메뉴 건너뛰기




Volumn , Issue , 2012, Pages

Glycogen synthase kinase 3: A point of integration in alzheimer's disease and a therapeutic target?

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOGEN SYNTHASE KINASE 3; TAU PROTEIN;

EID: 84863697825     PISSN: None     EISSN: 20900252     Source Type: Journal    
DOI: 10.1155/2012/276803     Document Type: Review
Times cited : (19)

References (47)
  • 1
    • 77649129121 scopus 로고    scopus 로고
    • GSK3: A multifaceted kinase in Wnt signaling
    • Wu D., Pan W., GSK3: a multifaceted kinase in Wnt signaling Trends in Biochemical Sciences 2010 35 3 161 168
    • (2010) Trends in Biochemical Sciences , vol.35 , Issue.3 , pp. 161-168
    • Wu, D.1    Pan, W.2
  • 2
    • 81355161240 scopus 로고    scopus 로고
    • Inhibition of GSK3 by Wnt signallingtwo contrasting models
    • Metcalfe C., Bienz M., Inhibition of GSK3 by Wnt signallingtwo contrasting models Journal of Cell Science 2011 124 21 3537 3544
    • (2011) Journal of Cell Science , vol.124 , Issue.21 , pp. 3537-3544
    • Metcalfe, C.1    Bienz, M.2
  • 4
    • 0032577899 scopus 로고    scopus 로고
    • WNT-1 and HGF regulate GSK3β activity and β-catenin signaling in mammary epithelial cells
    • DOI 10.1006/bbrc.1998.8888
    • Papkoff J., Aikawa M., WNT-1 and HGF regulate GSK3 activity and -catenin signaling in mammary epithelial cells Biochemical and Biophysical Research Communications 1998 247 3 851 858 (Pubitemid 28418480)
    • (1998) Biochemical and Biophysical Research Communications , vol.247 , Issue.3 , pp. 851-858
    • Papkoff, J.1    Aikawa, M.2
  • 5
    • 0028021566 scopus 로고
    • The mechanism by which epidermal growth factor inhibits glycogen synthase kinase 3 in A431 cells
    • Saito Y., Vandenheede J. R., Cohen P., The mechanism by which epidermal growth factor inhibits glycogen synthase kinase 3 in A431 cells Biochemical Journal 1994 303 1 27 31 (Pubitemid 24302894)
    • (1994) Biochemical Journal , vol.303 , Issue.1 , pp. 27-31
    • Saito, Y.1    Vandenheede, J.R.2    Cohen, P.3
  • 6
    • 0027978816 scopus 로고
    • The inhibition of glycogen synthase kinase-3 by insulin or insulin-like growth factor 1 in the rat skeletal muscle cell line L6 is blocked by wortmannin, but not by rapamycin: Evidence that wortmannin blocks activation of the mitogen-activated protein kinase pathway in L6 cells between Ras and Raf
    • Cross D. A. E., Alessi D. R., Vandenheede J. R., McDowell H. E., Hundal H. S., Cohen P., The inhibition of glycogen synthase kinase-3 by insulin or insulin-like growth factor 1 in the rat skeletal muscle cell line L6 is blocked by wortmannin, but not by rapamycin: evidence that wortmannin blocks activation of the mitogen-activated protein kinase pathway in L6 cells between Ras and Raf Biochemical Journal 1994 303 1 21 26 (Pubitemid 24302893)
    • (1994) Biochemical Journal , vol.303 , Issue.1 , pp. 21-26
    • Cross, D.A.E.1    Alessi, D.R.2    Vandenheede, J.R.3    McDowell, H.E.4    Hundal, H.S.5    Cohen, P.6
  • 7
    • 0027515127 scopus 로고
    • Inactivation of glycogen synthase kinase-3β by phosphorylation: New kinase connections in insulin and growth-factor signalling
    • Sutherland C., Leighton I. A., Cohen P., Inactivation of glycogen synthase kinase-3 by phosphorylation: new kinase connections in insulin and growth-factor signalling Biochemical Journal 1993 296 1 15 19 (Pubitemid 23344723)
    • (1993) Biochemical Journal , vol.296 , Issue.1 , pp. 15-19
    • Sutherland, C.1    Leighton, I.A.2    Cohen, P.3
  • 8
    • 0027960448 scopus 로고
    • Mitogen inactivation of glycogen synthase kinase-3β in intact cells via serine 9 phosphorylation
    • Stambolic V., Woodgett J. R., Mitogen inactivation of glycogen synthase kinase-3 in intact cells via serine 9 phosphorylation Biochemical Journal 1994 303 3 701 704 (Pubitemid 24325998)
    • (1994) Biochemical Journal , vol.303 , Issue.3 , pp. 701-704
    • Stambolic, V.1    Woodgett, J.R.2
  • 9
    • 34247865533 scopus 로고    scopus 로고
    • A chaperone-dependent GSK3β transitional intermediate mediates activation-loop autophosphorylation
    • DOI 10.1016/j.molcel.2006.10.009
    • Lochhead P. A., Kinstrie R., Sibbet G., Rawjee T., Morrice N., Cleghone V., A chaperone-dependent GSK3 transitional intermediate mediates activation-loop autophosphorylation Molecular Cell 2006 24 4 627 633 (Pubitemid 350284229)
    • (2006) Molecular Cell , vol.24 , Issue.4 , pp. 627-633
    • Lochhead, P.A.1    Kinstrie, R.2    Sibbet, G.3    Rawjee, T.4    Morrice, N.5    Cleghone, V.6
  • 11
    • 62849125293 scopus 로고    scopus 로고
    • Inhibition of GSK3 phosphorylation of -catenin via phosphorylated PPPSPXS motifs of Wnt coreceptor LRP6
    • Wu G., Huang H., Abreu J. G., He X., Inhibition of GSK3 phosphorylation of -catenin via phosphorylated PPPSPXS motifs of Wnt coreceptor LRP6 PLoS ONE 2009 4 3
    • (2009) PLoS ONE , vol.4 , Issue.3
    • Wu, G.1    Huang, H.2    Abreu, J.G.3    He, X.4
  • 12
    • 33644967242 scopus 로고    scopus 로고
    • Wnt signaling: Complexity at the surface
    • Cadigan K. M., Liu Y. I., Wnt signaling: complexity at the surface Journal of Cell Science 2006 119 3 395 402
    • (2006) Journal of Cell Science , vol.119 , Issue.3 , pp. 395-402
    • Cadigan, K.M.1    Liu, Y.I.2
  • 13
    • 0034969088 scopus 로고    scopus 로고
    • A common phosphate binding site explains the unique substrate specificity of GSK3 and its inactivation by phosphorylation
    • DOI 10.1016/S1097-2765(01)00253-2
    • Frame S., Cohen P., Biondi R. M., A common phosphate binding site explains the unique substrate specificity of GSK3 and its inactivation by phosphorylation Molecular Cell 2001 7 6 1321 1327 (Pubitemid 32607364)
    • (2001) Molecular Cell , vol.7 , Issue.6 , pp. 1321-1327
    • Frame, S.1    Cohen, P.2    Biondi, R.M.3
  • 14
    • 0025286104 scopus 로고
    • Molecular cloning and expression of glycogen synthase kinase-3/factor A
    • Woodgett J. R., Molecular cloning and expression of glycogen synthase kinase-3/factor A The EMBO Journal 1990 9 8 2431 2438
    • (1990) The EMBO Journal , vol.9 , Issue.8 , pp. 2431-2438
    • Woodgett, J.R.1
  • 15
    • 0035983533 scopus 로고    scopus 로고
    • Aternative splicing isoform of tau protein kinase I/glycogen synthase kinase 3β
    • DOI 10.1046/j.1471-4159.2002.00918.x
    • Mukai F., Ishiguro K., Sano Y., Fujita S. C., Aternative splicing isoform of tau protein kinase I/glycogen synthase kinase 3 Journal of Neurochemistry 2002 81 5 1073 1083 (Pubitemid 34809290)
    • (2002) Journal of Neurochemistry , vol.81 , Issue.5 , pp. 1073-1083
    • Mukai, F.1    Ishiguro, K.2    Sano, Y.3    Fujita, S.C.4
  • 17
    • 0034859101 scopus 로고    scopus 로고
    • The multifaceted roles of glycogen synthase kinase 3β in cellular signaling
    • DOI 10.1016/S0301-0082(01)00011-9, PII S0301008201000119
    • Grimes C. A., Jope R. S., The multifaceted roles of glycogen synthase kinase 3 in cellular signaling Progress in Neurobiology 2001 65 4 391 426 (Pubitemid 32781670)
    • (2001) Progress in Neurobiology , vol.65 , Issue.4 , pp. 391-426
    • Grimes, C.A.1    Jope, R.S.2
  • 19
    • 33750866196 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 (GSK3) in psychiatric disease and therapeutic interventions
    • Jope R. S., Roh M. S., Glycogen synthase kinase-3 (GSK3) in psychiatric disease and therapeutic interventions Current Drug Targets 2006 7 11 1421 1434 (Pubitemid 44718302)
    • (2006) Current Drug Targets , vol.7 , Issue.11 , pp. 1421-1434
    • Jope, R.S.1    Roh, M.-S.2
  • 20
    • 0036942638 scopus 로고    scopus 로고
    • The active form of glycogen synthase kinase-3β is associated with granulovacuolar degeneration in neurons in Alzheimers's disease
    • DOI 10.1007/s004010100435
    • Leroy K., Boutajangout A., Authelet M., Woodgett J. R., Anderton B. H., Brion J. P., The active form of glycogen synthase kinase-3 is associated with granulovacuolar degeneration in neurons in Alzheimers's disease Acta Neuropathologica 2002 103 2 91 99 (Pubitemid 36067485)
    • (2002) Acta Neuropathologica , vol.103 , Issue.2 , pp. 91-99
    • Leroy, K.1    Boutajangout, A.2    Authelet, M.3    Woodgett, J.R.4    Anderton, B.H.5    Brion, J.-P.6
  • 21
    • 0033302735 scopus 로고    scopus 로고
    • Tau protein in normal and Alzheimer's disease brain: An update
    • Johnson G. V. W., Hartigan J. A., Tau protein in normal and Alzheimer's disease brain: an update Journal of Alzheimer's Disease 1999 1 4-5 329 351
    • (1999) Journal of Alzheimer's Disease , vol.1 , Issue.45 , pp. 329-351
    • Johnson, G.V.W.1    Hartigan, J.A.2
  • 23
    • 12344323961 scopus 로고    scopus 로고
    • Tau phosphorylation in neuronal cell function and dysfunction
    • DOI 10.1242/jcs.01558
    • Johnson G. V. W., Stoothoff W. H., Tau phosphorylation in neuronal cell function and dysfunction Journal of Cell Science 2004 117 24 5721 5729 (Pubitemid 40123939)
    • (2004) Journal of Cell Science , vol.117 , Issue.24 , pp. 5721-5729
    • Johnson, G.V.W.1    Stoothoff, W.H.2
  • 24
    • 61849088424 scopus 로고    scopus 로고
    • Tau phosphorylation: The therapeutic challenge for neurodegenerative disease
    • Hanger D. P., Anderton B. H., Noble W., Tau phosphorylation: the therapeutic challenge for neurodegenerative disease Trends in Molecular Medicine 2009 15 3 112 119
    • (2009) Trends in Molecular Medicine , vol.15 , Issue.3 , pp. 112-119
    • Hanger, D.P.1    Anderton, B.H.2    Noble, W.3
  • 25
    • 36949040819 scopus 로고    scopus 로고
    • Site-specific effects of tau phosphorylation on its microtubule assembly activity and self-aggregation
    • DOI 10.1111/j.1460-9568.2007.05955.x
    • Liu F., Li B., Tung E. J., Grundke-Iqbal I., Iqbal K., Gong C. X., Site-specific effects of tau phosphorylation on its microtubule assembly activity and self-aggregation European Journal of Neuroscience 2007 26 12 3429 3436 (Pubitemid 350243526)
    • (2007) European Journal of Neuroscience , vol.26 , Issue.12 , pp. 3429-3436
    • Liu, F.1    Li, B.2    Tung, E.-J.3    Grundke-Iqbal, I.4    Iqbal, K.5    Gong, C.-X.6
  • 26
    • 84863705013 scopus 로고    scopus 로고
    • The chronology and maturation of the neurofibrillary tangle pathology in Alzheimer's disease is based on the state of phosphorylation, conformational changes, and cleavage of tau protein
    • In press
    • Mondragon-Rodriguez S. B.-I. G., Garca-Sierra F., The chronology and maturation of the neurofibrillary tangle pathology in Alzheimer's disease is based on the state of phosphorylation, conformational changes, and cleavage of tau protein. Novascience Book. In press
    • Novascience Book
    • Mondragon-Rodriguez, S.B.-I.G.1    Garca-Sierra, F.2
  • 28
    • 67149128179 scopus 로고    scopus 로고
    • Conformational changes and cleavage; Are these responsible for the tau aggregation in Alzheimer's disease?
    • Mondragn-Rodrguez S., Basurto-Islas G., Binder L. I., Garca-Sierra F., Conformational changes and cleavage; are these responsible for the tau aggregation in Alzheimer's disease? Future Neurology 2009 4 1 39 53
    • (2009) Future Neurology , vol.4 , Issue.1 , pp. 39-53
    • Mondragn-Rodrguez, S.1    Basurto-Islas, G.2    Binder, L.I.3    Garca-Sierra, F.4
  • 29
    • 70350234910 scopus 로고    scopus 로고
    • Conformational changes specific for pseudophosphorylation at serine 262 selectively impair binding of tau to microtubules
    • Fischer D., Mukrasch M. D., Biernat J., Bibow S., Blackledge M., Griesinger C., Mandelkow E., Zweckstetter M., Conformational changes specific for pseudophosphorylation at serine 262 selectively impair binding of tau to microtubules Biochemistry 2009 48 42 10047 10055
    • (2009) Biochemistry , vol.48 , Issue.42 , pp. 10047-10055
    • Fischer, D.1    Mukrasch, M.D.2    Biernat, J.3    Bibow, S.4    Blackledge, M.5    Griesinger, C.6    Mandelkow, E.7    Zweckstetter, M.8
  • 30
    • 22744459527 scopus 로고    scopus 로고
    • Pseudo-phosphorylation of tau at Ser202 and Thr205 affects tau filament formation
    • DOI 10.1016/j.molbrainres.2005.04.012, PII S0169328X05001762
    • Rankin C. A., Sun Q., Gamblin T. C., Pseudo-phosphorylation of tau at Ser202 and Thr205 affects tau filament formation Molecular Brain Research 2005 138 1 84 93 (Pubitemid 41032932)
    • (2005) Molecular Brain Research , vol.138 , Issue.1 , pp. 84-93
    • Rankin, C.A.1    Sun, Q.2    Gamblin, T.C.3
  • 32
    • 33845657460 scopus 로고    scopus 로고
    • GSK3α exhibits β-catenin and tau directed kinase activities that are modulated by Wnt
    • DOI 10.1111/j.1460-9568.2006.05243.x
    • Asuni A. A., Hooper C., Reynolds C. H., Lovestone S., Anderton B. H., Killick R., GSK3 exhibits -catenin and tau directed kinase activities that are modulated by Wnt European Journal of Neuroscience 2006 24 12 3387 3392 (Pubitemid 44952605)
    • (2006) European Journal of Neuroscience , vol.24 , Issue.12 , pp. 3387-3392
    • Asuni, A.A.1    Hooper, C.2    Reynolds, C.H.3    Lovestone, S.4    Anderton, B.H.5    Killick, R.6
  • 33
    • 0038187674 scopus 로고    scopus 로고
    • GSK-3α regulates production of Alzheimer's disease amyloid-β peptides
    • DOI 10.1038/nature01640
    • Phiel C. J., Wilson C. A., Lee V. M. Y., Klein P. S., GSK-3 regulates production of Alzheimer's disease amyloid- peptides Nature 2003 423 6938 435 439 (Pubitemid 36626994)
    • (2003) Nature , vol.423 , Issue.6938 , pp. 435-439
    • Phiel, C.J.1    Wilson, C.A.2    Lee, V.M.-Y.3    Klein, P.S.4
  • 34
    • 0036606693 scopus 로고    scopus 로고
    • The GSK3β signaling cascade and neurodegenerative disease
    • DOI 10.1016/S0959-4388(02)00320-3
    • Kaytor M. D., Orr H. T., The GSK3 signaling cascade and neurodegenerative disease Current Opinion in Neurobiology 2002 12 3 275 278 (Pubitemid 34615752)
    • (2002) Current Opinion in Neurobiology , vol.12 , Issue.3 , pp. 275-278
    • Kaytor, M.D.1    Orr, H.T.2
  • 35
    • 0036214603 scopus 로고    scopus 로고
    • Mood stabilizers, glycogen synthase kinase-3 and cell survival
    • Jope R. S., Bijur G. N., Mood stabilizers, glycogen synthase kinase-3 and cell survival Molecular Psychiatry 2002 7 supplement 1 S35 S45
    • (2002) Molecular Psychiatry , vol.7 , Issue.SUPPL. 1
    • Jope, R.S.1    Bijur, G.N.2
  • 36
    • 79960815278 scopus 로고    scopus 로고
    • Neuroprotective action of lithium in disorders of the central nervous system
    • Chiu C. T., Chuang D. M., Neuroprotective action of lithium in disorders of the central nervous system Zhong Nan Da Xue Xue Bao Yi Xue Ban 2011 36 6 461 476
    • (2011) Zhong Nan da Xue Xue Bao Yi Xue Ban , vol.36 , Issue.6 , pp. 461-476
    • Chiu, C.T.1    Chuang, D.M.2
  • 37
    • 79960377584 scopus 로고    scopus 로고
    • Drugs: A tangled web of targets
    • Gravitz L., Drugs: a tangled web of targets Nature 2011 475 7355 S9 S11
    • (2011) Nature , vol.475 , Issue.7355
    • Gravitz, L.1
  • 39
    • 41349106367 scopus 로고    scopus 로고
    • Chapter 8 Synaptic plasticity in learning and memory: Stress effects in the hippocampus
    • DOI 10.1016/S0079-6123(07)00008-8, PII S0079612307000088
    • Howland J. G., Wang Y. T., Synaptic plasticity in learning and memory: stress effects in the hippocampus Progress in Brain Research 2008 169 145 158 (Pubitemid 351451901)
    • (2008) Progress in Brain Research , vol.169 , pp. 145-158
    • Howland, J.G.1    Wang, Y.T.2
  • 40
    • 80555125111 scopus 로고    scopus 로고
    • The cell biology of synaptic plasticity
    • Ho V. M., Lee J.-A., Martin K. C., The cell biology of synaptic plasticity Science 2011 334 6056 623 628
    • (2011) Science , vol.334 , Issue.6056 , pp. 623-628
    • Ho, V.M.1    Lee, J.-A.2    Martin, K.C.3
  • 44
    • 55849090651 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta and tau genes interact in Alzheimer's disease
    • Kwok J. B., Loy C. T., Hamilton G., Glycogen synthase kinase-3beta and tau genes interact in Alzheimer's disease Annals of Neurology 2008 64 4 446 454
    • (2008) Annals of Neurology , vol.64 , Issue.4 , pp. 446-454
    • Kwok, J.B.1    Loy, C.T.2    Hamilton, G.3
  • 45
    • 79955591187 scopus 로고    scopus 로고
    • Association analysis of GSK3B and MAPT polymorphisms with Alzheimer's disease in Han Chinese
    • Zhang N., Yu J. T., Yang Y., Yang J., Zhang W., Tan L., Association analysis of GSK3B and MAPT polymorphisms with Alzheimer's disease in Han Chinese Brain Research 2011 1391 147 153
    • (2011) Brain Research , vol.1391 , pp. 147-153
    • Zhang, N.1    Yu, J.T.2    Yang, Y.3    Yang, J.4    Zhang, W.5    Tan, L.6
  • 46
    • 80054923695 scopus 로고    scopus 로고
    • Pharmacological treatment of Alzheimer disease
    • Massoud F., Leger G. C., Pharmacological treatment of Alzheimer disease Canadian Journal of Psychiatry 2011 56 10 579 588
    • (2011) Canadian Journal of Psychiatry , vol.56 , Issue.10 , pp. 579-588
    • Massoud, F.1    Leger, G.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.