메뉴 건너뛰기




Volumn 581, Issue 8, 2007, Pages 1649-1656

Heat shock protein 27 is associated with irinotecan resistance in human colorectal cancer cells

Author keywords

Hsp27; Human colorectal cancer cells; Irinotecan resistance

Indexed keywords

ANTISENSE OLIGODEOXYNUCLEOTIDE; CASPASE 3; FLUOROURACIL; FOLINIC ACID; HEAT SHOCK PROTEIN 27; IRINOTECAN;

EID: 34047132772     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.02.075     Document Type: Article
Times cited : (60)

References (41)
  • 1
    • 0035522658 scopus 로고    scopus 로고
    • Irinotecan plus oxaliplatin: a promising combination for advanced colorectal cancer
    • Wasserman E., Sutherland W., and Cvitkovic E. Irinotecan plus oxaliplatin: a promising combination for advanced colorectal cancer. Clin. Colorectal Cancer 1 (2001) 149-153
    • (2001) Clin. Colorectal Cancer , vol.1 , pp. 149-153
    • Wasserman, E.1    Sutherland, W.2    Cvitkovic, E.3
  • 2
    • 0028174984 scopus 로고
    • DNA topoisomerases: essential enzymes and lethal targets
    • Chen A.Y., and Liu L.F. DNA topoisomerases: essential enzymes and lethal targets. Annu. Rev. Pharmacol. Toxicol. 36 (1994) 191-218
    • (1994) Annu. Rev. Pharmacol. Toxicol. , vol.36 , pp. 191-218
    • Chen, A.Y.1    Liu, L.F.2
  • 3
    • 0029960812 scopus 로고    scopus 로고
    • Eukaryotic DNA topoisomerase I: genome gatekeeper and its intruders, camptothecins
    • Pommier Y. Eukaryotic DNA topoisomerase I: genome gatekeeper and its intruders, camptothecins. Semin. Oncol. 23 (1996) 3-10
    • (1996) Semin. Oncol. , vol.23 , pp. 3-10
    • Pommier, Y.1
  • 5
    • 0344394180 scopus 로고    scopus 로고
    • Mechanisms of resistance to topoisomerase I-targeting drugs
    • Rasheed Z.A., and Rubin E.H. Mechanisms of resistance to topoisomerase I-targeting drugs. Oncogene 22 (2003) 7296-7304
    • (2003) Oncogene , vol.22 , pp. 7296-7304
    • Rasheed, Z.A.1    Rubin, E.H.2
  • 6
    • 0032454360 scopus 로고    scopus 로고
    • Molecular chaperones in the etiology and therapy of cancer
    • Soti C.S., and Csermely P. Molecular chaperones in the etiology and therapy of cancer. Pathol. Oncol. Res. 4 (1998) 316-321
    • (1998) Pathol. Oncol. Res. , vol.4 , pp. 316-321
    • Soti, C.S.1    Csermely, P.2
  • 7
    • 0034605446 scopus 로고    scopus 로고
    • Role of the heat shock response and molecular chaperones in oncogenesis and cell death
    • Jolly C., and Morimoto R.I. Role of the heat shock response and molecular chaperones in oncogenesis and cell death. J. Natl. Cancer Res. Inst. 92 (2000) 1564-1572
    • (2000) J. Natl. Cancer Res. Inst. , vol.92 , pp. 1564-1572
    • Jolly, C.1    Morimoto, R.I.2
  • 9
    • 0030785821 scopus 로고    scopus 로고
    • HSP27 as a mediator of confluence-dependent resistance to cell death induced by anticancer drugs
    • Garrido C., Ottavi P., Fromentin A., Hammann A., Arrigo A.P., Chauffert B., and Mehlen P. HSP27 as a mediator of confluence-dependent resistance to cell death induced by anticancer drugs. Cancer Res. 57 (1997) 2661-2667
    • (1997) Cancer Res. , vol.57 , pp. 2661-2667
    • Garrido, C.1    Ottavi, P.2    Fromentin, A.3    Hammann, A.4    Arrigo, A.P.5    Chauffert, B.6    Mehlen, P.7
  • 10
    • 0034608892 scopus 로고    scopus 로고
    • Selective depletion of heat shock protein 70 (Hsp70) activates a tumor-specific death program that is independent of caspases and bypasses Bcl-2
    • Nylandsted J., Rohde M., Brand K., Bastholm L., Elling F., and Jaattela M. Selective depletion of heat shock protein 70 (Hsp70) activates a tumor-specific death program that is independent of caspases and bypasses Bcl-2. Proc. Natl. Acad. Sci. USA 97 (2000) 7871-7876
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7871-7876
    • Nylandsted, J.1    Rohde, M.2    Brand, K.3    Bastholm, L.4    Elling, F.5    Jaattela, M.6
  • 18
    • 0025988318 scopus 로고
    • Increased survival after treatments with anticancer agents of Chinese hamster cells expressing the human Mr 27,000 heat shock protein
    • Huot J., Roy G., Lambert H., Chretien P., and Landry J. Increased survival after treatments with anticancer agents of Chinese hamster cells expressing the human Mr 27,000 heat shock protein. Cancer Res. 51 (1991) 5245-5252
    • (1991) Cancer Res. , vol.51 , pp. 5245-5252
    • Huot, J.1    Roy, G.2    Lambert, H.3    Chretien, P.4    Landry, J.5
  • 20
    • 0035954829 scopus 로고    scopus 로고
    • Heat shock protein 27 was up-regulated in cisplatin resistant human ovarian tumor cell line and associated with the cisplatin resistance
    • Yamamoto K., Okamoto A., Isonishi S., Ochiai K., and Ohtake Y. Heat shock protein 27 was up-regulated in cisplatin resistant human ovarian tumor cell line and associated with the cisplatin resistance. Cancer Lett. 168 (2001) 173-181
    • (2001) Cancer Lett. , vol.168 , pp. 173-181
    • Yamamoto, K.1    Okamoto, A.2    Isonishi, S.3    Ochiai, K.4    Ohtake, Y.5
  • 22
    • 0035155013 scopus 로고    scopus 로고
    • TTF-1, a homeodomain gene required for diencephalic morphogenesis, is postnatally expressed in the neuroendocrine brain in a developmentally regulated and cell-specific fashion
    • Lee B.J., Cho G.J., Norgren Jr. R.B., Junier M.P., Hill D.F., Tapia V., Costa M.E., and Ojeda S.R. TTF-1, a homeodomain gene required for diencephalic morphogenesis, is postnatally expressed in the neuroendocrine brain in a developmentally regulated and cell-specific fashion. Mol. Cell. Neurosci. 17 (2001) 107-126
    • (2001) Mol. Cell. Neurosci. , vol.17 , pp. 107-126
    • Lee, B.J.1    Cho, G.J.2    Norgren Jr., R.B.3    Junier, M.P.4    Hill, D.F.5    Tapia, V.6    Costa, M.E.7    Ojeda, S.R.8
  • 24
    • 0037246247 scopus 로고    scopus 로고
    • On the role of Hsp27 in regulating apoptosis
    • Concannon C.G., Gorman A.M., and Samali A. On the role of Hsp27 in regulating apoptosis. Apoptosis 8 (2003) 61-70
    • (2003) Apoptosis , vol.8 , pp. 61-70
    • Concannon, C.G.1    Gorman, A.M.2    Samali, A.3
  • 25
    • 0033082063 scopus 로고    scopus 로고
    • Activation and role of caspases in chemotherapy-induced apoptosis
    • Schmitt E., Sane A.T., and Bertrand R. Activation and role of caspases in chemotherapy-induced apoptosis. Drug Resist. Update 2 (1999) 21-29
    • (1999) Drug Resist. Update , vol.2 , pp. 21-29
    • Schmitt, E.1    Sane, A.T.2    Bertrand, R.3
  • 26
    • 0028273481 scopus 로고
    • A 27 kDa heat shock protein that has anomalous prognostic powers in early and advanced breast cancer
    • Love S., and King R.J. A 27 kDa heat shock protein that has anomalous prognostic powers in early and advanced breast cancer. Br. J. Cancer 69 (1994) 743-748
    • (1994) Br. J. Cancer , vol.69 , pp. 743-748
    • Love, S.1    King, R.J.2
  • 27
    • 0027366354 scopus 로고
    • The small heat shock protein hsp27 is correlated with growth and drug resistance in human breast cancer cell lines
    • Oesterreich S., Weng C.N., Qiu M., Hilsenbeck S.G., Osborne C.K., and Fuqua S.A. The small heat shock protein hsp27 is correlated with growth and drug resistance in human breast cancer cell lines. Cancer Res. 53 (1993) 4443-4448
    • (1993) Cancer Res. , vol.53 , pp. 4443-4448
    • Oesterreich, S.1    Weng, C.N.2    Qiu, M.3    Hilsenbeck, S.G.4    Osborne, C.K.5    Fuqua, S.A.6
  • 29
    • 0028842632 scopus 로고
    • Heat shock proteins are differentially expressed in human gastrointestinal cancers
    • Ehrenfried J.A., Herron B.E., Townsend Jr. C.M., and Evers B.M. Heat shock proteins are differentially expressed in human gastrointestinal cancers. Surg. Oncol. 4 (1995) 197-203
    • (1995) Surg. Oncol. , vol.4 , pp. 197-203
    • Ehrenfried, J.A.1    Herron, B.E.2    Townsend Jr., C.M.3    Evers, B.M.4
  • 31
    • 0036511128 scopus 로고    scopus 로고
    • Prognostic significance of heat shock protein 27 (HSP27) in patients with oral squamous cell carcinoma
    • Mese H., Sasaki A., Nakayama S., Yoshioka N., Yoshihama Y., Kishimoto K., and Matsumura T. Prognostic significance of heat shock protein 27 (HSP27) in patients with oral squamous cell carcinoma. Oncol. Rep. 9 (2002) 341-344
    • (2002) Oncol. Rep. , vol.9 , pp. 341-344
    • Mese, H.1    Sasaki, A.2    Nakayama, S.3    Yoshioka, N.4    Yoshihama, Y.5    Kishimoto, K.6    Matsumura, T.7
  • 32
    • 0032403161 scopus 로고    scopus 로고
    • Abundance of heat shock proteins (hsp89, hsp60, and hsp27) in malignant cells of Hodgkin's disease
    • Hsu P.L., and Hsu S.M. Abundance of heat shock proteins (hsp89, hsp60, and hsp27) in malignant cells of Hodgkin's disease. Cancer Res. 58 (1998) 5507-5513
    • (1998) Cancer Res. , vol.58 , pp. 5507-5513
    • Hsu, P.L.1    Hsu, S.M.2
  • 33
    • 0029882949 scopus 로고    scopus 로고
    • Effect of overexpression of the small heat shock protein HSP27 on the heat and drug sensitivities of human testis tumor cells
    • Richards E.H., Hickey E., Weber L., and Master J.R. Effect of overexpression of the small heat shock protein HSP27 on the heat and drug sensitivities of human testis tumor cells. Cancer Res. 56 (1996) 2446-2451
    • (1996) Cancer Res. , vol.56 , pp. 2446-2451
    • Richards, E.H.1    Hickey, E.2    Weber, L.3    Master, J.R.4
  • 35
    • 0025727532 scopus 로고
    • Phosphorylation of HSP27 during development and decay of thermotolerance in Chinese hamster cells
    • Landry J., Chretien P., Laszlo A., and Lambert H. Phosphorylation of HSP27 during development and decay of thermotolerance in Chinese hamster cells. J. Cell Physiol. 147 (1991) 93-101
    • (1991) J. Cell Physiol. , vol.147 , pp. 93-101
    • Landry, J.1    Chretien, P.2    Laszlo, A.3    Lambert, H.4
  • 37
    • 0033664112 scopus 로고    scopus 로고
    • Differential regulation of P53, c-Myc, Bcl-2, Bax and AFP protein expression, and caspase activity during 10-hydroxycamptothecin-induced apoptosis in Hep G2 cells
    • Zhang X.W., and Xu B. Differential regulation of P53, c-Myc, Bcl-2, Bax and AFP protein expression, and caspase activity during 10-hydroxycamptothecin-induced apoptosis in Hep G2 cells. Anti-cancer Drug 11 (2000) 747-756
    • (2000) Anti-cancer Drug , vol.11 , pp. 747-756
    • Zhang, X.W.1    Xu, B.2
  • 38
    • 0034963578 scopus 로고    scopus 로고
    • Hsp27 inhibits cytochrome c-mediated caspase activation by sequestering both pro-caspase-3 and cytochrome c
    • Concannon C.G., Orrenius S., and Samali A. Hsp27 inhibits cytochrome c-mediated caspase activation by sequestering both pro-caspase-3 and cytochrome c. Gene Expression 9 (2001) 195-201
    • (2001) Gene Expression , vol.9 , pp. 195-201
    • Concannon, C.G.1    Orrenius, S.2    Samali, A.3
  • 41
    • 0029610424 scopus 로고
    • Intracellular reactive oxygen species as apparent modulators of heat-shock protein 27 (hsp27) structural organization and phosphorylation in basal and tumour necrosis factor alpha-treated T47D human carcinoma cells
    • Mehlen P., Kretz-Remy C., Briolay J., Fostan P., Mirault M.E., and Arrigo A.P. Intracellular reactive oxygen species as apparent modulators of heat-shock protein 27 (hsp27) structural organization and phosphorylation in basal and tumour necrosis factor alpha-treated T47D human carcinoma cells. Biochem. J. 312 (1995) 367-375
    • (1995) Biochem. J. , vol.312 , pp. 367-375
    • Mehlen, P.1    Kretz-Remy, C.2    Briolay, J.3    Fostan, P.4    Mirault, M.E.5    Arrigo, A.P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.