence of epidermal growth factor receptor, c-erbB-2 protein, estrogen receptor related protein, p21-ras protein, and proliferation indicators in relation to tumor recurrences and patient survival
    • Akslen LA, Varhaug JE 1995 Oncoproteins and tumor progression in papillary thyroid carcinoma: presence of epidermal growth factor receptor, c-erbB-2 protein, estrogen receptor related protein, p21-ras protein, and proliferation indicators in relation to tumor recurrences and patient survival. Cancer 76:1643-1654
    • (1995) Cancer , vol.76 , pp. 1643-1654
    • Akslen, L.A.1    Varhaug, J.E.2
  • 46
    • 0028925355 scopus 로고
    • Expression of growth factors and growth factor receptors in normal and tumorous human thyroid tissues
    • van der Laan BF, Freeman JL, Asa SL 1995 Expression of growth factors and growth factor receptors in normal and tumorous human thyroid tissues. Thyroid 5:67-73
    • (1995) Thyroid , vol.5 , pp. 67-73
    • Van Der Laan, B.F.1    Freeman, J.L.2    Asa, S.L.3
  • 47
    • 0034698143 scopus 로고    scopus 로고
    • Intracellular retention and degradation of the epidermal growth factor receptor, two distinct processes mediated by benzoquinone ansamycins
    • Supino-Rosin L, Yoshimura A, Yarden Y, Elazar Z, Neumann D 2000 Intracellular retention and degradation of the epidermal growth factor receptor, two distinct processes mediated by benzoquinone ansamycins. J Biol Chem 275:21850-21855
    • (2000) J Biol Chem , vol.275 , pp. 21850-21855
    • Supino-Rosin, L.1    Yoshimura, A.2    Yarden, Y.3    Elazar, Z.4    Neumann, D.5
  • 48
    • 0035810742 scopus 로고    scopus 로고
    • Measurement of the novel antitumor agent 17-(allylamino)-17-demethoxygeldanamycin in human plasma by high-performance liquid chromatography
    • Agnew EB, Wilson RH, Grem JL, Neckers L, Bi D, Takimoto CH 2001 Measurement of the novel antitumor agent 17-(allylamino)-17-demethoxygeldanamycin in human plasma by high-performance liquid chromatography. J Chromatogr B Biomed Sci Appl 755:237-243
    • (2001) J Chromatogr B Biomed Sci Appl , vol.755 , pp. 237-243
    • Agnew, E.B.1    Wilson, R.H.2    Grem, J.L.3    Neckers, L.4    Bi, D.5    Takimoto, C.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.