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Volumn 255, Issue 1-2, 2004, Pages 227-237

Vanadate activated Akt and promoted S phase entry

Author keywords

Akt; Cell cycle regulation; E2F1; PI3k; pRb; Vanadate

Indexed keywords

CYCLIN A; CYCLIN E; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE B; PROTEIN KINASE INHIBITOR; RETINOBLASTOMA PROTEIN; SERINE; THREONINE; TRANSCRIPTION FACTOR E2F; TRANSCRIPTION FACTOR E2F1; VANADIC ACID;

EID: 0742324105     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:MCBI.0000007278.27936.8b     Document Type: Review
Times cited : (33)

References (46)
  • 2
    • 0032189381 scopus 로고    scopus 로고
    • Protein kinase B (c-Akt): A multifunctional mediator of phosphatidylinositol 3-kinase activation
    • Coffer PJ, Jin J, Woodgett JR: Protein kinase B (c-Akt): A multifunctional mediator of phosphatidylinositol 3-kinase activation. Biochem J 335: 1-13, 1998
    • (1998) Biochem. J. , vol.335 , pp. 1-13
    • Coffer, P.J.1    Jin, J.2    Woodgett, J.R.3
  • 4
    • 0035902180 scopus 로고    scopus 로고
    • Oncogenic kinase signalling
    • Blume-Jensen P, Hunter T: Oncogenic kinase signalling. Nature 411: 355-365, 2001
    • (2001) Nature , vol.411 , pp. 355-365
    • Blume-Jensen, P.1    Hunter, T.2
  • 5
    • 0031433335 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase couples the interleukin-2 receptor to the cell cycle regulator E2F
    • Brennan P, Babbage JW, Burgering BM, Groner B, Reif K, Cantrell DA: Phosphatidylinositol 3-kinase couples the interleukin-2 receptor to the cell cycle regulator E2F. Immunity 7: 679-689, 1997
    • (1997) Immunity , vol.7 , pp. 679-689
    • Brennan, P.1    Babbage, J.W.2    Burgering, B.M.3    Groner, B.4    Reif, K.5    Cantrell, D.A.6
  • 6
    • 0032146274 scopus 로고    scopus 로고
    • The regulation of E2F by pRB-family proteins
    • Dyson N: The regulation of E2F by pRB-family proteins. Genes Dev 12: 2245-2262, 1998
    • (1998) Genes Dev. , vol.12 , pp. 2245-2262
    • Dyson, N.1
  • 7
    • 0029033861 scopus 로고
    • The retinoblastoma protein and cell cycle control
    • Weinberg RA: The retinoblastoma protein and cell cycle control. Cell 81: 323-330, 1995
    • (1995) Cell , vol.81 , pp. 323-330
    • Weinberg, R.A.1
  • 8
    • 0026636908 scopus 로고
    • Retinoblastoma protein switches the E2F site from positive to negative element
    • Weintraub SJ, Prater CA, Dean DC: Retinoblastoma protein switches the E2F site from positive to negative element. Nature 358: 259-261, 1992
    • (1992) Nature , vol.358 , pp. 259-261
    • Weintraub, S.J.1    Prater, C.A.2    Dean, D.C.3
  • 9
    • 0035092886 scopus 로고    scopus 로고
    • DNA replication control through interaction of E2F-RB and the origin recognition complex
    • Bosco G, Du W, Orr-Weaver TL: DNA replication control through interaction of E2F-RB and the origin recognition complex. Nat Cell Biol, 3: 289-295, 2001
    • (2001) Nat. Cell Biol. , vol.3 , pp. 289-295
    • Bosco, G.1    Du, W.2    Orr-Weaver, T.L.3
  • 10
    • 0029849620 scopus 로고    scopus 로고
    • Cancer cell cycles
    • Sherr CJ: Cancer cell cycles. Science 274: 1672-1677, 1996
    • (1996) Science , vol.274 , pp. 1672-1677
    • Sherr, C.J.1
  • 11
    • 0019168397 scopus 로고
    • Vanadate enhances the stimulatory action of insurin on DNA synthesis in cultured mouse mammary glands
    • Hori CaO T: Vanadate enhances the stimulatory action of insurin on DNA synthesis in cultured mouse mammary glands. Biochim Biophys Acta 610: 235-240, 1987
    • (1987) Biochim. Biophys. Acta , vol.610 , pp. 235-240
    • Hori Cao, T.1
  • 12
    • 0023050755 scopus 로고
    • Vanadyl (IV) and vanadate (V) binding to selected endogenous phosphate, carboxyl, and amino ligands; calculations of cellular vanadium species distribution
    • Nechay BR, Nanninga LB, Nechay PS: Vanadyl (IV) and vanadate (V) binding to selected endogenous phosphate, carboxyl, and amino ligands; calculations of cellular vanadium species distribution. Arch Biochem Biophys 251: 128-138, 1986
    • (1986) Arch. Biochem. Biophys. , vol.251 , pp. 128-138
    • Nechay, B.R.1    Nanninga, L.B.2    Nechay, P.S.3
  • 13
    • 0026090587 scopus 로고
    • Cellular retention, cytotoxicity and morphological transformation by vanadium(IV) and vanadium(V) in BALB/3T3 cell lines
    • Sabbioni E, Pozzi G, Pintar A, Casella L, Garattini S: Cellular retention, cytotoxicity and morphological transformation by vanadium(IV) and vanadium(V) in BALB/3T3 cell lines. Carcinogenesis 12: 47-52, 1991
    • (1991) Carcinogenesis , vol.12 , pp. 47-52
    • Sabbioni, E.1    Pozzi, G.2    Pintar, A.3    Casella, L.4    Garattini, S.5
  • 14
    • 0019822952 scopus 로고
    • Vanadate, epidermal growth factor and the stimulation of DNA synthesis
    • Carpenter G: Vanadate, epidermal growth factor and the stimulation of DNA synthesis. Biochem Biophys Res Commun 102: 1115-1121, 1981
    • (1981) Biochem. Biophys. Res. Commun. , vol.102 , pp. 1115-1121
    • Carpenter, G.1
  • 15
    • 0014187105 scopus 로고
    • Relationship between air pollution and certain chronic disease death rates. Multivariate statistical studies
    • Hickey RJ, Schoff EP, Clelland RC: Relationship between air pollution and certain chronic disease death rates. Multivariate statistical studies. Arch Environ Health 15: 728-738, 1967
    • (1967) Arch. Environ. Health , vol.15 , pp. 728-738
    • Hickey, R.J.1    Schoff, E.P.2    Clelland, R.C.3
  • 16
    • 0028157138 scopus 로고
    • Mutagenicity, carcinogenicity and teratogenicity of vanadium compounds
    • Leonard A, Gerber GB: Mutagenicity, carcinogenicity and teratogenicity of vanadium compounds. Mutat Res 317: 81-88, 1994
    • (1994) Mutat. Res. , vol.317 , pp. 81-88
    • Leonard, A.1    Gerber, G.B.2
  • 17
    • 84966153013 scopus 로고
    • On the relations between atmospheric pollution in urban and rural location and mortality from cancer, bronchitis, pneumonia, with particular reference to 3,4-benzopyrene, beryllium, molybdenum, vanadium and arsenic
    • Stock P: On the relations between atmospheric pollution in urban and rural location and mortality from cancer, bronchitis, pneumonia, with particular reference to 3,4-benzopyrene, beryllium, molybdenum, vanadium and arsenic. Br J Cancer 14: 397-418, 1965
    • (1965) Br. J. Cancer , vol.14 , pp. 397-418
    • Stock, P.1
  • 18
    • 0028065965 scopus 로고
    • Genotoxicity of vanadium pentoxide in Chinese hamster V79 cells
    • Zhong BZ, Gu ZW, Wallace WE, Whong WZ, Ong T: Genotoxicity of vanadium pentoxide in Chinese hamster V79 cells. Mutat Res 321: 35-42, 1994
    • (1994) Mutat. Res. , vol.321 , pp. 35-42
    • Zhong, B.Z.1    Gu, Z.W.2    Wallace, W.E.3    Whong, W.Z.4    Ong, T.5
  • 20
    • 0037051786 scopus 로고    scopus 로고
    • Vanadate-induced cell growth arrest is p53-dependent through activation of p21 in C141 cells
    • Zhang Z, Huang C, Li J, Shi X: Vanadate-induced cell growth arrest is p53-dependent through activation of p21 in C141 cells. J Inorg Biochem 89: 142-148, 2002
    • (2002) J. Inorg. Biochem. , vol.89 , pp. 142-148
    • Zhang, Z.1    Huang, C.2    Li, J.3    Shi, X.4
  • 21
    • 0025726216 scopus 로고
    • A rapid and simple method for measuring thymocyte apoptosis by propidium iodide staining and flow cytometry
    • Nicoletti I, Migliorati G, Pagliacci MC, Grignani F, Riccardi C: A rapid and simple method for measuring thymocyte apoptosis by propidium iodide staining and flow cytometry. J Immunol Methods 139: 271-279, 1991
    • (1991) J. Immunol. Methods , vol.139 , pp. 271-279
    • Nicoletti, I.1    Migliorati, G.2    Pagliacci, M.C.3    Grignani, F.4    Riccardi, C.5
  • 22
    • 0028036487 scopus 로고
    • Methods for the detection of apoptosis
    • Sgonic Raw G: Methods for the detection of apoptosis. Int Arch Allergy Immunol 105: 327-332, 1994
    • (1994) Int. Arch. Allergy Immunol. , vol.105 , pp. 327-332
    • Sgonic Raw, G.1
  • 23
    • 0027572351 scopus 로고
    • Vanadium as a modulator of cellular regulatory cascades and oncogene expression
    • Stern A, Yin X, Tsang SS, Davison A, Moon J: Vanadium as a modulator of cellular regulatory cascades and oncogene expression. Biochem Cell Biol 71: 103-112, 1993
    • (1993) Biochem. Cell Biol. , vol.71 , pp. 103-112
    • Stern, A.1    Yin, X.2    Tsang, S.S.3    Davison, A.4    Moon, J.5
  • 24
    • 0029558183 scopus 로고
    • In vitro and in vivo antineoplastic effects of orthovanadate
    • Cruz TF, Morgan A, Min W: In vitro and in vivo antineoplastic effects of orthovanadate. Mol Cell Biochem 153: 161-166, 1995
    • (1995) Mol. Cell Biochem. , vol.153 , pp. 161-166
    • Cruz, T.F.1    Morgan, A.2    Min, W.3
  • 25
    • 0032961422 scopus 로고    scopus 로고
    • Cell cycle control, checkpoint mechanisms, and genotoxic stress
    • Shackelford RE, Kaufmann WK, Paules RS: (1999) Cell cycle control, checkpoint mechanisms, and genotoxic stress. Environ Health Perspect 107 (suppl 1): 5-24.
    • (1999) Environ. Health Perspect. , vol.107 , Issue.SUPPL. 1 , pp. 5-24
    • Shackelford, R.E.1    Kaufmann, W.K.2    Paules, R.S.3
  • 28
    • 0032881288 scopus 로고    scopus 로고
    • AKT/PKB and other D3 phosphoinositide-regulated kinases: Kinase activation by phosphoinositide-dependent phosphorylation
    • Chan TO, Rittenhouse SE, Tsichlis PN: AKT/PKB and other D3 phosphoinositide-regulated kinases: Kinase activation by phosphoinositide-dependent phosphorylation. Annu Rev Biochem 68: 965-1014, 1999
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 965-1014
    • Chan, T.O.1    Rittenhouse, S.E.2    Tsichlis, P.N.3
  • 29
    • 0030943057 scopus 로고    scopus 로고
    • cAMP stimulates protein kinase B in a Wortmannin-insensitive manner
    • Sable CL, Filippa N, Hemmings B, Van Obberghen E: cAMP stimulates protein kinase B in a Wortmannin-insensitive manner. FEBS Lett 409: 253-257, 1997
    • (1997) FEBS Lett. , vol.409 , pp. 253-257
    • Sable, C.L.1    Filippa, N.2    Hemmings, B.3    Van Obberghen, E.4
  • 30
    • 0030785701 scopus 로고    scopus 로고
    • Activation of protein kinase B (Akt/RAC-protein kinase) by cellular stress and its association with heat shock protein Hsp27
    • Konishi H, Matsuzaki H, Tanaka M, Takemura Y, Kuroda S, Ono Y, Kikkawa U: Activation of protein kinase B (Akt/RAC-protein kinase) by cellular stress and its association with heat shock protein Hsp27. FEBS Lett 410: 493-498, 1997
    • (1997) FEBS Lett. , vol.410 , pp. 493-498
    • Konishi, H.1    Matsuzaki, H.2    Tanaka, M.3    Takemura, Y.4    Kuroda, S.5    Ono, Y.6    Kikkawa, U.7
  • 31
    • 0029821721 scopus 로고    scopus 로고
    • Activation of RAC-protein kinase by heat shock and hyperosmolarity stress through a pathway independent of phosphatidylinositol 3-kinase
    • Konishi H, Matsuzaki H, Tanaka M, Ono Y, Tokunaga C, Kuroda S, Kikkawa U: Activation of RAC-protein kinase by heat shock and hyperosmolarity stress through a pathway independent of phosphatidylinositol 3-kinase. Proc Natl Acad Sci USA 93: 7639-7643, 1996
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7639-7643
    • Konishi, H.1    Matsuzaki, H.2    Tanaka, M.3    Ono, Y.4    Tokunaga, C.5    Kuroda, S.6    Kikkawa, U.7
  • 32
    • 0032533546 scopus 로고    scopus 로고
    • 2 or heat shock is mediated by phosphoinositide 3-kinase and not by mitogen-activated protein kinase-activated protein kinase-2
    • 2 or heat shock is mediated by phosphoinositide 3-kinase and not by mitogen-activated protein kinase-activated protein kinase-2. Biochem J 336: 241-246, 1998
    • (1998) Biochem. J. , vol.336 , pp. 241-246
    • Shaw, M.1    Cohen, P.2    Alessi, D.R.3
  • 33
    • 0035955722 scopus 로고    scopus 로고
    • UV Induces phosphorylation of protein kinase B (Akt) at Ser-473 and Thr-308 in mouse epidermal Cl 41 cells through hydrogen peroxide
    • Huang C, Li J, Ding M, Leonard SS, Wang L, Castranova V, Vallyathan V, Shi X: UV Induces phosphorylation of protein kinase B (Akt) at Ser-473 and Thr-308 in mouse epidermal Cl 41 cells through hydrogen peroxide. J Biol Chem 276: 40234-40240, 2001
    • (2001) J. Biol. Chem. , vol.276 , pp. 40234-40240
    • Huang, C.1    Li, J.2    Ding, M.3    Leonard, S.S.4    Wang, L.5    Castranova, V.6    Vallyathan, V.7    Shi, X.8
  • 34
  • 35
    • 0031039024 scopus 로고    scopus 로고
    • Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate
    • Franke TF, Kaplan DR, Cantley LC, Toker A: Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate. Science 275: 665-668, 1997
    • (1997) Science , vol.275 , pp. 665-668
    • Franke, T.F.1    Kaplan, D.R.2    Cantley, L.C.3    Toker, A.4
  • 36
    • 0035920145 scopus 로고    scopus 로고
    • Regulation of protein kinase B/Akt-serine 473 phosphorylation by integrin-linked kinase: Critical roles for kinase activity and amino acids arginine 211 and serine 343
    • Persad S, Attwell S, Gray V, Mawji N, Deng JT, Leung D, Yan J, Sanghera J, Walsh MP, Dedhar S: Regulation of protein kinase B/Akt-serine 473 phosphorylation by integrin-linked kinase: Critical roles for kinase activity and amino acids arginine 211 and serine 343. J Biol Chem 276: 27462-27469, 2001
    • (2001) J. Biol. Chem. , vol.276 , pp. 27462-27469
    • Persad, S.1    Attwell, S.2    Gray, V.3    Mawji, N.4    Deng, J.T.5    Leung, D.6    Yan, J.7    Sanghera, J.8    Walsh, M.P.9    Dedhar, S.10
  • 38
    • 0034708482 scopus 로고    scopus 로고
    • Akt/protein kinase B is regulated by autophosphorylation at the hypothetical PDK-2 site
    • Toker A, Newton AC: Akt/protein kinase B is regulated by autophosphorylation at the hypothetical PDK-2 site. J Biol Chem 275: 8271-8274, 2000
    • (2000) J. Biol. Chem. , vol.275 , pp. 8271-8274
    • Toker, A.1    Newton, A.C.2
  • 40
    • 0033564697 scopus 로고    scopus 로고
    • CDK inhibitors: Positive and negative regulators of G1-phase progression
    • Sherr CJ, Roberts JM: CDK inhibitors: Positive and negative regulators of G1-phase progression. Genes Dev 13: 1501-1512, 1999
    • (1999) Genes Dev. , vol.13 , pp. 1501-1512
    • Sherr, C.J.1    Roberts, J.M.2
  • 43
    • 0032622050 scopus 로고    scopus 로고
    • p53-independent increase in E2F-1 expression enhances the cytotoxic effects of etoposide and of adriamycin
    • Meng RD, Phillips P, El-Deiry WS: p53-independent increase in E2F-1 expression enhances the cytotoxic effects of etoposide and of adriamycin. Int J Oncol 14: 5-14, 1999
    • (1999) Int. J. Oncol. , vol.14 , pp. 5-14
    • Meng, R.D.1    Phillips, P.2    El-Deiry, W.S.3
  • 44
    • 0035878122 scopus 로고    scopus 로고
    • Selective induction of E2F1 in response to DNA damage, mediated by ATM-dependent phosphorylation
    • Lin WC, Lin FT, Nevins JR: Selective induction of E2F1 in response to DNA damage, mediated by ATM-dependent phosphorylation. Genes Dev 15: 1833-1844, 2001
    • (2001) Genes Dev. , vol.15 , pp. 1833-1844
    • Lin, W.C.1    Lin, F.T.2    Nevins, J.R.3
  • 45
    • 0033618410 scopus 로고    scopus 로고
    • Multiple ras effector pathways contribute to G(1) cell cycle progression
    • Gille H, Downward J: Multiple ras effector pathways contribute to G(1) cell cycle progression. J Biol Chem 274: 22033-22040, 1999
    • (1999) J. Biol. Chem. , vol.274 , pp. 22033-22040
    • Gille, H.1    Downward, J.2
  • 46
    • 0035900792 scopus 로고    scopus 로고
    • Ras induces elevation of E2F-1 mRNA levels
    • Berkovich E, Ginsberg D: Ras induces elevation of E2F-1 mRNA levels. J Biol Chem 276: 42851-42856, 2001
    • (2001) J. Biol. Chem. , vol.276 , pp. 42851-42856
    • Berkovich, E.1    Ginsberg, D.2


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