메뉴 건너뛰기




Volumn 12, Issue 4, 1999, Pages 337-346

Molecular alchemy of the tumor suppressor protein p53: Metals and cell growth control

Author keywords

Cadmium; Cancer; Cell cycle; Oxidation reduction

Indexed keywords

CADMIUM; METAL; METAL CHELATE; PROTEIN P53; TRANSCRIPTION FACTOR; ZINC;

EID: 1642602482     PISSN: 0896548X     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1520-670X(1999)12:4<337::AID-JTRA7>3.0.CO;2-J     Document Type: Conference Paper
Times cited : (3)

References (41)
  • 2
    • 0030667702 scopus 로고    scopus 로고
    • DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
    • Shieh SY, Ikeda M, Taya Y, Prives C. DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2. Cell 1997;91:325-334.
    • (1997) Cell , vol.91 , pp. 325-334
    • Shieh, S.Y.1    Ikeda, M.2    Taya, Y.3    Prives, C.4
  • 3
    • 0032514485 scopus 로고    scopus 로고
    • DNA-dependent protein kinase acts upstream of p53 in response to DNA damage
    • Woo RA, McLure KG, Lees-Miller SP, Rancourt DE, Lee PW. DNA-dependent protein kinase acts upstream of p53 in response to DNA damage. Nature 1998;394:700-704.
    • (1998) Nature , vol.394 , pp. 700-704
    • Woo, R.A.1    McLure, K.G.2    Lees-Miller, S.P.3    Rancourt, D.E.4    Lee, P.W.5
  • 4
    • 0033992478 scopus 로고    scopus 로고
    • p53 and human cancer: The first ten thousand mutations
    • Hainaut P, Hollstein M. p53 and human cancer: the first ten thousand mutations. Adv Cancer Res 1999;77:81-137.
    • (1999) Adv Cancer Res , vol.77 , pp. 81-137
    • Hainaut, P.1    Hollstein, M.2
  • 6
    • 0031971228 scopus 로고    scopus 로고
    • Multisite phosphorylation and the integration of stress signals at p53
    • Meek DW. Multisite phosphorylation and the integration of stress signals at p53. Cell Signal 1998; 10:159-166.
    • (1998) Cell Signal , vol.10 , pp. 159-166
    • Meek, D.W.1
  • 7
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt Y, Maya R, Kazaz A, Oren M. Mdm2 promotes the rapid degradation of p53. Nature 1997;387: 296-299.
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 8
    • 0030965946 scopus 로고    scopus 로고
    • Regulation of p53 stability by Mdm2
    • Kubbutat MH, Jones SN, Vousden, KH. Regulation of p53 stability by Mdm2. Nature 1997;387: 299-303.
    • (1997) Nature , vol.387 , pp. 299-303
    • Kubbutat, M.H.1    Jones, S.N.2    Vousden, K.H.3
  • 9
    • 0027250493 scopus 로고
    • Activation of the cryptic DNA binding function of mutant forms of p53
    • Hupp TR, Meek DW, Midgley CA, Lane DP. Activation of the cryptic DNA binding function of mutant forms of p53. Nucleic Acids Res 1993;21:3167-174.
    • (1993) Nucleic Acids Res , vol.21 , pp. 3167-3174
    • Hupp, T.R.1    Meek, D.W.2    Midgley, C.A.3    Lane, D.P.4
  • 10
    • 0029972806 scopus 로고    scopus 로고
    • p53: Puzzle and paradigm
    • Ko LJ, Prives C. p53: puzzle and paradigm. Genes Dev 1996;10:1054-1072.
    • (1996) Genes Dev , vol.10 , pp. 1054-1072
    • Ko, L.J.1    Prives, C.2
  • 11
    • 0027361046 scopus 로고
    • Redox modulation of p53 conformation and sequence-specific DNA binding in vitro
    • Hainaut P, Milner J. Redox modulation of p53 conformation and sequence-specific DNA binding in vitro. Cancer Res 1993;53:4469-4473.
    • (1993) Cancer Res , vol.53 , pp. 4469-4473
    • Hainaut, P.1    Milner, J.2
  • 14
    • 0028877982 scopus 로고    scopus 로고
    • Flexibility: The key to p53 function?
    • Milner J. Flexibility: the key to p53 function? Trends Biochem Sci 20:49-51.
    • Trends Biochem Sci , vol.20 , pp. 49-51
    • Milner, J.1
  • 16
    • 0032541325 scopus 로고    scopus 로고
    • The requirement for the p53 proline-rich functional domain for mediation of apoptosis is correlated with specific PIG3 gene transactivation and with transcriptional repression
    • Venot C, Maratrat M, Dureuil C, Conseiller E, Bracco L, Debussche L. The requirement for the p53 proline-rich functional domain for mediation of apoptosis is correlated with specific PIG3 gene transactivation and with transcriptional repression. EMBO J 1998;17:4668-4679.
    • (1998) EMBO J , vol.17 , pp. 4668-4679
    • Venot, C.1    Maratrat, M.2    Dureuil, C.3    Conseiller, E.4    Bracco, L.5    Debussche, L.6
  • 17
    • 0027109075 scopus 로고
    • Cancer: p53, guardian of the genome
    • Lane DP. Cancer: p53, guardian of the genome. Nature 1992;358:15-16.
    • (1992) Nature , vol.358 , pp. 15-16
    • Lane, D.P.1
  • 19
    • 0030011897 scopus 로고    scopus 로고
    • New insights into p53 function from structural studies
    • Arrowsmith CH, Morin P. New insights into p53 function from structural studies. Oncogene 1996; 12:1379-1385.
    • (1996) Oncogene , vol.12 , pp. 1379-1385
    • Arrowsmith, C.H.1    Morin, P.2
  • 21
    • 0027983669 scopus 로고
    • Crystal structure of a p53 tumor suppressor-DNA complex: Understanding tumorigenic mutations
    • Cho Y, Gorina S, Jeffrey PD, Pavletich NP. Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations. Science 1994;265:346-355.
    • (1994) Science , vol.265 , pp. 346-355
    • Cho, Y.1    Gorina, S.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 22
    • 0027183546 scopus 로고
    • Transition metals in control of gene expression
    • O'Halloran TV. Transition metals in control of gene expression. Science 1993;261:715-725.
    • (1993) Science , vol.261 , pp. 715-725
    • O'Halloran, T.V.1
  • 23
    • 0027269545 scopus 로고
    • A structural role for metal ions in the "wild-type" conformation of the tumor suppressor protein p53
    • Hainaut P, Milner J. A structural role for metal ions in the "wild-type" conformation of the tumor suppressor protein p53. Cancer Res 1993;53:1739-1742.
    • (1993) Cancer Res , vol.53 , pp. 1739-1742
    • Hainaut, P.1    Milner, J.2
  • 24
    • 0027771333 scopus 로고
    • The DNA-binding domain of p53 contains the four conserved regions and the major mutation hot spots
    • Pavletich NP, Chambers KA, Pabo CO. The DNA-binding domain of p53 contains the four conserved regions and the major mutation hot spots. Genes Dev 1993;7:2556-2564.
    • (1993) Genes Dev , vol.7 , pp. 2556-2564
    • Pavletich, N.P.1    Chambers, K.A.2    Pabo, C.O.3
  • 25
    • 0028016446 scopus 로고
    • Characterization of baculovirus recombinant wild-type p53. Dimerization of p53 is required for high-affinity DNA binding and cysteine oxidation inhibits p53 DNA binding
    • Delphin C, Cahen, P, Lawrence JJ, Baudier J. Characterization of baculovirus recombinant wild-type p53. Dimerization of p53 is required for high-affinity DNA binding and cysteine oxidation inhibits p53 DNA binding. Eur J Biochem 1994;223:683-692.
    • (1994) Eur J Biochem , vol.223 , pp. 683-692
    • Delphin, C.1    Cahen, P.2    Lawrence, J.J.3    Baudier, J.4
  • 26
    • 0028830748 scopus 로고
    • Modulation by copper of p53 conformation and sequence-specific DNA binding: Role for Cu(II)/Cu(I) redox mechanism
    • Hainaut P, Rolley N, Davies M, Milner J. Modulation by copper of p53 conformation and sequence-specific DNA binding: role for Cu(II)/Cu(I) redox mechanism. Oncogene 1995;10:27-32.
    • (1995) Oncogene , vol.10 , pp. 27-32
    • Hainaut, P.1    Rolley, N.2    Davies, M.3    Milner, J.4
  • 27
    • 0031978026 scopus 로고    scopus 로고
    • Modulation of p53 protein conformation and DNA-binding activity by intracellular chelation of zinc
    • Verhaegh GW, Parat MO, Richard M.J, Hainaut P. Modulation of p53 protein conformation and DNA-binding activity by intracellular chelation of zinc. Mol Carcinog 1998;21:205-214.
    • (1998) Mol Carcinog , vol.21 , pp. 205-214
    • Verhaegh, G.W.1    Parat, M.O.2    Richard, M.J.3    Hainaut, P.4
  • 28
    • 0026779422 scopus 로고
    • Interaction of heat-shock protein 70 with p53 translated in vitro: Evidence for interaction with dimeric p53 and for a role in the regulation of p53 conformation
    • Hainaut P, Milner J. Interaction of heat-shock protein 70 with p53 translated in vitro: evidence for interaction with dimeric p53 and for a role in the regulation of p53 conformation. EMBO J 1992; 11:3513-3520.
    • (1992) EMBO J , vol.11 , pp. 3513-3520
    • Hainaut, P.1    Milner, J.2
  • 29
    • 0030764172 scopus 로고    scopus 로고
    • Regulation of p53 by metal ions and by antioxidants: Dithiocarbamate down-regulates p53 DNA-binding activity by increasing the intracellular level of copper
    • Verhaegh GW, Richard MJ, Hainaut, P. Regulation of p53 by metal ions and by antioxidants: dithiocarbamate down-regulates p53 DNA-binding activity by increasing the intracellular level of copper. Mol Cell Biol 1997;17:5699-5706.
    • (1997) Mol Cell Biol , vol.17 , pp. 5699-5706
    • Verhaegh, G.W.1    Richard, M.J.2    Hainaut, P.3
  • 30
    • 0032563191 scopus 로고    scopus 로고
    • Pyrrolidine dithiocarbamate prevents p53 activation and promotes p53 cysteine residue oxidation
    • Wu HH, Momand J. Pyrrolidine dithiocarbamate prevents p53 activation and promotes p53 cysteine residue oxidation. J Biol Chem 1998;273:18898-18905.
    • (1998) J Biol Chem , vol.273 , pp. 18898-18905
    • Wu, H.H.1    Momand, J.2
  • 31
    • 0000349342 scopus 로고    scopus 로고
    • Cadmium, Mercury and exposures in the glass manufacturing industry
    • International Agency for Cancer Research Beryllium, Cadmium, Mercury and exposures in the glass manufacturing industry. IARC Monographs on the Evaluation of Carcinogenic Risks 1998;58: pp. 119-237.
    • (1998) IARC Monographs on the Evaluation of Carcinogenic Risks , vol.58 , pp. 119-237
  • 32
    • 0039136305 scopus 로고    scopus 로고
    • Cadmium induces conformational modifications of Wild-type p53 and suppresses p53 response to DNA damage in intact cells
    • in press
    • Meplan C, Mann K, Hainaut P. Cadmium induces conformational modifications of Wild-type p53 and suppresses p53 response to DNA damage in intact cells. J Biol Chem 1999 (in press).
    • (1999) J Biol Chem
    • Meplan, C.1    Mann, K.2    Hainaut, P.3
  • 33
    • 0030808955 scopus 로고    scopus 로고
    • Nitric oxide induces conformational and functional modifications of wild-type p53 tumor suppressor protein
    • Calmels S, Hainaut P, Ohshima H. Nitric oxide induces conformational and functional modifications of wild-type p53 tumor suppressor protein. Cancer Res 1997;57:3365-3369.
    • (1997) Cancer Res , vol.57 , pp. 3365-3369
    • Calmels, S.1    Hainaut, P.2    Ohshima, H.3
  • 34
    • 0029866646 scopus 로고    scopus 로고
    • The galvanization of biology: A growing appreciation for the roles of zinc
    • Berg JM, Shi Y. The galvanization of biology: a growing appreciation for the roles of zinc. Science 1996;271:1081-1085.
    • (1996) Science , vol.271 , pp. 1081-1085
    • Berg, J.M.1    Shi, Y.2
  • 35
    • 0026410002 scopus 로고
    • Structural aspects of metal liganding to functional groups in proteins
    • Glusker JP. Structural aspects of metal liganding to functional groups in proteins. Adv Protein Chem 1991;42:1-76.
    • (1991) Adv Protein Chem , vol.42 , pp. 1-76
    • Glusker, J.P.1
  • 36
    • 0026353521 scopus 로고
    • Overview of metallothionein
    • Kagi JH. Overview of metallothionein. Methods Enzymol 1991;205:613-626.
    • (1991) Methods Enzymol , vol.205 , pp. 613-626
    • Kagi, J.H.1
  • 37
    • 0028836796 scopus 로고
    • Cell cycle regulation of metallothionein in human colonie cancer cells
    • Nagel WW, Vallee, BL. Cell cycle regulation of metallothionein in human colonie cancer cells. Proc Natl Acad Sci USA 1995;92:579-583.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 579-583
    • Nagel, W.W.1    Vallee, B.L.2
  • 38
    • 0031424866 scopus 로고    scopus 로고
    • Induction and repair inhibition of oxidative DNA damage by nickel(II) and cadmium(II) in mammalian cells
    • Dally H, Hartwig A. Induction and repair inhibition of oxidative DNA damage by nickel(II) and cadmium(II) in mammalian cells. Carcinogenesis 1997;18:1021-1026.
    • (1997) Carcinogenesis , vol.18 , pp. 1021-1026
    • Dally, H.1    Hartwig, A.2
  • 39
    • 0028001088 scopus 로고
    • The LEC rat has a deletion in the copper transporting ATPase gene homologous to the Wilson disease gene
    • Wu J, Forbes JR, Chen HS, Cox, DW. The LEC rat has a deletion in the copper transporting ATPase gene homologous to the Wilson disease gene. Nature Genet 1994;7:541-545.
    • (1994) Nature Genet , vol.7 , pp. 541-545
    • Wu, J.1    Forbes, J.R.2    Chen, H.S.3    Cox, D.W.4
  • 40
    • 0029833470 scopus 로고    scopus 로고
    • Cell proliferation and esophageal carcinogenesis in the zinc-deficient rat
    • Fong LY, Li JX, Farber JL, Magee PN. Cell proliferation and esophageal carcinogenesis in the zinc-deficient rat. Carcinogenesis 1996;17:1841-1848.
    • (1996) Carcinogenesis , vol.17 , pp. 1841-1848
    • Fong, L.Y.1    Li, J.X.2    Farber, J.L.3    Magee, P.N.4
  • 41
    • 0021849078 scopus 로고
    • No effect of riboflavine, retinol, and zinc on prevalence of precancerous lesions of oesophagus: Randomised double-blind intervention study in high-risk population of China
    • Muñoz N, Wahrendorf J , Bang LJ, Crespi M, Thurnham DI, Day NE, Ji ZH, Grassi A, Yan LW, Lin LG. No effect of riboflavine, retinol, and zinc on prevalence of precancerous lesions of oesophagus: randomised double-blind intervention study in high-risk population of China. Lancet 1985;2:111-114.
    • (1985) Lancet , vol.2 , pp. 111-114
    • Muñoz, N.1    Wahrendorf, J.2    Bang, L.J.3    Crespi, M.4    Thurnham, D.I.5    Day, N.E.6    Ji, Z.H.7    Grassi, A.8    Yan, L.W.9    Lin, L.G.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.