메뉴 건너뛰기




Volumn 31, Issue 6, 2004, Pages 532-537

Activation of glycogen synthase kinase 3 induces Alzheimer-like hyperphosphorylation of cytoskeleton protein and cell damage

Author keywords

Alzheimer disease; Glycogen synthase kinase 3; Neurofilament; Phosphorylation; Wortmannin

Indexed keywords

CYTOSKELETON PROTEIN; GLYCOGEN SYNTHASE KINASE 3; PHOSPHATIDYLINOSITOL 3 KINASE INHIBITOR; TAU PROTEIN; WORTMANNIN;

EID: 3242785633     PISSN: 10003282     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (2)

References (29)
  • 1
    • 0035914046 scopus 로고    scopus 로고
    • Hyperphosphorylation and accumulation of NF proteins in Alzheimer disease brain and in okadaic acid-treated SY5Y cells
    • Wang J, Tung Y C, Wang Y, et al. Hyperphosphorylation and accumulation of NF proteins in Alzheimer disease brain and in okadaic acid-treated SY5Y cells. FEBS Lett, 2001, 507 (1): 81-87
    • (2001) FEBS Lett , vol.507 , Issue.1 , pp. 81-87
    • Wang, J.1    Tung, Y.C.2    Wang, Y.3
  • 2
    • 0032006074 scopus 로고    scopus 로고
    • The slow axonal transport of cytoskeletal proteins
    • Nixon R A. The slow axonal transport of cytoskeletal proteins. Curr Opin Cell Biol, 1998, 10 (1): 87-92
    • (1998) Curr Opin Cell Biol , vol.10 , Issue.1 , pp. 87-92
    • Nixon, R.A.1
  • 3
    • 0032566623 scopus 로고    scopus 로고
    • Tau is phosphoiylated by GSK-3 at several sites found in Alzheimer disease and its biological activity markedly inhibited only after it is prephosphorylated by A-kinase
    • Wang J Z, Wu Q, Smith A, et al. Tau is phosphoiylated by GSK-3 at several sites found in Alzheimer disease and its biological activity markedly inhibited only after it is prephosphorylated by A-kinase. FEBS Lett, 1998, 436 (1): 28-34
    • (1998) FEBS Lett , vol.436 , Issue.1 , pp. 28-34
    • Wang, J.Z.1    Wu, Q.2    Smith, A.3
  • 4
    • 0032850599 scopus 로고    scopus 로고
    • Distribution of active glycogen synthase kinase 3beta (GSK-3beta) in brains staged for Alzheimer disease neurofibrillary changes
    • Pei J J, Braak E, Braak H, et al. Distribution of active glycogen synthase kinase 3beta (GSK-3beta) in brains staged for Alzheimer disease neurofibrillary changes. J Neuropathol Exp Neurol, 1999, 58 (9): 1010-1019
    • (1999) J Neuropathol Exp Neurol , vol.58 , Issue.9 , pp. 1010-1019
    • Pei, J.J.1    Braak, E.2    Braak, H.3
  • 5
    • 0038187674 scopus 로고    scopus 로고
    • GSK-3a regulates production of Alzheimer's disease amyloid-β Peptides
    • Phiel C J, Wilson C A, Lee V M Y, et al. GSK-3a regulates production of Alzheimer's disease amyloid-β Peptides. Nature, 2003, 423 (6938): 435-439
    • (2003) Nature , vol.423 , Issue.6938 , pp. 435-439
    • Phiel, C.J.1    Wilson, C.A.2    Lee, V.M.Y.3
  • 6
    • 0035863188 scopus 로고    scopus 로고
    • Decreased nuclear-catenin, tau hyperphosphorylation and neurodegeneration in GSK-3 conditional transgenic mice
    • Lucas J J, Hernandez F, Gomez-Ramos P, et al. Decreased nuclear-catenin, tau hyperphosphorylation and neurodegeneration in GSK-3 conditional transgenic mice. EMBO J , 2001, 20 (1-2): 27-39
    • (2001) EMBO J , vol.20 , Issue.1-2 , pp. 27-39
    • Lucas, J.J.1    Hernandez, F.2    Gomez-Ramos, P.3
  • 7
    • 0034731461 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 phosphorylates protein tau and rescues the axonopathy in the central nervous system of human four-repeat tau transgenic mice
    • Spittaels K, Van den Haute C, Van Dorpe J, et al. Glycogen synthase kinase-3 phosphorylates protein tau and rescues the axonopathy in the central nervous system of human four-repeat tau transgenic mice. J Biol Chem, 2000, 275 (52): 41340-41349
    • (2000) J Biol Chem , vol.275 , Issue.52 , pp. 41340-41349
    • Spittaels, K.1    Van Den Haute, C.2    Van Dorpe, J.3
  • 8
    • 0346434153 scopus 로고    scopus 로고
    • Overactivation of glycogen synthase kinase-3 by inhibition of phosphoinositol-3 kinase and protein kinase C leads to hyperphosphorylation of tau and impairment of spatial memory
    • Liu S J, Zhang A H, Li H L, et al. Overactivation of glycogen synthase kinase-3 by inhibition of phosphoinositol-3 kinase and protein kinase C leads to hyperphosphorylation of tau and impairment of spatial memory. J Neurochem, 2003, 87 (6): 1333-1344
    • (2003) J Neurochem , vol.87 , Issue.6 , pp. 1333-1344
    • Liu, S.J.1    Zhang, A.H.2    Li, H.L.3
  • 9
    • 0031892270 scopus 로고    scopus 로고
    • Potential mechanism (s) involved in the regulation of glycogen synthesis by insulin
    • Srivastava A K, Pandey S K. Potential mechanism (s) involved in the regulation of glycogen synthesis by insulin. Mol Cell Biochem, 1998. 182 (1-2): 135-141
    • (1998) Mol Cell Biochem , vol.182 , Issue.1-2 , pp. 135-141
    • Srivastava, A.K.1    Pandey, S.K.2
  • 10
    • 0029587224 scopus 로고
    • Inhibition of GSK-3 by insulin mediated by PKB
    • Cross D A, Alessi D R, Cohen P, et al. Inhibition of GSK-3 by insulin mediated by PKB. Nature, 1995, 378 (6559): 785-789
    • (1995) Nature , vol.378 , Issue.6559 , pp. 785-789
    • Cross, D.A.1    Alessi, D.R.2    Cohen, P.3
  • 11
    • 0032530482 scopus 로고    scopus 로고
    • Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/ AKT by the integrin-linked kinase
    • Delcommenne M, Tan C, Gray V, et al. Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/ AKT by the integrin-linked kinase. Proc Natl Acad Sci USA, 1998, 95 (19): 11211-11216
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.19 , pp. 11211-11216
    • Delcommenne, M.1    Tan, C.2    Gray, V.3
  • 12
    • 0032881288 scopus 로고    scopus 로고
    • AKT/PKB and other D3 phosphoinositide-regulated kinases: Kinase activation by phosphoinositide-dependent phosphorylation
    • Chan T O, Rittenhouse S E, Tsichlis P N. AKT/PKB and other D3 phosphoinositide-regulated kinases: kinase activation by phosphoinositide- dependent phosphorylation. Ann Rev Biochem, 1999, 68: 965-1014
    • (1999) Ann Rev Biochem , vol.68 , pp. 965-1014
    • Chan, T.O.1    Rittenhouse, S.E.2    Tsichlis, P.N.3
  • 13
    • 0034598963 scopus 로고    scopus 로고
    • Inactivation of glycogen synthase kinase-3 by protein kinase C delta: Implications for regulation of tau phosphorylation
    • Tsujio I, Tanaka T, Kudo T, et al. Inactivation of glycogen synthase kinase-3 by protein kinase C delta: implications for regulation of tau phosphorylation. FEBS Lett, 2000, 469 (1): 111-117
    • (2000) FEBS Lett , vol.469 , Issue.1 , pp. 111-117
    • Tsujio, I.1    Tanaka, T.2    Kudo, T.3
  • 14
    • 0028176021 scopus 로고
    • GSK-3beta; is a dual specificity kinase differentially regulated by Tyrosine and Serine/Threonine phosphorylation
    • Wang Q M, Fiol C J, Anna A, et al. GSK-3beta; is a dual specificity kinase differentially regulated by Tyrosine and Serine/Threonine phosphorylation. J Biol Chem, 1994, 269 (20): 14566-14574
    • (1994) J Biol Chem , vol.269 , Issue.20 , pp. 14566-14574
    • Wang, Q.M.1    Fiol, C.J.2    Anna, A.3
  • 15
    • 0028967378 scopus 로고
    • Rapid Alzheimer-like phosphorylation of tau by the synergistic actions of non-proline-dependent protein kinases and GSK-3
    • Singh TJ, Haque N, Grundke-Iqbal I, et al. Rapid Alzheimer-like phosphorylation of tau by the synergistic actions of non-proline-dependent protein kinases and GSK-3. FEBS Letters, 1995, 358 (3): 267-272
    • (1995) FEBS Letters , vol.358 , Issue.3 , pp. 267-272
    • Singh, T.J.1    Haque, N.2    Grundke-Iqbal, I.3
  • 16
    • 0029994754 scopus 로고    scopus 로고
    • Phosphorylation of tau by glycogen synthase kinase-3 beta in intact mammalian cells: The effects on the organization and stability of microtubules
    • Lovestone S, Hartley C L, Pearce J, et al. Phosphorylation of tau by glycogen synthase kinase-3 beta in intact mammalian cells: the effects on the organization and stability of microtubules. Neuroscience, 1996, 3 (4): 1145-1157
    • (1996) Neuroscience , vol.3 , Issue.4 , pp. 1145-1157
    • Lovestone, S.1    Hartley, C.L.2    Pearce, J.3
  • 17
    • 0028981873 scopus 로고
    • Glycogen synthase kinase-3 beta phosphorylates tau protein at multiple sites in intact cells
    • Sperber B R, Leight S, Goedert M, et al. Glycogen synthase kinase-3 beta phosphorylates tau protein at multiple sites in intact cells. Neurosci Lett, 1995, 197 (2): 149-153
    • (1995) Neurosci Lett , vol.197 , Issue.2 , pp. 149-153
    • Sperber, B.R.1    Leight, S.2    Goedert, M.3
  • 18
    • 0032521599 scopus 로고    scopus 로고
    • Sequential phosphorylation of Tau by glycogen synthase kinase-3 beta and protein kinase A at Thr212 and Ser214 generates the Alzheimer-specific epitope of antibody AT100 and requires a paired-helical-filament-like conformation
    • Zheng-Fischhofer Q, Biernat J, Mandelkow E M, et al. Sequential phosphorylation of Tau by glycogen synthase kinase-3 beta and protein kinase A at Thr212 and Ser214 generates the Alzheimer-specific epitope of antibody AT100 and requires a paired-helical-filament-like conformation. Eur J Biochem, 1998, 252 (3): 542-552
    • (1998) Eur J Biochem , vol.252 , Issue.3 , pp. 542-552
    • Zheng-Fischhofer, Q.1    Biernat, J.2    Mandelkow, E.M.3
  • 19
    • 0034329543 scopus 로고    scopus 로고
    • Phosphorylation of human tau protein by microtubule-associated kinases: GSK3beta and cdk5 are key participants
    • Flaherty D B, Soria J P, Tomasiewicz H G, et al. Phosphorylation of human tau protein by microtubule-associated kinases: GSK3beta and cdk5 are key participants. J Neurosci Res, 2000, 62 (3): 463-472
    • (2000) J Neurosci Res , vol.62 , Issue.3 , pp. 463-472
    • Flaherty, D.B.1    Soria, J.P.2    Tomasiewicz, H.G.3
  • 20
    • 0036769733 scopus 로고    scopus 로고
    • GSK3beta signalling: Casting a wide net in Alzheimer's disease
    • Bhat R V, Budd S L. GSK3beta signalling: casting a wide net in Alzheimer's disease. Neurosignals, 2002, 11 (5): 251-261
    • (2002) Neurosignals , vol.11 , Issue.5 , pp. 251-261
    • Bhat, R.V.1    Budd, S.L.2
  • 22
    • 0028879044 scopus 로고
    • Overexpressed tau protein in cultured cells is phosphorylated without formation of PHF: Implication of phosphoprotein phosphatase involvement
    • Baum L, Seger R, Woodgett J R, et al. Overexpressed tau protein in cultured cells is phosphorylated without formation of PHF: implication of phosphoprotein phosphatase involvement. Brain Res Mol Brain Res, 1995, 34 (1): 1-17
    • (1995) Brain Res Mol Brain Res , vol.34 , Issue.1 , pp. 1-17
    • Baum, L.1    Seger, R.2    Woodgett, J.R.3
  • 23
    • 0030813929 scopus 로고    scopus 로고
    • Selective destruction of stable microtubules and axons by inhibitors of protein serine/threonine phosphatases in cultured human neurons
    • Merrick S E, Trojanowski J Q, Lee V M. Selective destruction of stable microtubules and axons by inhibitors of protein serine/threonine phosphatases in cultured human neurons. J Neurosci, 1997, 17 (15): 5726-5737
    • (1997) J Neurosci , vol.17 , Issue.15 , pp. 5726-5737
    • Merrick, S.E.1    Trojanowski, J.Q.2    Lee, V.M.3
  • 24
    • 0027531842 scopus 로고
    • The regulation of neurofilament protein dynamics by phosphorylation: Clues to neurofibrillary pathobiology
    • Nixon R A. The regulation of neurofilament protein dynamics by phosphorylation: clues to neurofibrillary pathobiology. Brain Pathol, 1993, 3 (1): 29-38
    • (1993) Brain Pathol , vol.3 , Issue.1 , pp. 29-38
    • Nixon, R.A.1
  • 25
    • 0018400102 scopus 로고
    • Characterization of the calcium-induced disruption of neurofilaments in rat peripheral nerve
    • Schlaepfer W W, Micko S. Characterization of the calcium-induced disruption of neurofilaments in rat peripheral nerve. Brain Res, 1979, 168 (2): 299-309
    • (1979) Brain Res , vol.168 , Issue.2 , pp. 299-309
    • Schlaepfer, W.W.1    Micko, S.2
  • 26
    • 0033778845 scopus 로고    scopus 로고
    • Accumulation of phosphorylated neurofilaments and increase in apoptosis-specific protein and phosphorylated c-Jun induced by proteasome inhibitors
    • Masaki R, Saito T, Yamada K, et al. Accumulation of phosphorylated neurofilaments and increase in apoptosis-specific protein and phosphorylated c-Jun induced by proteasome inhibitors. J Neurosci Res, 2000, 62 (1): 75-83
    • (2000) J Neurosci Res , vol.62 , Issue.1 , pp. 75-83
    • Masaki, R.1    Saito, T.2    Yamada, K.3
  • 27
    • 0034728670 scopus 로고    scopus 로고
    • β-Amyloid-induced calcium influx induces apoptosis in culture by oxidative stress rather than tau phosphorylation
    • Ekinci F J, Linsley M D, Shea T B. β-Amyloid-induced calcium influx induces apoptosis in culture by oxidative stress rather than tau phosphorylation. Molecular Brain Research, 2000, 76 (2): 389-395
    • (2000) Molecular Brain Research , vol.76 , Issue.2 , pp. 389-395
    • Ekinci, F.J.1    Linsley, M.D.2    Shea, T.B.3
  • 28
    • 1842505349 scopus 로고    scopus 로고
    • Melatonin protects SHSY5Y neuroblastoma cells from calyculin A-induces neurofilament impairment and neurotoxicity
    • Li S P, Deng Y Q, Wang Y P, et al. Melatonin protects SHSY5Y neuroblastoma cells from calyculin A-induces neurofilament impairment and neurotoxicity. J Pineal Res, 2004, 36 (3): 186-191
    • (2004) J Pineal Res , vol.36 , Issue.3 , pp. 186-191
    • Li, S.P.1    Deng, Y.Q.2    Wang, Y.P.3
  • 29
    • 0035929569 scopus 로고    scopus 로고
    • New leads on the "How" of Alzheimer's
    • Marx J. New leads on the "How" of Alzheimer's. Science, 2001, 293 (5538): 2192-2194
    • (2001) Science , vol.293 , Issue.5538 , pp. 2192-2194
    • Marx, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.