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Volumn 314, Issue 13, 2008, Pages 2468-2476

Hsp70B′ and Hsp72 form a complex in stressed human colon cells and each contributes to cytoprotection

Author keywords

Acquired thermotolerance; Colon cancer; CRL 1807; Cytoprotection; Heat shock; HOP; Hsp70B'; Hsp72; HT 29; siRNA; Stress complex

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 72; SMALL INTERFERING RNA; HEAT SHOCK PROTEIN; HSPA7 PROTEIN, HUMAN; ISOPROTEIN; MULTIPROTEIN COMPLEX; STIP1 PROTEIN, HUMAN;

EID: 47349097542     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2008.05.002     Document Type: Article
Times cited : (33)

References (25)
  • 1
    • 0023375806 scopus 로고
    • Complex interactions among members of an essential subfamily of hsp70 genes in Saccharomyces cerevisiae
    • Werner-Washburne M., Stone D.E., and Craig E.A. Complex interactions among members of an essential subfamily of hsp70 genes in Saccharomyces cerevisiae. Mol. Cell. Biol. 7 (1987) 2568-2577
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2568-2577
    • Werner-Washburne, M.1    Stone, D.E.2    Craig, E.A.3
  • 2
    • 0035197692 scopus 로고    scopus 로고
    • Insights into regulation and function of the major stress-induced hsp70 molecular chaperone in vivo: analysis of mice with targeted gene disruption of the hsp70.1 or hsp70.3 gene
    • Huang L., Mivechi N.F., and Moskophidis D. Insights into regulation and function of the major stress-induced hsp70 molecular chaperone in vivo: analysis of mice with targeted gene disruption of the hsp70.1 or hsp70.3 gene. Mol. Cell. Biol. 21 (2001) 8575-8591
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 8575-8591
    • Huang, L.1    Mivechi, N.F.2    Moskophidis, D.3
  • 3
    • 1342265394 scopus 로고    scopus 로고
    • Proteasome inhibition increases HuR level, restores heat-inducible HSP72 expression and thermotolerance in WI-38 senescent human fibroblasts
    • Bonelli M.A., Alfieri R.R., Desenzani S., Petronini P.G., and Borghetti A.F. Proteasome inhibition increases HuR level, restores heat-inducible HSP72 expression and thermotolerance in WI-38 senescent human fibroblasts. Exp. Gerontol. 39 (2004) 423-432
    • (2004) Exp. Gerontol. , vol.39 , pp. 423-432
    • Bonelli, M.A.1    Alfieri, R.R.2    Desenzani, S.3    Petronini, P.G.4    Borghetti, A.F.5
  • 4
    • 0041528154 scopus 로고    scopus 로고
    • Sensitization of human Ewing's tumor cells to chemotherapy and heat treatment by the bioflavonoid quercetin
    • Debes A., Oerding M., Willers R., Gobel U., and Wessalowski R. Sensitization of human Ewing's tumor cells to chemotherapy and heat treatment by the bioflavonoid quercetin. Anticancer Res. 23 (2003) 3359-3366
    • (2003) Anticancer Res. , vol.23 , pp. 3359-3366
    • Debes, A.1    Oerding, M.2    Willers, R.3    Gobel, U.4    Wessalowski, R.5
  • 5
    • 0036450294 scopus 로고    scopus 로고
    • Cytoprotection against thermal injury: evaluation of herbimycin A by cell viability and cDNA arrays
    • Dinh H.K., Stavchansky S., Schuschereba S.T., Stuck B.E., and Bowman P.D. Cytoprotection against thermal injury: evaluation of herbimycin A by cell viability and cDNA arrays. Pharmacogenomics J. 2 (2002) 318-326
    • (2002) Pharmacogenomics J. , vol.2 , pp. 318-326
    • Dinh, H.K.1    Stavchansky, S.2    Schuschereba, S.T.3    Stuck, B.E.4    Bowman, P.D.5
  • 6
    • 33747875267 scopus 로고    scopus 로고
    • Targeting the heat shock factor 1 by RNA interference: a potent tool to enhance hyperthermochemotherapy efficacy in cervical cancer
    • Rossi A., Ciafre S., Balsamo M., Pierimarchi P., and Santoro M.G. Targeting the heat shock factor 1 by RNA interference: a potent tool to enhance hyperthermochemotherapy efficacy in cervical cancer. Cancer Res. 66 (2006) 7678-7685
    • (2006) Cancer Res. , vol.66 , pp. 7678-7685
    • Rossi, A.1    Ciafre, S.2    Balsamo, M.3    Pierimarchi, P.4    Santoro, M.G.5
  • 7
    • 0025363926 scopus 로고
    • The human heat-shock protein family. Expression of a novel heat-inducible HSP70 (HSP70B') and isolation of its cDNA and genomic DNA
    • Leung T.K., Rajendran M.Y., Monfries C., Hall C., and Lim L. The human heat-shock protein family. Expression of a novel heat-inducible HSP70 (HSP70B') and isolation of its cDNA and genomic DNA. Biochem. J. 267 (1990) 125-132
    • (1990) Biochem. J. , vol.267 , pp. 125-132
    • Leung, T.K.1    Rajendran, M.Y.2    Monfries, C.3    Hall, C.4    Lim, L.5
  • 9
    • 33845409610 scopus 로고    scopus 로고
    • Cell number-dependent regulation of Hsp70B' expression: evidence of an extracellular regulator
    • Noonan E.J., Place R.F., Rasoulpour R.J., Giardina C., and Hightower L.E. Cell number-dependent regulation of Hsp70B' expression: evidence of an extracellular regulator. J. Cell. Physiol. 210 (2007) 201-211
    • (2007) J. Cell. Physiol. , vol.210 , pp. 201-211
    • Noonan, E.J.1    Place, R.F.2    Rasoulpour, R.J.3    Giardina, C.4    Hightower, L.E.5
  • 10
    • 67349249714 scopus 로고    scopus 로고
    • Surface expression of Hsp70B' in response to proteasome inhibition in human colon cells
    • Noonan E.J., Fournier G., and Hightower L.E. Surface expression of Hsp70B' in response to proteasome inhibition in human colon cells. Cell Stress Chaperones 13 (2008) 105-110
    • (2008) Cell Stress Chaperones , vol.13 , pp. 105-110
    • Noonan, E.J.1    Fournier, G.2    Hightower, L.E.3
  • 11
    • 40749086430 scopus 로고    scopus 로고
    • E.J. Noonan, R.F. Place, C. Giardina, L.E. Hightower, Hsp70B′ regulation and function, cell stress chaperones 12 (2007) 219-229. Corrections in Cell Stress & Chaperones 12 (2007): 393-402.
    • E.J. Noonan, R.F. Place, C. Giardina, L.E. Hightower, Hsp70B′ regulation and function, cell stress chaperones 12 (2007) 219-229. Corrections in Cell Stress & Chaperones 12 (2007): 393-402.
  • 12
    • 2342651518 scopus 로고    scopus 로고
    • Molecular chaperones and the stress of oncogenesis
    • Mosser D.D., and Morimoto R.I. Molecular chaperones and the stress of oncogenesis. Oncogene 23 (2004) 2907-2918
    • (2004) Oncogene , vol.23 , pp. 2907-2918
    • Mosser, D.D.1    Morimoto, R.I.2
  • 15
    • 11844252002 scopus 로고    scopus 로고
    • Low tumor cell density environment yields survival advantage of tumor cells exposed to MTX in vitro
    • de Anta J.M., Real F.X., and Mayol X. Low tumor cell density environment yields survival advantage of tumor cells exposed to MTX in vitro. Biochim. Biophys. Acta 1721 (2005) 98-106
    • (2005) Biochim. Biophys. Acta , vol.1721 , pp. 98-106
    • de Anta, J.M.1    Real, F.X.2    Mayol, X.3
  • 17
    • 0036324853 scopus 로고    scopus 로고
    • Role of Raf-1 and FAK in cell density-dependent regulation of integrin-dependent activation of MAP kinase
    • Zhang L., Bewick M., and Lafrenie R.M. Role of Raf-1 and FAK in cell density-dependent regulation of integrin-dependent activation of MAP kinase. Carcinogenesis 23 (2002) 1251-1258
    • (2002) Carcinogenesis , vol.23 , pp. 1251-1258
    • Zhang, L.1    Bewick, M.2    Lafrenie, R.M.3
  • 18
    • 0034653824 scopus 로고    scopus 로고
    • Overexpression of the 27 kDa heat shock protein is associated with thermoresistance and chemoresistance but not with radioresistance
    • Fortin A., Raybaud-Diogene H., Tetu B., Deschenes R., Huot J., and Landry J. Overexpression of the 27 kDa heat shock protein is associated with thermoresistance and chemoresistance but not with radioresistance. Int. J. Radiat. Oncol. Biol. Phys. 46 (2000) 1259-1266
    • (2000) Int. J. Radiat. Oncol. Biol. Phys. , vol.46 , pp. 1259-1266
    • Fortin, A.1    Raybaud-Diogene, H.2    Tetu, B.3    Deschenes, R.4    Huot, J.5    Landry, J.6
  • 19
    • 0033669698 scopus 로고    scopus 로고
    • Expression of antisense hsp70 is a major determining factor in heat-induced cell death of P-19 carcinoma cells
    • Nishimura R.N., Santos D., Esmaili L., Fu S.T., and Dwyer B.E. Expression of antisense hsp70 is a major determining factor in heat-induced cell death of P-19 carcinoma cells. Cell Stress Chaperones 5 (2000) 173-180
    • (2000) Cell Stress Chaperones , vol.5 , pp. 173-180
    • Nishimura, R.N.1    Santos, D.2    Esmaili, L.3    Fu, S.T.4    Dwyer, B.E.5
  • 20
    • 33745667754 scopus 로고    scopus 로고
    • A disulfide bridge mediated by cysteine 574 is formed in the dimer of the 70-kDa heat shock protein
    • Nemoto T.K., Fukuma Y., Itoh H., Takagi T., and Ono T. A disulfide bridge mediated by cysteine 574 is formed in the dimer of the 70-kDa heat shock protein. J. Biochem. (Tokyo) 139 (2006) 677-687
    • (2006) J. Biochem. (Tokyo) , vol.139 , pp. 677-687
    • Nemoto, T.K.1    Fukuma, Y.2    Itoh, H.3    Takagi, T.4    Ono, T.5
  • 21
    • 67349249714 scopus 로고    scopus 로고
    • Surface expression of Hsp70B′ in response to proteasome inhibition in human colon cells
    • Noonan E.J., Fournier G., and Hightower L.E. Surface expression of Hsp70B′ in response to proteasome inhibition in human colon cells. Cell Stress Chaperones 13 (2008) 105-110
    • (2008) Cell Stress Chaperones , vol.13 , pp. 105-110
    • Noonan, E.J.1    Fournier, G.2    Hightower, L.E.3
  • 22
    • 0031106603 scopus 로고    scopus 로고
    • Chaperones get in touch: the Hip-Hop connection
    • Frydman J., and Hohfeld J. Chaperones get in touch: the Hip-Hop connection. Trends Biochem. Sci. 22 (1997) 87-92
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 87-92
    • Frydman, J.1    Hohfeld, J.2
  • 23
    • 0030324952 scopus 로고    scopus 로고
    • A pathway of multi-chaperone interactions common to diverse regulatory proteins: estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf1, and the aryl hydrocarbon receptor
    • Nair S.C., Toran E.J., Rimerman R.A., Hjermstad S., Smithgall T.E., and Smith D.F. A pathway of multi-chaperone interactions common to diverse regulatory proteins: estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf1, and the aryl hydrocarbon receptor. Cell Stress Chaperones 1 (1996) 237-250
    • (1996) Cell Stress Chaperones , vol.1 , pp. 237-250
    • Nair, S.C.1    Toran, E.J.2    Rimerman, R.A.3    Hjermstad, S.4    Smithgall, T.E.5    Smith, D.F.6
  • 24
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    • Scheufler C., Brinker A., Bourenkov G., Pegoraro S., Moroder L., Bartunik H., Hartl F.U., and Moarefi I. Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 101 (2000) 199-210
    • (2000) Cell , vol.101 , pp. 199-210
    • Scheufler, C.1    Brinker, A.2    Bourenkov, G.3    Pegoraro, S.4    Moroder, L.5    Bartunik, H.6    Hartl, F.U.7    Moarefi, I.8
  • 25
    • 0030046813 scopus 로고    scopus 로고
    • A multicopy suppressor of a cell cycle defect in S. pombe encodes a heat shock-inducible 40 kDa cyclophilin-like protein
    • Weisman R., Creanor J., and Fantes P. A multicopy suppressor of a cell cycle defect in S. pombe encodes a heat shock-inducible 40 kDa cyclophilin-like protein. Embo J. 15 (1996) 447-456
    • (1996) Embo J. , vol.15 , pp. 447-456
    • Weisman, R.1    Creanor, J.2    Fantes, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.