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Volumn 265, Issue 1-2, 2009, Pages 10-14

Correlations and co-localizations of Hsp70 with XPA, XPG in human bronchial epithelia cells exposed to benzo[a]pyrene

Author keywords

Benzo a pyrene; Heat shock protein 70; Human bronchial epithelia cells; Nucleotide excision repair

Indexed keywords

BENZO[A]PYRENE; DNA; HEAT SHOCK PROTEIN 70;

EID: 70349982574     PISSN: 0300483X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tox.2009.09.001     Document Type: Article
Times cited : (23)

References (42)
  • 1
    • 0034113806 scopus 로고    scopus 로고
    • Variability in nucleotide excision repair and cancer risk: a review
    • Benhamou S., and Sarasin A. Variability in nucleotide excision repair and cancer risk: a review. Mutat. Res. 462 (2000) 149-158
    • (2000) Mutat. Res. , vol.462 , pp. 149-158
    • Benhamou, S.1    Sarasin, A.2
  • 2
    • 0033168167 scopus 로고    scopus 로고
    • A novel function of emodin: enhancement of the nucleotide excision repair of UV- and cisplatin-induced DNA damage in human cells
    • Chang L.C., Sheu H.M., Huang Y.S., Tsai T.R., and Kuo K.W. A novel function of emodin: enhancement of the nucleotide excision repair of UV- and cisplatin-induced DNA damage in human cells. Biochem. Pharmacol. 58 (1999) 49-57
    • (1999) Biochem. Pharmacol. , vol.58 , pp. 49-57
    • Chang, L.C.1    Sheu, H.M.2    Huang, Y.S.3    Tsai, T.R.4    Kuo, K.W.5
  • 3
    • 0034725975 scopus 로고    scopus 로고
    • Magnetic field exposure enhances DNA repair through the induction of DnaK/J synthesis
    • Chow K., and Tung W.L. Magnetic field exposure enhances DNA repair through the induction of DnaK/J synthesis. FEBS Lett. 478 (2000) 133-136
    • (2000) FEBS Lett. , vol.478 , pp. 133-136
    • Chow, K.1    Tung, W.L.2
  • 4
    • 0035827709 scopus 로고    scopus 로고
    • Starvation promotes nuclear accumulation of the hsp70 Ssa4p in yeast cells
    • Chughtai Z.S., Rassadi R., Matusiewicz N., and Stochaj U. Starvation promotes nuclear accumulation of the hsp70 Ssa4p in yeast cells. J. Biol. Chem. 276 (2001) 20261-20266
    • (2001) J. Biol. Chem. , vol.276 , pp. 20261-20266
    • Chughtai, Z.S.1    Rassadi, R.2    Matusiewicz, N.3    Stochaj, U.4
  • 5
    • 0027300506 scopus 로고
    • Heat shock proteins: molecular chaperones of protein biogenesis
    • Craig E.A., Gambill B.D., and Nelson R.J. Heat shock proteins: molecular chaperones of protein biogenesis. Microbiol. Rev. 57 (1993) 402-414
    • (1993) Microbiol. Rev. , vol.57 , pp. 402-414
    • Craig, E.A.1    Gambill, B.D.2    Nelson, R.J.3
  • 6
    • 4544242205 scopus 로고    scopus 로고
    • Mechanisms of DNA damage recognition and strand discrimination in human nucleotide excision repair
    • Dip R., Camenisch U., and Naegeli H. Mechanisms of DNA damage recognition and strand discrimination in human nucleotide excision repair. DNA Repair (Amst) 3 (2004) 1409-1423
    • (2004) DNA Repair (Amst) , vol.3 , pp. 1409-1423
    • Dip, R.1    Camenisch, U.2    Naegeli, H.3
  • 7
    • 0028279371 scopus 로고
    • Regulation of heat shock protein synthesis by quercetin in human erythroleukaemia cells
    • Elia G., and Santoro M.G. Regulation of heat shock protein synthesis by quercetin in human erythroleukaemia cells. Biochem. J. 300 Pt 1 (1994) 201-209
    • (1994) Biochem. J. , vol.300 , Issue.PART 1 , pp. 201-209
    • Elia, G.1    Santoro, M.G.2
  • 8
    • 0030732132 scopus 로고    scopus 로고
    • Mechanism of open complex and dual incision formation by human nucleotide excision repair factors
    • Evans E., Moggs J.G., Hwang J.R., Egly J.M., and Wood R.D. Mechanism of open complex and dual incision formation by human nucleotide excision repair factors. EMBO J. 16 (1997) 6559-6573
    • (1997) EMBO J. , vol.16 , pp. 6559-6573
    • Evans, E.1    Moggs, J.G.2    Hwang, J.R.3    Egly, J.M.4    Wood, R.D.5
  • 9
    • 4344692138 scopus 로고    scopus 로고
    • In vitro study on role of Hsp70 expression in DNA damage of human embryonic lung cells exposed to benzo[a]pyrene
    • Gao Y.J., Xiao C.F., Chen S., Wang R.B., He H.Z., Tanguay R.M., and Wu T.C. In vitro study on role of Hsp70 expression in DNA damage of human embryonic lung cells exposed to benzo[a]pyrene. Biomed. Environ. Sci. 17 (2004) 144-152
    • (2004) Biomed. Environ. Sci. , vol.17 , pp. 144-152
    • Gao, Y.J.1    Xiao, C.F.2    Chen, S.3    Wang, R.B.4    He, H.Z.5    Tanguay, R.M.6    Wu, T.C.7
  • 10
    • 0027333423 scopus 로고
    • Role of the major heat shock proteins as molecular chaperones
    • Georgopoulos C., and Welch W.J. Role of the major heat shock proteins as molecular chaperones. Annu. Rev. Cell Biol. 9 (1993) 601-634
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 601-634
    • Georgopoulos, C.1    Welch, W.J.2
  • 11
    • 0027184721 scopus 로고
    • Molecular chaperone functions of heat-shock proteins
    • Hendrick J.P., and Hartl F.U. Molecular chaperone functions of heat-shock proteins. Annu. Rev. Biochem. 62 (1993) 349-384
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 349-384
    • Hendrick, J.P.1    Hartl, F.U.2
  • 12
    • 0025777354 scopus 로고
    • Heat shock, stress proteins, chaperones, and proteotoxicity
    • Hightower L.E. Heat shock, stress proteins, chaperones, and proteotoxicity. Cell 66 (1991) 191-197
    • (1991) Cell , vol.66 , pp. 191-197
    • Hightower, L.E.1
  • 13
    • 0035937744 scopus 로고    scopus 로고
    • Heat shock protein 70 binds to human apurinic/apyrimidinic endonuclease and stimulates endonuclease activity at abasic sites
    • Kenny M.K., Mendez F., Sandigursky M., Kureekattil R.P., Goldman J.D., Franklin W.A., and Bases R. Heat shock protein 70 binds to human apurinic/apyrimidinic endonuclease and stimulates endonuclease activity at abasic sites. J. Biol. Chem. 276 (2001) 9532-9536
    • (2001) J. Biol. Chem. , vol.276 , pp. 9532-9536
    • Kenny, M.K.1    Mendez, F.2    Sandigursky, M.3    Kureekattil, R.P.4    Goldman, J.D.5    Franklin, W.A.6    Bases, R.7
  • 19
    • 0020533372 scopus 로고
    • Revised methods for the Salmonella mutagenicity test
    • Maron D.M., and Ames B.N. Revised methods for the Salmonella mutagenicity test. Mutat. Res. 113 (1983) 173-215
    • (1983) Mutat. Res. , vol.113 , pp. 173-215
    • Maron, D.M.1    Ames, B.N.2
  • 20
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: cellular functions and molecular mechanism
    • Mayer M.P., and Bukau B. Hsp70 chaperones: cellular functions and molecular mechanism. Cell. Mol. Life Sci. 62 (2005) 670-684
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 22
    • 0042527130 scopus 로고    scopus 로고
    • Heat shock protein 70 stimulation of the deoxyribonucleic acid base excision repair enzyme polymerase beta
    • Mendez F., Kozin E., and Bases R. Heat shock protein 70 stimulation of the deoxyribonucleic acid base excision repair enzyme polymerase beta. Cell Stress Chaperones 8 (2003) 153-161
    • (2003) Cell Stress Chaperones , vol.8 , pp. 153-161
    • Mendez, F.1    Kozin, E.2    Bases, R.3
  • 23
    • 0026649409 scopus 로고
    • The translation machinery and 70 kD heat shock protein cooperate in protein synthesis
    • Nelson R.J., Ziegelhoffer T., Nicolet C., Werner-Washburne M., and Craig E.A. The translation machinery and 70 kD heat shock protein cooperate in protein synthesis. Cell 71 (1992) 97-105
    • (1992) Cell , vol.71 , pp. 97-105
    • Nelson, R.J.1    Ziegelhoffer, T.2    Nicolet, C.3    Werner-Washburne, M.4    Craig, E.A.5
  • 24
    • 33745330907 scopus 로고    scopus 로고
    • Overexpressed heat shock protein 70 protects cells against DNA damage caused by ultraviolet C in a dose-dependent manner
    • Niu P., Liu L., Gong Z., Tan H., Wang F., Yuan J., Feng Y., Wei Q., Tanguay R.M., and Wu T. Overexpressed heat shock protein 70 protects cells against DNA damage caused by ultraviolet C in a dose-dependent manner. Cell Stress Chaperones 11 (2006) 162-169
    • (2006) Cell Stress Chaperones , vol.11 , pp. 162-169
    • Niu, P.1    Liu, L.2    Gong, Z.3    Tan, H.4    Wang, F.5    Yuan, J.6    Feng, Y.7    Wei, Q.8    Tanguay, R.M.9    Wu, T.10
  • 25
    • 0028085556 scopus 로고
    • XPG endonuclease makes the 3' incision in human DNA nucleotide excision repair
    • O'Donovan A., Davies A.A., Moggs J.G., West S.C., and Wood R.D. XPG endonuclease makes the 3' incision in human DNA nucleotide excision repair. Nature 371 (1994) 432-435
    • (1994) Nature , vol.371 , pp. 432-435
    • O'Donovan, A.1    Davies, A.A.2    Moggs, J.G.3    West, S.C.4    Wood, R.D.5
  • 26
    • 0029095693 scopus 로고
    • Purification and characterization of the XPF-ERCC1 complex of human DNA repair excision nuclease
    • Park C.H., Bessho T., Matsunaga T., and Sancar A. Purification and characterization of the XPF-ERCC1 complex of human DNA repair excision nuclease. J. Biol. Chem. 270 (1995) 22657-22660
    • (1995) J. Biol. Chem. , vol.270 , pp. 22657-22660
    • Park, C.H.1    Bessho, T.2    Matsunaga, T.3    Sancar, A.4
  • 27
    • 14144254346 scopus 로고    scopus 로고
    • Individual susceptibility to occupational carcinogens: the evidence from biomonitoring and molecular epidemiology studies
    • Pavanello S., and Clonfero E. Individual susceptibility to occupational carcinogens: the evidence from biomonitoring and molecular epidemiology studies. G. Ital. Med. Lav. Ergon. 26 (2004) 311-321
    • (2004) G. Ital. Med. Lav. Ergon. , vol.26 , pp. 311-321
    • Pavanello, S.1    Clonfero, E.2
  • 30
    • 15844372318 scopus 로고    scopus 로고
    • ERCC1 expression is a predictor of survival in resected patients with non-small cell lung cancer
    • Simon G.R., Sharma S., Cantor A., Smith P., and Bepler G. ERCC1 expression is a predictor of survival in resected patients with non-small cell lung cancer. Chest 127 (2005) 978-983
    • (2005) Chest , vol.127 , pp. 978-983
    • Simon, G.R.1    Sharma, S.2    Cantor, A.3    Smith, P.4    Bepler, G.5
  • 31
    • 36048936637 scopus 로고    scopus 로고
    • Modulation of RAG/DNA complex by HSP70 in V(D)J recombination
    • Son Y.M., Lee J.H., and Kim D.R. Modulation of RAG/DNA complex by HSP70 in V(D)J recombination. Biochem. Biophys. Res. Commun. 365 (2008) 113-117
    • (2008) Biochem. Biophys. Res. Commun. , vol.365 , pp. 113-117
    • Son, Y.M.1    Lee, J.H.2    Kim, D.R.3
  • 32
    • 0028832880 scopus 로고
    • Reversible nucleolar translocation of Epstein-Barr virus-encoded EBNA-5 and hsp70 proteins after exposure to heat shock or cell density congestion
    • Szekely L., Jiang W.Q., Pokrovskaja K., Wiman K.G., Klein G., and Ringertz N. Reversible nucleolar translocation of Epstein-Barr virus-encoded EBNA-5 and hsp70 proteins after exposure to heat shock or cell density congestion. J. Gen. Virol. 76 Pt 10 (1995) 2423-2432
    • (1995) J. Gen. Virol. , vol.76 , Issue.PART 10 , pp. 2423-2432
    • Szekely, L.1    Jiang, W.Q.2    Pokrovskaja, K.3    Wiman, K.G.4    Klein, G.5    Ringertz, N.6
  • 33
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications
    • Towbin H., Staehelin T., and Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U.S.A. 76 (1979) 4350-4354
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 35
    • 0025775473 scopus 로고
    • Xeroderma pigmentosum complementation group C cells remove pyrimidine dimers selectively from the transcribed strand of active genes
    • Venema J., van Hoffen A., Karcagi V., Natarajan A.T., van Zeeland A.A., and Mullenders L.H. Xeroderma pigmentosum complementation group C cells remove pyrimidine dimers selectively from the transcribed strand of active genes. Mol. Cell. Biol. 11 (1991) 4128-4134
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 4128-4134
    • Venema, J.1    van Hoffen, A.2    Karcagi, V.3    Natarajan, A.T.4    van Zeeland, A.A.5    Mullenders, L.H.6
  • 37
    • 0029892791 scopus 로고    scopus 로고
    • DNA repair in eukaryotes
    • Wood R.D. DNA repair in eukaryotes. Annu. Rev. Biochem. 65 (1996) 135-167
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 135-167
    • Wood, R.D.1
  • 38
    • 0030337652 scopus 로고    scopus 로고
    • Presence of antibodies to heat stress proteins and its possible significance in workers exposed to high temperature and carbon monoxide
    • Wu T.C., Tanguay R.M., Wu Y., He H.Z., Xu D.G., Feng J.D., Shi W.X., and Zhang G.G. Presence of antibodies to heat stress proteins and its possible significance in workers exposed to high temperature and carbon monoxide. Biomed. Environ. Sci. 9 (1996) 370-379
    • (1996) Biomed. Environ. Sci. , vol.9 , pp. 370-379
    • Wu, T.C.1    Tanguay, R.M.2    Wu, Y.3    He, H.Z.4    Xu, D.G.5    Feng, J.D.6    Shi, W.X.7    Zhang, G.G.8
  • 40
    • 0036819192 scopus 로고    scopus 로고
    • Association of HSP70 and genotoxic damage in lymphocytes of workers exposed to coke-oven emission
    • Xiao C., Chen S., Li J., Hai T., Lu Q., Sun E., Wang R., Tanguay R.M., and Wu T. Association of HSP70 and genotoxic damage in lymphocytes of workers exposed to coke-oven emission. Cell Stress Chaperones 7 (2002) 396-402
    • (2002) Cell Stress Chaperones , vol.7 , pp. 396-402
    • Xiao, C.1    Chen, S.2    Li, J.3    Hai, T.4    Lu, Q.5    Sun, E.6    Wang, R.7    Tanguay, R.M.8    Wu, T.9
  • 41
    • 20444412643 scopus 로고    scopus 로고
    • Metabolic activation of polycyclic and heterocyclic aromatic hydrocarbons and DNA damage: a review
    • Xue W., and Warshawsky D. Metabolic activation of polycyclic and heterocyclic aromatic hydrocarbons and DNA damage: a review. Toxicol. Appl. Pharmacol. 206 (2005) 73-93
    • (2005) Toxicol. Appl. Pharmacol. , vol.206 , pp. 73-93
    • Xue, W.1    Warshawsky, D.2
  • 42
    • 0032557562 scopus 로고    scopus 로고
    • Involvement of molecular chaperonins in nucleotide excision repair. Dnak leads to increased thermal stability of UvrA, catalytic UvrB loading, enhanced repair, and increased UV resistance
    • Zou Y., Crowley D.J., and Van Houten B. Involvement of molecular chaperonins in nucleotide excision repair. Dnak leads to increased thermal stability of UvrA, catalytic UvrB loading, enhanced repair, and increased UV resistance. J. Biol. Chem. 273 (1998) 12887-12892
    • (1998) J. Biol. Chem. , vol.273 , pp. 12887-12892
    • Zou, Y.1    Crowley, D.J.2    Van Houten, B.3


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