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Volumn 126, Issue 1, 2004, Pages 45-56

Regulation of FOXO3a by brain-derived neurotrophic factor in differentiated human SH-SY5Y neuroblastoma cells

Author keywords

Bim; Brain derived neurotrophic factor (BDNF); Development and Regeneration Neurotransmitters, Modulators, Transporters, and Receptors; FOXO3a; Neurotrophic factors: biological effects, signal transduction, phosphorylation, gene expression

Indexed keywords

BRAIN DERIVED NEUROTROPHIC FACTOR; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOPROTEIN PHOSPHATASE 1; PHOSPHOPROTEIN PHOSPHATASE 2A; PHOSPHOPROTEIN PHOSPHATASE INHIBITOR; PROTEIN BCL 2; PROTEIN KINASE B; RETINOIC ACID; THAPSIGARGIN; THREONINE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR FKHRL1; UNCLASSIFIED DRUG;

EID: 2942682872     PISSN: 0169328X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbrainres.2004.03.019     Document Type: Article
Times cited : (57)

References (47)
  • 1
    • 0029942186 scopus 로고    scopus 로고
    • Activation and phosphorylation of a pleckstrin homology domain containing protein kinase (RAC-PK/PKB) promoted by serum and protein phosphatase inhibitors
    • Andjelkovic M., Jakubowicz T., Cron P., Ming X.F., Han J.W., Hemmings B.A. Activation and phosphorylation of a pleckstrin homology domain containing protein kinase (RAC-PK/PKB) promoted by serum and protein phosphatase inhibitors. Proc. Natl. Acad. Sci. U. S. A. 93:1996;5699-5704
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 5699-5704
    • Andjelkovic, M.1    Jakubowicz, T.2    Cron, P.3    Ming, X.F.4    Han, J.W.5    Hemmings, B.A.6
  • 2
    • 0033595011 scopus 로고    scopus 로고
    • Protein kinase B/Akt-mediated phosphorylation promotes nuclear exclusion of the winged helix transcription factor FKHR1
    • Biggs W.H. III, Meisenhelder J., Hunter T., Cavenee W.K., Arden K.C. Protein kinase B/Akt-mediated phosphorylation promotes nuclear exclusion of the winged helix transcription factor FKHR1. Proc. Natl. Acad. Sci. U. S. A. 96:1999;7421-7426
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 7421-7426
    • Biggs III, W.H.1    Meisenhelder, J.2    Hunter, T.3    Cavenee, W.K.4    Arden, K.C.5
  • 3
    • 0035813212 scopus 로고    scopus 로고
    • Proapoptotic stimuli induce nuclear accumulation of glycogen synthase kinase-3 beta
    • Bijur G.N., Jope R.S. Proapoptotic stimuli induce nuclear accumulation of glycogen synthase kinase-3 beta. J. Biol. Chem. 276:2001;37436-37442
    • (2001) J. Biol. Chem. , vol.276 , pp. 37436-37442
    • Bijur, G.N.1    Jope, R.S.2
  • 4
    • 0037147122 scopus 로고    scopus 로고
    • Nerve growth factor (NGF) down-regulates the Bcl-2 homology 3 (BH3) domain-only protein Bim and suppresses its proapoptotic activity by phosphorylation
    • Biswas S.C., Greene L.A. Nerve growth factor (NGF) down-regulates the Bcl-2 homology 3 (BH3) domain-only protein Bim and suppresses its proapoptotic activity by phosphorylation. J. Biol. Chem. 277:2002;49511-49516
    • (2002) J. Biol. Chem. , vol.277 , pp. 49511-49516
    • Biswas, S.C.1    Greene, L.A.2
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of proteins 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
  • 7
    • 0029160069 scopus 로고
    • Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction
    • Burgering B.M., Coffer P.J. Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction. Nature. 376:1995;599-602
    • (1995) Nature , vol.376 , pp. 599-602
    • Burgering, B.M.1    Coffer, P.J.2
  • 8
    • 0033518120 scopus 로고    scopus 로고
    • Regulation of the forkhead transcription factor FKHR, but not the PAX3-FKHR fusion protein, by the serine/threonine kinase Akt
    • del Peso L., Gonzalez V.M., Hernandez R., Barr F.G., Nunez G. Regulation of the forkhead transcription factor FKHR, but not the PAX3-FKHR fusion protein, by the serine/threonine kinase Akt. Oncogene. 18:1999;7328-7333
    • (1999) Oncogene , vol.18 , pp. 7328-7333
    • Del Peso, L.1    Gonzalez, V.M.2    Hernandez, R.3    Barr, F.G.4    Nunez, G.5
  • 9
    • 0034609737 scopus 로고    scopus 로고
    • Expression of the pro-apoptotic Bcl-2 family member Bim is regulated by the forkhead transcription factor FKHR-L1
    • Dijkers P.F., Medema R.H., Lammers J.W., Koenderman L., Coffer P.J. Expression of the pro-apoptotic Bcl-2 family member Bim is regulated by the forkhead transcription factor FKHR-L1. Curr. Biol. 10:2000;1201-1204
    • (2000) Curr. Biol. , vol.10 , pp. 1201-1204
    • Dijkers, P.F.1    Medema, R.H.2    Lammers, J.W.3    Koenderman, L.4    Coffer, P.J.5
  • 10
    • 0036214671 scopus 로고    scopus 로고
    • Synaptic plasticity and mood disorders
    • Duman R.S. Synaptic plasticity and mood disorders. Mol. Psychiatry. 7:2002;S29-S34
    • (2002) Mol. Psychiatry , vol.7 , pp. 29-S34
    • Duman, R.S.1
  • 11
    • 0034661826 scopus 로고    scopus 로고
    • Identification of the differential distribution patterns of mRNAs and consensus binding sequences for mouse DAF-16 homologues
    • Furuyama T., Nakazawa T., Nakano I., Mori N. Identification of the differential distribution patterns of mRNAs and consensus binding sequences for mouse DAF-16 homologues. Biochem. J. 349:2000;629-634
    • (2000) Biochem. J. , vol.349 , pp. 629-634
    • Furuyama, T.1    Nakazawa, T.2    Nakano, I.3    Mori, N.4
  • 12
    • 0033546192 scopus 로고    scopus 로고
    • Phosphorylation of serine 256 by protein kinase B disrupts transactivation by FKHR and mediates effects of insulin on insulin-like growth factor-binding protein-1 promoter activity through a conserved insulin response sequence
    • Guo S., Rena G., Cichy S., He X., Cohen P., Unterman T. Phosphorylation of serine 256 by protein kinase B disrupts transactivation by FKHR and mediates effects of insulin on insulin-like growth factor-binding protein-1 promoter activity through a conserved insulin response sequence. J. Biol. Chem. 274:1999;17184-17192
    • (1999) J. Biol. Chem. , vol.274 , pp. 17184-17192
    • Guo, S.1    Rena, G.2    Cichy, S.3    He, X.4    Cohen, P.5    Unterman, T.6
  • 13
    • 0035851204 scopus 로고    scopus 로고
    • BH3-only Bcl-2 family members are coordinately regulated by the JNK pathway and require Bax to induce apoptosis in neurons
    • Harris C.A., Johnson E.M. Jr. BH3-only Bcl-2 family members are coordinately regulated by the JNK pathway and require Bax to induce apoptosis in neurons. J. Biol. Chem. 276:2001;37754-37760
    • (2001) J. Biol. Chem. , vol.276 , pp. 37754-37760
    • Harris, C.A.1    Johnson Jr., E.M.2
  • 14
    • 0036845266 scopus 로고    scopus 로고
    • Identification of JNK-dependent and -independent components of cerebellar granule neuron apoptosis
    • Harris C., Maroney A.C., Johnson E.M. Jr. Identification of JNK-dependent and -independent components of cerebellar granule neuron apoptosis. J. Neurochem. 83:2002;992-1001
    • (2002) J. Neurochem. , vol.83 , pp. 992-1001
    • Harris, C.1    Maroney, A.C.2    Johnson Jr., E.M.3
  • 15
    • 0027323932 scopus 로고
    • Induction of TrkB by retinoic acid mediates biologic responsiveness to BDNF and differentiation of human neuroblastoma cells. Eukaryotic signal transduction group
    • Kaplan D.R., Matsumoto K., Lucarelli E., Thiele C.J. Induction of TrkB by retinoic acid mediates biologic responsiveness to BDNF and differentiation of human neuroblastoma cells. Eukaryotic signal transduction group. Neuron. 11:1993;321-331
    • (1993) Neuron , vol.11 , pp. 321-331
    • Kaplan, D.R.1    Matsumoto, K.2    Lucarelli, E.3    Thiele, C.J.4
  • 17
    • 0038482050 scopus 로고    scopus 로고
    • Activation of the ERK1/2 signaling pathway promotes phosphorylation and proteasome-dependent degradation of the BH3-only protein Bim
    • Ley R., Balmanno K., Hadfield K., Weston C., Cook S.J. Activation of the ERK1/2 signaling pathway promotes phosphorylation and proteasome-dependent degradation of the BH3-only protein Bim. J. Biol. Chem. 278:2003;18811-18816
    • (2003) J. Biol. Chem. , vol.278 , pp. 18811-18816
    • Ley, R.1    Balmanno, K.2    Hadfield, K.3    Weston, C.4    Cook, S.J.5
  • 18
    • 0036850972 scopus 로고    scopus 로고
    • Insulin-like growth factor-I blocks Bcl-2 interacting mediator of cell death (Bim) induction and intrinsic death signaling in cerebellar granule neurons
    • Linseman D.A., Phelps R.A., Bouchard R.J., Le S.S., Laessig T.A., McClure M.L., Heidenreich K.A. Insulin-like growth factor-I blocks Bcl-2 interacting mediator of cell death (Bim) induction and intrinsic death signaling in cerebellar granule neurons. J. Neurosci. 22:2002;9287-9297
    • (2002) J. Neurosci. , vol.22 , pp. 9287-9297
    • Linseman, D.A.1    Phelps, R.A.2    Bouchard, R.J.3    Le S., S.4    Laessig, T.A.5    McClure, M.L.6    Heidenreich, K.A.7
  • 19
    • 0036310511 scopus 로고    scopus 로고
    • BDNF-mediated signal transduction is modulated by GSK3beta and mood stabilizing agents
    • Mai L., Jope R.S., Li X. BDNF-mediated signal transduction is modulated by GSK3beta and mood stabilizing agents. J. Neurochem. 82:2002;75-83
    • (2002) J. Neurochem. , vol.82 , pp. 75-83
    • Mai, L.1    Jope, R.S.2    Li, X.3
  • 20
    • 0032535490 scopus 로고    scopus 로고
    • Inactivation and dephosphorylation of protein kinase Balpha (PKBalpha) promoted by hyperosmotic stress
    • Meier R., Thelen M., Hemmings B.A. Inactivation and dephosphorylation of protein kinase Balpha (PKBalpha) promoted by hyperosmotic stress. EMBO J. 17:1998;7294-7303
    • (1998) EMBO J. , vol.17 , pp. 7294-7303
    • Meier, R.1    Thelen, M.2    Hemmings, B.A.3
  • 21
    • 0033522897 scopus 로고    scopus 로고
    • Insulin stimulates phosphorylation of the forkhead transcription factor FKHR on serine 253 through a Wortmannin-sensitive pathway
    • Nakae J., Park B.C., Accili D. Insulin stimulates phosphorylation of the forkhead transcription factor FKHR on serine 253 through a Wortmannin-sensitive pathway. J. Biol. Chem. 274:1999;15982-15985
    • (1999) J. Biol. Chem. , vol.274 , pp. 15982-15985
    • Nakae, J.1    Park, B.C.2    Accili, D.3
  • 22
    • 0036724341 scopus 로고    scopus 로고
    • The brain-derived neurotrophic factor gene confers susceptibility to bipolar disorder: Evidence from a family-based association study
    • Neves-Pereira M., Mundo E., Muglia P., King N., Macciardi F., Kennedy J.L. The brain-derived neurotrophic factor gene confers susceptibility to bipolar disorder: evidence from a family-based association study. Am. J. Hum. Genet. 71:2002;651-655
    • (2002) Am. J. Hum. Genet. , vol.71 , pp. 651-655
    • Neves-Pereira, M.1    Mundo, E.2    Muglia, P.3    King, N.4    MacCiardi, F.5    Kennedy, J.L.6
  • 23
    • 0028815653 scopus 로고
    • Regulation of BDNF and trkB mRNA in rat brain by chronic electroconvulsive seizure and antidepressant drug treatments
    • Nibuya M., Morinobu S., Duman R.S. Regulation of BDNF and trkB mRNA in rat brain by chronic electroconvulsive seizure and antidepressant drug treatments. J. Neurosci. 15:1995;7539-7547
    • (1995) J. Neurosci. , vol.15 , pp. 7539-7547
    • Nibuya, M.1    Morinobu, S.2    Duman, R.S.3
  • 27
    • 0033546439 scopus 로고    scopus 로고
    • Phosphorylation of the transcription factor forkhead family member FKHR by protein kinase B
    • Rena G., Guo S., Cichy S.C., Unterman T.G., Cohen P. Phosphorylation of the transcription factor forkhead family member FKHR by protein kinase B. J. Biol. Chem. 274:1999;17179-17183
    • (1999) J. Biol. Chem. , vol.274 , pp. 17179-17183
    • Rena, G.1    Guo, S.2    Cichy, S.C.3    Unterman, T.G.4    Cohen, P.5
  • 28
    • 0036024263 scopus 로고    scopus 로고
    • Early maternal deprivation reduces the expression of BDNF and NMDA receptor subunits in rat hippocampus
    • Roceri M., Hendriks W., Racagni G., Ellenbroek B.A., Riva M.A. Early maternal deprivation reduces the expression of BDNF and NMDA receptor subunits in rat hippocampus. Mol. Psychiatry. 7:2002;609-616
    • (2002) Mol. Psychiatry , vol.7 , pp. 609-616
    • Roceri, M.1    Hendriks, W.2    Racagni, G.3    Ellenbroek, B.A.4    Riva, M.A.5
  • 29
    • 0035196587 scopus 로고    scopus 로고
    • Transforming growth factor beta enhances epithelial cell survival via Akt-dependent regulation of FKHRL1
    • Shin I., Bakin A.V., Rodeck U., Brunet A., Arteaga C.L. Transforming growth factor beta enhances epithelial cell survival via Akt-dependent regulation of FKHRL1. Mol. Biol. Cell. 12:2001;3328-3339
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3328-3339
    • Shin, I.1    Bakin, A.V.2    Rodeck, U.3    Brunet, A.4    Arteaga, C.L.5
  • 30
    • 0035135349 scopus 로고    scopus 로고
    • Downregulation of Bim, a proapoptotic relative of Bcl-2, is a pivotal step in cytokine-initiated survival signaling in murine hematopoietic progenitors
    • Shinjyo T., Kuribara R., Inukai T., Hosoi H., Kinoshita T., Miyajima A., Houghton P.J., Look A.T., Ozawa K., Inaba T. Downregulation of Bim, a proapoptotic relative of Bcl-2, is a pivotal step in cytokine-initiated survival signaling in murine hematopoietic progenitors. Mol. Cell. Biol. 21:2001;854-864
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 854-864
    • Shinjyo, T.1    Kuribara, R.2    Inukai, T.3    Hosoi, H.4    Kinoshita, T.5    Miyajima, A.6    Houghton, P.J.7    Look, A.T.8    Ozawa, K.9    Inaba, T.10
  • 32
    • 0029555826 scopus 로고
    • Effects of stress on neurotrophic factor expression in the rat brain
    • Smith M.A., Makino S., Kvetnansky R., Post R.M. Effects of stress on neurotrophic factor expression in the rat brain. Ann. N.Y. Acad. Sci. 771:1995;234-239
    • (1995) Ann. N.Y. Acad. Sci. , vol.771 , pp. 234-239
    • Smith, M.A.1    Makino, S.2    Kvetnansky, R.3    Post, R.M.4
  • 33
    • 0037160134 scopus 로고    scopus 로고
    • Central role of glycogen synthase kinase-3beta in endoplasmic reticulum stress-induced caspase-3 activation
    • Song L., De Sarno P., Jope R.S. Central role of glycogen synthase kinase-3beta in endoplasmic reticulum stress-induced caspase-3 activation. J. Biol. Chem. 277:2002;44701-44708
    • (2002) J. Biol. Chem. , vol.277 , pp. 44701-44708
    • Song, L.1    De Sarno, P.2    Jope, R.S.3
  • 34
    • 0037094096 scopus 로고    scopus 로고
    • The forkhead transcription factor FoxO regulates transcription of p27Kip1 and Bim in response to IL-2
    • Stahl M., Dijkers P.F., Kops G.J., Lens S.M., Coffer P.J., Burgering B.M., Medema R.H. The forkhead transcription factor FoxO regulates transcription of p27Kip1 and Bim in response to IL-2. J. Immunol. 168:2002;5024-5031
    • (2002) J. Immunol. , vol.168 , pp. 5024-5031
    • Stahl, M.1    Dijkers, P.F.2    Kops, G.J.3    Lens, S.M.4    Coffer, P.J.5    Burgering, B.M.6    Medema, R.H.7
  • 36
    • 0039425278 scopus 로고    scopus 로고
    • Negative regulation of the forkhead transcription factor FKHR by Akt
    • Tang E.D., Nunez G., Barr F.G., Guan K.L. Negative regulation of the forkhead transcription factor FKHR by Akt. J. Biol. Chem. 274:1999;16741-16746
    • (1999) J. Biol. Chem. , vol.274 , pp. 16741-16746
    • Tang, E.D.1    Nunez, G.2    Barr, F.G.3    Guan, K.L.4
  • 37
    • 0025332577 scopus 로고
    • Thapsigargin, a tumor promoter, discharges intracellular Ca2+ stores by specific inhibition of the endoplasmic reticulum Ca2(+)-ATPase
    • Thastrup O., Cullen P.J., Drobak B.K., Hanley M.R., Dawson A.P. Thapsigargin, a tumor promoter, discharges intracellular Ca2+ stores by specific inhibition of the endoplasmic reticulum Ca2(+)-ATPase. Proc. Natl. Acad. Sci. U. S. A. 87:1990;2466-2470
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 2466-2470
    • Thastrup, O.1    Cullen, P.J.2    Drobak, B.K.3    Hanley, M.R.4    Dawson, A.P.5
  • 39
    • 0031960313 scopus 로고    scopus 로고
    • A tool coming of age: Thapsigargin as an inhibitor of sarco-endoplasmic reticulum Ca(2+)-ATPases
    • Treiman M., Caspersen C., Christensen S.B. A tool coming of age: thapsigargin as an inhibitor of sarco-endoplasmic reticulum Ca(2+)-ATPases. Trends Pharmacol. Sci. 19:1998;131-135
    • (1998) Trends Pharmacol. Sci. , vol.19 , pp. 131-135
    • Treiman, M.1    Caspersen, C.2    Christensen, S.B.3
  • 40
    • 0031576359 scopus 로고    scopus 로고
    • Characterization of tau proteins in human neuroblastoma SH-SY5Y cell line
    • Uberti D., Rizzini C., Spano P.F., Memo M. Characterization of tau proteins in human neuroblastoma SH-SY5Y cell line. Neurosci. Lett. 235:1997;149-153
    • (1997) Neurosci. Lett. , vol.235 , pp. 149-153
    • Uberti, D.1    Rizzini, C.2    Spano, P.F.3    Memo, M.4
  • 42
    • 0037422172 scopus 로고    scopus 로고
    • Activation of ERK1/2 by deltaRaf-1:ER* represses Bim expression independently of the JNK or PI3K pathways
    • Weston C.R., Balmanno K., Chalmers C., Hadfield K., Molton S.A., Ley R., Wagner E.F., Cook S.J. Activation of ERK1/2 by deltaRaf-1:ER* represses Bim expression independently of the JNK or PI3K pathways. Oncogene. 22:2003;1281-1293
    • (2003) Oncogene , vol.22 , pp. 1281-1293
    • Weston, C.R.1    Balmanno, K.2    Chalmers, C.3    Hadfield, K.4    Molton, S.A.5    Ley, R.6    Wagner, E.F.7    Cook, S.J.8
  • 43
    • 0035049449 scopus 로고    scopus 로고
    • Dominant-negative c-Jun promotes neuronal survival by reducing BIM expression and inhibiting mitochondrial cytochrome c release
    • Whitfield J., Neame S.J., Paquet L., Bernard O., Ham J. Dominant-negative c-Jun promotes neuronal survival by reducing BIM expression and inhibiting mitochondrial cytochrome c release. Neuron. 29:2001;629-643
    • (2001) Neuron , vol.29 , pp. 629-643
    • Whitfield, J.1    Neame, S.J.2    Paquet, L.3    Bernard, O.4    Ham, J.5
  • 44
    • 0027530567 scopus 로고
    • Inhibition of protein synthesis and early protein processing by thapsigargin in cultured cells
    • Wong W.L., Brostrom M.A., Kuznetsov G., Gmitter-Yellen D., Brostrom C.O. Inhibition of protein synthesis and early protein processing by thapsigargin in cultured cells. Biochem. J. 289:1993;71-79
    • (1993) Biochem. J. , vol.289 , pp. 71-79
    • Wong, W.L.1    Brostrom, M.A.2    Kuznetsov, G.3    Gmitter-Yellen, D.4    Brostrom, C.O.5
  • 45
    • 0034671848 scopus 로고    scopus 로고
    • Insulin-like growth factor-1-induced phosphorylation of the forkhead family transcription factor FKHRL1 is mediated by Akt kinase in PC12 cells
    • Zheng W.H., Kar S., Quirion R. Insulin-like growth factor-1-induced phosphorylation of the forkhead family transcription factor FKHRL1 is mediated by Akt kinase in PC12 cells. J. Biol. Chem. 275:2000;39152-39158
    • (2000) J. Biol. Chem. , vol.275 , pp. 39152-39158
    • Zheng, W.H.1    Kar, S.2    Quirion, R.3
  • 46
    • 0036328592 scopus 로고    scopus 로고
    • FKHRL1 and its homologs are new targets of nerve growth factor Trk receptor signaling
    • Zheng W.H., Kar S., Quirion R. FKHRL1 and its homologs are new targets of nerve growth factor Trk receptor signaling. J. Neurochem. 80:2002;1049-1061
    • (2002) J. Neurochem. , vol.80 , pp. 1049-1061
    • Zheng, W.H.1    Kar, S.2    Quirion, R.3
  • 47
    • 0036078618 scopus 로고    scopus 로고
    • Insulin-like growth factor-1-induced phosphorylation of transcription factor FKHRL1 is mediated by phosphatidylinositol 3-kinase/Akt kinase and role of this pathway in insulin-like growth factor-1-induced survival of cultured hippocampal neurons
    • Zheng W.H., Kar S., Quirion R. Insulin-like growth factor-1-induced phosphorylation of transcription factor FKHRL1 is mediated by phosphatidylinositol 3-kinase/Akt kinase and role of this pathway in insulin-like growth factor-1-induced survival of cultured hippocampal neurons. Mol. Pharmacol. 62:2002;225-233
    • (2002) Mol. Pharmacol. , vol.62 , pp. 225-233
    • Zheng, W.H.1    Kar, S.2    Quirion, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.