메뉴 건너뛰기




Volumn 24, Issue 3, 2010, Pages 830-834

Acrylamide catalytically inhibits topoisomerase II in V79 cells

Author keywords

Acrylamide; Topoisomerase II; V79 cells

Indexed keywords

ACRYLAMIDE; DNA TOPOISOMERASE (ATP HYDROLYSING); KINETOPLAST DNA;

EID: 77649338945     PISSN: 08872333     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tiv.2009.12.010     Document Type: Article
Times cited : (19)

References (27)
  • 1
    • 12744272921 scopus 로고    scopus 로고
    • DNA adduction and mutagenic properties of acrylamide
    • Besaratinia A., and Pfeifer G.P. DNA adduction and mutagenic properties of acrylamide. Mutat. Res. 580 (2005) 31-40
    • (2005) Mutat. Res. , vol.580 , pp. 31-40
    • Besaratinia, A.1    Pfeifer, G.P.2
  • 2
    • 34047156621 scopus 로고    scopus 로고
    • A review of mechanisms of acrylamide carcinogenicity
    • Besaratinia A., and Pfeifer G.P. A review of mechanisms of acrylamide carcinogenicity. Carcinogenesis 28 (2007) 519-528
    • (2007) Carcinogenesis , vol.28 , pp. 519-528
    • Besaratinia, A.1    Pfeifer, G.P.2
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 33749828010 scopus 로고    scopus 로고
    • Genotoxicity and carcinogenicity of acrylamide: a critical review
    • Carere A. Genotoxicity and carcinogenicity of acrylamide: a critical review. Ann Ist Super Sanita. 42 (2006) 144-155
    • (2006) Ann Ist Super Sanita. , vol.42 , pp. 144-155
    • Carere, A.1
  • 6
    • 0032504157 scopus 로고    scopus 로고
    • Merbarone inhibits the catalytic activity of human topoisomerase IIa by blocking DNA cleavage
    • Fortune J.M., and Osheroff N. Merbarone inhibits the catalytic activity of human topoisomerase IIa by blocking DNA cleavage. J. Biol. Chem. 273 (1998) 17643-17650
    • (1998) J. Biol. Chem. , vol.273 , pp. 17643-17650
    • Fortune, J.M.1    Osheroff, N.2
  • 7
    • 0033628701 scopus 로고    scopus 로고
    • Topoisomerase II as a target for anticancer drugs: when enzymes stop being nice
    • Fortune J.M., and Osheroff N. Topoisomerase II as a target for anticancer drugs: when enzymes stop being nice. Prog. Nucleic Acid Res. Mol. Biol. 64 (2000) 221-253
    • (2000) Prog. Nucleic Acid Res. Mol. Biol. , vol.64 , pp. 221-253
    • Fortune, J.M.1    Osheroff, N.2
  • 8
    • 0041802954 scopus 로고    scopus 로고
    • Chemistry, biochemistry, and safety of acrylamide. A review
    • Friedman M. Chemistry, biochemistry, and safety of acrylamide. A review. J. Agric. Food Chem. 57 (2003) 4504-4526
    • (2003) J. Agric. Food Chem. , vol.57 , pp. 4504-4526
    • Friedman, M.1
  • 10
    • 12744258127 scopus 로고    scopus 로고
    • V79-hCYP2E1-hSULT1A1, a cell line for the sensitive detection of genotoxic effects induced by carbohydrate pyrolysis products and other food-borne chemicals
    • Glatt H., Schneider H., and Liu Y. V79-hCYP2E1-hSULT1A1, a cell line for the sensitive detection of genotoxic effects induced by carbohydrate pyrolysis products and other food-borne chemicals. Mutat. Res. 580 (2005) 41-52
    • (2005) Mutat. Res. , vol.580 , pp. 41-52
    • Glatt, H.1    Schneider, H.2    Liu, Y.3
  • 11
    • 20144362708 scopus 로고    scopus 로고
    • Biochemical and proteomics approaches to characterize topoisomerase IIα cysteines and DNA as targets responsible for cisplatin-induced inhibition of topoisomerase IIα
    • Hasinoff B.B., Wu X., Krokhin O.V., Ens W., Standing K.G., Nitiss L., Sivaram T., Giorgianni A., Yang S., Jiang Y., and Yalowich J.C. Biochemical and proteomics approaches to characterize topoisomerase IIα cysteines and DNA as targets responsible for cisplatin-induced inhibition of topoisomerase IIα. Mol. Pharmacol. 67 (2005) 937-947
    • (2005) Mol. Pharmacol. , vol.67 , pp. 937-947
    • Hasinoff, B.B.1    Wu, X.2    Krokhin, O.V.3    Ens, W.4    Standing, K.G.5    Nitiss, L.6    Sivaram, T.7    Giorgianni, A.8    Yang, S.9    Jiang, Y.10    Yalowich, J.C.11
  • 12
    • 0028589882 scopus 로고
    • IARC International Agency for Research on Cancer, International Agency for Research on Cancer, Lyon, France
    • IARC (International Agency for Research on Cancer), 1994. IARC Monographs on the Evaluation of Carcinogen Risks to Humans: Some Industrial Chemicals. International Agency for Research on Cancer, Lyon, France 60, 389-433.
    • (1994) IARC Monographs on the Evaluation of Carcinogen Risks to Humans: Some Industrial Chemicals , vol.60 , pp. 389-433
  • 16
    • 0025298540 scopus 로고
    • Antagonistic effect of aclarubicin on the cytotoxixity of etoposide and 4′-(9-acridinylamino) methanesulfon-m-anisidide in human small cell lung cancer cell lines and on topoisomerase II-mediated DNA cleavage
    • Jensen P.B., Sorensen B.S., Demant E.J., Sehested M., Jensen P.S., Vindelov L., and Hansen H.H. Antagonistic effect of aclarubicin on the cytotoxixity of etoposide and 4′-(9-acridinylamino) methanesulfon-m-anisidide in human small cell lung cancer cell lines and on topoisomerase II-mediated DNA cleavage. Cancer Res. 50 (1990) 3311-3316
    • (1990) Cancer Res. , vol.50 , pp. 3311-3316
    • Jensen, P.B.1    Sorensen, B.S.2    Demant, E.J.3    Sehested, M.4    Jensen, P.S.5    Vindelov, L.6    Hansen, H.H.7
  • 17
    • 0021353424 scopus 로고
    • Effects of acrylamide and some other sulfhydryl reagents on spontaneous and pathologically induced terminal sprouting from motor end-plates
    • Kemplay S., and Cavanagh J.B. Effects of acrylamide and some other sulfhydryl reagents on spontaneous and pathologically induced terminal sprouting from motor end-plates. Muscle Nerve 7 (1984) 94-100
    • (1984) Muscle Nerve , vol.7 , pp. 94-100
    • Kemplay, S.1    Cavanagh, J.B.2
  • 20
    • 12744259430 scopus 로고    scopus 로고
    • DNA strand breaking capacity of acrylamide and glycidamide in mammalian cells
    • Puppel N., Tjaden Z., Fuellear F., and Marko D. DNA strand breaking capacity of acrylamide and glycidamide in mammalian cells. Mutat. Res. 580 (2005) 71-80
    • (2005) Mutat. Res. , vol.580 , pp. 71-80
    • Puppel, N.1    Tjaden, Z.2    Fuellear, F.3    Marko, D.4
  • 21
    • 12744279172 scopus 로고    scopus 로고
    • The carcinogeneity of acrylamide
    • Rice J. The carcinogeneity of acrylamide. Mutat. Res. 580 (2005) 3-20
    • (2005) Mutat. Res. , vol.580 , pp. 3-20
    • Rice, J.1
  • 22
    • 0032054222 scopus 로고    scopus 로고
    • Chinese hamster ovary cells resistant to the topoisomerase II catalytic inhibitor ICRF-159: a Tyr49Phe mutation confers high-level resistance to bisdioxopiperazines
    • Sehested M., Wessel I., Jensen L.H., Holm B., Oliveri R.S., Kenwrick S., Creigthon A.M., Nitiss J.L., and Jensen P.B. Chinese hamster ovary cells resistant to the topoisomerase II catalytic inhibitor ICRF-159: a Tyr49Phe mutation confers high-level resistance to bisdioxopiperazines. Cancer Res. 58 (1998) 1460-1468
    • (1998) Cancer Res. , vol.58 , pp. 1460-1468
    • Sehested, M.1    Wessel, I.2    Jensen, L.H.3    Holm, B.4    Oliveri, R.S.5    Kenwrick, S.6    Creigthon, A.M.7    Nitiss, J.L.8    Jensen, P.B.9
  • 24
    • 0027457104 scopus 로고
    • Acrylamide: induction of DNA damage, chromosomal aberrations and cell transformation without gene mutations
    • Tsuda H., Shimizu C.S., Taketomi M.K., Hasegawa M.M., Hamada A., Kawata K.M., and Inui N. Acrylamide: induction of DNA damage, chromosomal aberrations and cell transformation without gene mutations. Mutagenesis 8 (1993) 23-29
    • (1993) Mutagenesis , vol.8 , pp. 23-29
    • Tsuda, H.1    Shimizu, C.S.2    Taketomi, M.K.3    Hasegawa, M.M.4    Hamada, A.5    Kawata, K.M.6    Inui, N.7
  • 25
    • 0035916938 scopus 로고    scopus 로고
    • Stimulation of topoisomerase II-mediated DNA damage via a mechanism involving protein thiolation
    • Wang H., Mao Y., Chen A.Y., Zhou N., LaVoie E.J., and Liu L.F. Stimulation of topoisomerase II-mediated DNA damage via a mechanism involving protein thiolation. Biochemistry 40 (2001) 3316-3323
    • (2001) Biochemistry , vol.40 , pp. 3316-3323
    • Wang, H.1    Mao, Y.2    Chen, A.Y.3    Zhou, N.4    LaVoie, E.J.5    Liu, L.F.6
  • 26
    • 0022340168 scopus 로고
    • Identification of DNA topoisomerase II as an intracellular target of antitumor epipodophyllotoxins in simian virus 40-infected monkey cells
    • Yang L., Rowe T.C., and Liu L.F. Identification of DNA topoisomerase II as an intracellular target of antitumor epipodophyllotoxins in simian virus 40-infected monkey cells. Cancer Res. 45 (1985) 5872-5876
    • (1985) Cancer Res. , vol.45 , pp. 5872-5876
    • Yang, L.1    Rowe, T.C.2    Liu, L.F.3
  • 27
    • 65049086069 scopus 로고    scopus 로고
    • Protective effect of hydroxytyrosol against acrylamide-induced cytotoxicity and DNA damage in HepG2 cells
    • Zhang X., Cao J., Jiang L., Geng C., and Zhong L. Protective effect of hydroxytyrosol against acrylamide-induced cytotoxicity and DNA damage in HepG2 cells. Mutat. Res. 664 (2009) 64-68
    • (2009) Mutat. Res. , vol.664 , pp. 64-68
    • Zhang, X.1    Cao, J.2    Jiang, L.3    Geng, C.4    Zhong, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.