메뉴 건너뛰기




Volumn 34, Issue 1, 2014, Pages 26-37

Curcumin attenuates amyloid-β-induced tau hyperphosphorylation in human neuroblastoma SH-SY5Y cells involving PTEN/Akt/GSK-3β signaling pathway

Author keywords

Alzheimer's disease; Amyloid ; Curcumin; GSK 3 ; PTEN; Tau hyperphosphorylation

Indexed keywords

AMYLOID BETA PROTEIN[1-40]; CURCUMIN; GLYCOGEN SYNTHASE KINASE 3BETA; HISTONE DEACETYLASE 6; INSULIN RECEPTOR; MESSENGER RNA; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PHOSPHOINOSITIDE DEPENDENT PROTEIN KINASE 1; PROTEIN KINASE B; PROTEIN P55; PROTEIN P85; TAU PROTEIN;

EID: 84893118788     PISSN: 10799893     EISSN: 15324281     Source Type: Journal    
DOI: 10.3109/10799893.2013.848891     Document Type: Article
Times cited : (80)

References (41)
  • 1
    • 58849143335 scopus 로고    scopus 로고
    • Accumulated amyloid-beta peptide and hyperphosphorylated tau protein: Relationship and links in Alzheimer's disease
    • Huang HC, Jiang ZF. Accumulated amyloid-beta peptide and hyperphosphorylated tau protein: relationship and links in Alzheimer's disease. J Alzheimers Dis 2009;16:15-27.
    • (2009) J Alzheimers Dis , vol.16 , pp. 15-27
    • Huang, H.C.1    Jiang, Z.F.2
  • 2
    • 80055039585 scopus 로고    scopus 로고
    • Amyloid-beta protein precursor family members: A review from homology to biological function
    • Huang HC, Jiang ZF. Amyloid-beta protein precursor family members: a review from homology to biological function. J Alzheimers Dis 2011;26:607-26.
    • (2011) J Alzheimers Dis , vol.26 , pp. 607-626
    • Huang, H.C.1    Jiang, Z.F.2
  • 3
    • 0025365401 scopus 로고
    • Platelet coagulation factor XIa-inhibitor, a form of Alzheimer amyloid precursor protein
    • Smith RP, Higuchi DA, Broze GJ, Jr. Platelet coagulation factor XIa-inhibitor, a form of Alzheimer amyloid precursor protein. Science 1990;248:1126-8.
    • (1990) Science , vol.248 , pp. 1126-1128
    • Smith, R.P.1    Higuchi, D.A.2    Broze Jr., G.J.3
  • 4
    • 0033301776 scopus 로고    scopus 로고
    • Neurite-outgrowth regulating functions of the amyloid protein precursor of Alzheimer's disease
    • Small DH, Clarris HL, Williamson TG, et al. Neurite-outgrowth regulating functions of the amyloid protein precursor of Alzheimer's disease. J Alzheimers Dis 1999;1:275-85.
    • (1999) J Alzheimers Dis , vol.1 , pp. 275-285
    • Small, D.H.1    Clarris, H.L.2    Williamson, T.G.3
  • 5
    • 0033012737 scopus 로고    scopus 로고
    • Mechanisms contributing to the deficits in hippocampal synaptic plasticity in mice lacking amyloid precursor protein
    • Seabrook GR, Smith DW, Bowery BJ, et al. Mechanisms contributing to the deficits in hippocampal synaptic plasticity in mice lacking amyloid precursor protein. Neuropharmacology 1999; 38:349-59.
    • (1999) Neuropharmacology , vol.38 , pp. 349-359
    • Seabrook, G.R.1    Smith, D.W.2    Bowery, B.J.3
  • 6
    • 34248172449 scopus 로고    scopus 로고
    • Structure and functions of the human amyloid precursor protein: The whole is more than the sum of its parts
    • Gralle M, Ferreira ST. Structure and functions of the human amyloid precursor protein: the whole is more than the sum of its parts. Prog Neurobiol 2007;82:11-32.
    • (2007) Prog Neurobiol , vol.82 , pp. 11-32
    • Gralle, M.1    Ferreira, S.T.2
  • 7
    • 84865455602 scopus 로고    scopus 로고
    • Amyloid precursor protein regulates netrin-1-mediated commissural axon outgrowth
    • Rama N, Goldschneider D, Corset V, et al. Amyloid precursor protein regulates netrin-1-mediated commissural axon outgrowth. J Biol Chem 2012;287:30014-23.
    • (2012) J Biol Chem , vol.287 , pp. 30014-30023
    • Rama, N.1    Goldschneider, D.2    Corset, V.3
  • 8
    • 84857641625 scopus 로고    scopus 로고
    • Ubiquitin is associated with early truncation of tau protein at aspartic acid421 during the maturation of neurofibrillary tangles in Alzheimer's disease
    • Garci'a-Sierra F, Jarero-Basulto JJ, Kristofikova K, et al. Ubiquitin is associated with early truncation of tau protein at aspartic acid421 during the maturation of neurofibrillary tangles in Alzheimer's disease. Brain Pathol 2012;22:240-50.
    • (2012) Brain Pathol , vol.22 , pp. 240-250
    • Garci'A-Sierra, F.1    Jarero-Basulto, J.J.2    Kristofikova, K.3
  • 9
    • 0026595846 scopus 로고
    • Tau proteins of Alzheimer paired helical filaments: Abnormal phosphorylation of all six brain isoforms
    • Goedert M, Spillantini MG, Cairns NJ, Crowther RA. Tau proteins of Alzheimer paired helical filaments: abnormal phosphorylation of all six brain isoforms. Neuron 1992;8(1):159-68.
    • (1992) Neuron , vol.8 , Issue.1 , pp. 159-168
    • Goedert, M.1    Spillantini, M.G.2    Cairns, N.J.3    Crowther, R.A.4
  • 10
    • 0033850407 scopus 로고    scopus 로고
    • Tau protein isoforms, phosphorylation and role in neurodegenerative disorders
    • Buee L, Bussiere T, Buee-Scherrer V, et al. Tau protein isoforms, phosphorylation and role in neurodegenerative disorders. Brain Res Brain Res Rev 2000;33:95-130.
    • (2000) Brain Res Brain Res Rev , vol.33 , pp. 95-130
    • Buee, L.1    Bussiere, T.2    Buee-Scherrer, V.3
  • 11
    • 79551510136 scopus 로고    scopus 로고
    • Tau protein is required for amyloid {beta}-induced impairment of hippocampal long-term potentiation
    • Shipton OA, Leitz JR, Dworzak J, et al. Tau protein is required for amyloid {beta}-induced impairment of hippocampal long-term potentiation. J Neurosci 2011;31:1688-92.
    • (2011) J Neurosci , vol.31 , pp. 1688-1692
    • Shipton, O.A.1    Leitz, J.R.2    Dworzak, J.3
  • 12
    • 84866478442 scopus 로고    scopus 로고
    • The synaptic accumulation of hyperphosphorylated tau oligomers in Alzheimer disease is associated with dysfunction of the ubiquitin-proteasome system
    • Tai HC, Serrano-Pozo A, Hashimoto T, et al. The synaptic accumulation of hyperphosphorylated tau oligomers in Alzheimer disease is associated with dysfunction of the ubiquitin-proteasome system. Am J Pathol 2012;181:1426-35.
    • (2012) Am J Pathol , vol.181 , pp. 1426-1435
    • Tai, H.C.1    Serrano-Pozo, A.2    Hashimoto, T.3
  • 13
    • 0026597063 scopus 로고
    • Alzheimer's disease: The amyloid cascade hypothesis
    • Hardy JA, Higgins GA. Alzheimer's disease: the amyloid cascade hypothesis. Science 1992;256:184-5.
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 14
    • 84882939776 scopus 로고    scopus 로고
    • Advances in the pathogenesis of Alzheimer's disease: A re-evaluation of amyloid cascade hypothesis
    • Dong S, Duan Y, Hu Y, Zhao Z. Advances in the pathogenesis of Alzheimer's disease: a re-evaluation of amyloid cascade hypothesis. Transl Neurodegener 2012;1:18.
    • (2012) Transl Neurodegener , vol.1 , pp. 18
    • Dong, S.1    Duan, Y.2    Hu, Y.3    Zhao, Z.4
  • 15
    • 79955645442 scopus 로고    scopus 로고
    • Curcuminoid binds to amyloid-beta1-42 oligomer and fibril
    • Yanagisawa D, Taguchi H, Yamamoto A, et al. Curcuminoid binds to amyloid-beta1-42 oligomer and fibril. J Alzheimers Dis 2011;24: 33-42.
    • (2011) J Alzheimers Dis , vol.24 , pp. 33-42
    • Yanagisawa, D.1    Taguchi, H.2    Yamamoto, A.3
  • 16
    • 84856803616 scopus 로고    scopus 로고
    • Binding of curcumin to senile plaques and cerebral amyloid angiopathy in the aged brain of various animals and to neurofibrillary tangles in Alzheimer's brain
    • Mutsuga M, Chambers JK, Uchida K, et al. Binding of curcumin to senile plaques and cerebral amyloid angiopathy in the aged brain of various animals and to neurofibrillary tangles in Alzheimer's brain. J Vet Med Sci 2012;74:51-7.
    • (2012) J Vet Med Sci , vol.74 , pp. 51-57
    • Mutsuga, M.1    Chambers, J.K.2    Uchida, K.3
  • 17
    • 20044370990 scopus 로고    scopus 로고
    • Curcumin inhibits formation of amyloid beta oligomers and fibrils, binds plaques, and reduces amyloid in vivo
    • Yang F, Lim GP, Begum AN, et al. Curcumin inhibits formation of amyloid beta oligomers and fibrils, binds plaques, and reduces amyloid in vivo. J Biol Chem 2005;280:5892-901.
    • (2005) J Biol Chem , vol.280 , pp. 5892-5901
    • Yang, F.1    Lim, G.P.2    Begum, A.N.3
  • 18
    • 77956498654 scopus 로고    scopus 로고
    • Curcumin decreases amyloid-beta peptide levels by attenuating the maturation of amyloid-beta precursor protein
    • Zhang C, Browne A, Child D, Tanzi RE. Curcumin decreases amyloid-beta peptide levels by attenuating the maturation of amyloid-beta precursor protein. J Biol Chem 2010;285: 28472-80.
    • (2010) J Biol Chem , vol.285 , pp. 28472-28480
    • Zhang, C.1    Browne, A.2    Child, D.3    Tanzi, R.E.4
  • 19
    • 77957337974 scopus 로고    scopus 로고
    • The inhibitory effects of different curcuminoids on beta-amyloid protein, beta-amyloid precursor protein and beta-site amyloid precursor protein cleaving enzyme 1 in swAPP HEK293 cells
    • Liu H, Li Z, Qiu D, et al. The inhibitory effects of different curcuminoids on beta-amyloid protein, beta-amyloid precursor protein and beta-site amyloid precursor protein cleaving enzyme 1 in swAPP HEK293 cells. Neurosci Lett 2010;485: 83-8.
    • (2010) Neurosci Lett , vol.485 , pp. 83-88
    • Liu, H.1    Li, Z.2    Qiu, D.3
  • 20
    • 84872956586 scopus 로고    scopus 로고
    • Curcumin as a potential treatment for Alzheimer's disease: A study of the effects of curcumin on hippocampal expression of glial fibrillary acidic protein
    • Wang Y, Yin H, Wang L, et al. Curcumin as a potential treatment for Alzheimer's disease: a study of the effects of curcumin on hippocampal expression of glial fibrillary acidic protein. Am J Chin Med 2013;41:59-70.
    • (2013) Am J Chin Med , vol.41 , pp. 59-70
    • Wang, Y.1    Yin, H.2    Wang, L.3
  • 21
    • 84862866441 scopus 로고    scopus 로고
    • Protective effects of curcumin on amyloid-beta-induced neuronal oxidative damage
    • Huang HC, Chang P, Dai XL, Jiang ZF. Protective effects of curcumin on amyloid-beta-induced neuronal oxidative damage. Neurochem Res 2012;37:1584-97.
    • (2012) Neurochem Res , vol.37 , pp. 1584-1597
    • Huang, H.C.1    Chang, P.2    Dai, X.L.3    Jiang, Z.F.4
  • 22
    • 84871451491 scopus 로고    scopus 로고
    • Curcumin-mediated neuroprotection against amyloid-beta-induced mitochondrial dysfunction involves the inhibition of GSK-3beta
    • Huang HC, Xu K, Jiang ZF. Curcumin-mediated neuroprotection against amyloid-beta-induced mitochondrial dysfunction involves the inhibition of GSK-3beta. J Alzheimers Dis 2012; 32:981-96.
    • (2012) J Alzheimers Dis , vol.32 , pp. 981-996
    • Huang, H.C.1    Xu, K.2    Jiang, Z.F.3
  • 23
    • 84856604061 scopus 로고    scopus 로고
    • GSK-3beta regulates cell growth, migration, and angiogenesis via Fbw7 and USP28- dependent degradation of HIF-1alpha
    • Flugel D, Gorlach A, Kietzmann T. GSK-3beta regulates cell growth, migration, and angiogenesis via Fbw7 and USP28- dependent degradation of HIF-1alpha. Blood 2012;119: 1292-301.
    • (2012) Blood , vol.119 , pp. 1292-1301
    • Flugel, D.1    Gorlach, A.2    Kietzmann, T.3
  • 24
    • 84865519156 scopus 로고    scopus 로고
    • GSK-3alpha and GSK-3beta proteins are involved in early stages of chondrocyte differentiation with functional redundancy through RelA protein phosphorylation
    • Itoh S, Saito T, Hirata M, et al. GSK-3alpha and GSK-3beta proteins are involved in early stages of chondrocyte differentiation with functional redundancy through RelA protein phosphorylation. J Biol Chem 2012;287:29227-36.
    • (2012) J Biol Chem , vol.287 , pp. 29227-29236
    • Itoh, S.1    Saito, T.2    Hirata, M.3
  • 25
    • 84866744899 scopus 로고    scopus 로고
    • Berberine ameliorates betaamyloid pathology, gliosis, and cognitive impairment in an Alzheimer's disease transgenic mouse model
    • Durairajan SS, Liu LF, Lu JH, et al. Berberine ameliorates betaamyloid pathology, gliosis, and cognitive impairment in an Alzheimer's disease transgenic mouse model. Neurobiol Aging 2012;33:2903-19.
    • (2012) Neurobiol Aging , vol.33 , pp. 2903-2919
    • Durairajan, S.S.1    Liu, L.F.2    Lu, J.H.3
  • 26
    • 40449098952 scopus 로고    scopus 로고
    • Amyloid activates GSK- 3beta to aggravate neuronal tauopathy in bigenic mice
    • Terwel D, Muyllaert D, Dewachter I, et al. Amyloid activates GSK- 3beta to aggravate neuronal tauopathy in bigenic mice. Am J Pathol 2008;172:786-98.
    • (2008) Am J Pathol , vol.172 , pp. 786-798
    • Terwel, D.1    Muyllaert, D.2    Dewachter, I.3
  • 27
    • 84855484573 scopus 로고    scopus 로고
    • Evidence for irreversible inhibition of glycogen synthase kinase-3beta by tideglusib
    • Dominguez JM, Fuertes A, Orozco L, et al. Evidence for irreversible inhibition of glycogen synthase kinase-3beta by tideglusib. J Biol Chem 2012;287:893-904.
    • (2012) J Biol Chem , vol.287 , pp. 893-904
    • Dominguez, J.M.1    Fuertes, A.2    Orozco, L.3
  • 28
    • 84865405744 scopus 로고    scopus 로고
    • Alzheimer's disease, beta-amyloid, glutamate, NMDA receptors and memantine - Searching for the connections
    • Danysz W, Parsons CG. Alzheimer's disease, beta-amyloid, glutamate, NMDA receptors and memantine - searching for the connections. Br J Pharmacol 2012;167:324-52.
    • (2012) Br J Pharmacol , vol.167 , pp. 324-352
    • Danysz, W.1    Parsons, C.G.2
  • 29
    • 0346216156 scopus 로고    scopus 로고
    • Type 2 diabetes and atrophy of medial temporal lobe structures on brain MRI
    • den Heijer T, Vermeer SE, van Dijk EJ, et al. Type 2 diabetes and atrophy of medial temporal lobe structures on brain MRI. Diabetologia 2003;46:1604-10.
    • (2003) Diabetologia , vol.46 , pp. 1604-1610
    • Den Heijer, T.1    Vermeer, S.E.2    Van Dijk, E.J.3
  • 30
    • 33644585223 scopus 로고    scopus 로고
    • Therapy insight: Type 2 diabetes mellitus and the risk of late-onset Alzheimer's disease
    • Haan MN. Therapy insight: type 2 diabetes mellitus and the risk of late-onset Alzheimer's disease. Nat Clin Pract Neurol 2006;2: 159-66.
    • (2006) Nat Clin Pract Neurol , vol.2 , pp. 159-166
    • Haan, M.N.1
  • 31
    • 84856496197 scopus 로고    scopus 로고
    • Brain insulin resistance and deficiency as therapeutic targets in Alzheimer's disease
    • de la Monte SM. Brain insulin resistance and deficiency as therapeutic targets in Alzheimer's disease. Curr Alzheimer Res 2012;9:35-66.
    • (2012) Curr Alzheimer Res , vol.9 , pp. 35-66
    • De La Monte, S.M.1
  • 32
    • 84863011816 scopus 로고    scopus 로고
    • TLR2 is a primary receptor for Alzheimer's amyloid b peptide to trigger neuroinflammatory activation
    • Liu S, Liu Y, Hao WL, et al. TLR2 is a primary receptor for Alzheimer's amyloid b peptide to trigger neuroinflammatory activation. J. Immunol 2012;188:1098-107.
    • (2012) J. Immunol , vol.188 , pp. 1098-1107
    • Liu, S.1    Liu, Y.2    Hao, W.L.3
  • 33
    • 77956587739 scopus 로고    scopus 로고
    • Abeta oligomers cause localized Ca(2) elevation, missorting of endogenous tau into dendrites, tau phosphorylation, and destruction of microtubules and spines
    • Zempel H, Thies E, Mandelkow E, Mandelkow EM. Abeta oligomers cause localized Ca(2) elevation, missorting of endogenous tau into dendrites, tau phosphorylation, and destruction of microtubules and spines. J Neurosci 2010;30:11938-50.
    • (2010) J Neurosci , vol.30 , pp. 11938-11950
    • Zempel, H.1    Thies, E.2    Mandelkow, E.3    Mandelkow, E.M.4
  • 34
    • 77949267093 scopus 로고    scopus 로고
    • Amyloid beta oligomers induce Ca2 dysregulation and neuronal death through activation of ionotropic glutamate receptors
    • Alberdi E, Sanchez-Gomez MV, Cavaliere F, et al. Amyloid beta oligomers induce Ca2 dysregulation and neuronal death through activation of ionotropic glutamate receptors. Cell Calcium 2010;47: 264-72.
    • (2010) Cell Calcium , vol.47 , pp. 264-272
    • Alberdi, E.1    Sanchez-Gomez, M.V.2    Cavaliere, F.3
  • 35
    • 60349093657 scopus 로고    scopus 로고
    • The role of Abetainduced calcium dysregulation in the pathogenesis of Alzheimer's disease
    • Small DH, Gasperini R, Vincent AJ, et al. The role of Abetainduced calcium dysregulation in the pathogenesis of Alzheimer's disease. J Alzheimers Dis 2009;16:225-33.
    • (2009) J Alzheimers Dis , vol.16 , pp. 225-233
    • Small, D.H.1    Gasperini, R.2    Vincent, A.J.3
  • 36
    • 84866468436 scopus 로고    scopus 로고
    • Amyloid-beta peptide 1-42 causes microtubule deregulation through N-methyl-D-aspartate receptors in mature hippocampal cultures
    • Mota SI, Ferreira IL, Pereira C, et al. Amyloid-beta peptide 1-42 causes microtubule deregulation through N-methyl-D-aspartate receptors in mature hippocampal cultures. Curr Alzheimer Res 2012;9:844-56.
    • (2012) Curr Alzheimer Res , vol.9 , pp. 844-856
    • Mota, S.I.1    Ferreira, I.L.2    Pereira, C.3
  • 37
    • 84867525210 scopus 로고    scopus 로고
    • Selective impairment of some forms of synaptic plasticity by oligomeric amyloid-beta peptide in the mouse hippocampus: Implication of extrasynaptic NMDA receptors
    • Kervern M, Angeli A, Nicole O, et al. Selective impairment of some forms of synaptic plasticity by oligomeric amyloid-beta peptide in the mouse hippocampus: implication of extrasynaptic NMDA receptors. J Alzheimers Dis 2012;32(1):183-96.
    • (2012) J Alzheimers Dis , vol.32 , Issue.1 , pp. 183-196
    • Kervern, M.1    Angeli, A.2    Nicole, O.3
  • 38
    • 79958844396 scopus 로고    scopus 로고
    • Tolerability and efficacy of memantine add-on therapy to rivastigmine transdermal patches in mild to moderate Alzheimer's disease: A multicenter, randomized, open-label, parallel-group study
    • Choi SH, Park KW, Na DL, et al. Tolerability and efficacy of memantine add-on therapy to rivastigmine transdermal patches in mild to moderate Alzheimer's disease: a multicenter, randomized, open-label, parallel-group study. Curr Med Res Opin 2011;27: 1375-83.
    • (2011) Curr Med Res Opin , vol.27 , pp. 1375-1383
    • Choi, S.H.1    Park, K.W.2    Na, D.L.3
  • 40
    • 84871452231 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and cellular metabolic deficiency in Alzheimer's disease
    • Gu XM, Huang HC, Jiang ZF. Mitochondrial dysfunction and cellular metabolic deficiency in Alzheimer's disease. Neurosci Bull 2012;28:631-40.
    • (2012) Neurosci Bull , vol.28 , pp. 631-640
    • Gu, X.M.1    Huang, H.C.2    Jiang, Z.F.3
  • 41
    • 0013079948 scopus 로고    scopus 로고
    • An intracellular protein that binds amyloid-beta peptide and mediates neurotoxicity in Alzheimer's disease
    • Yan SD, Fu J, Soto C, et al. An intracellular protein that binds amyloid-beta peptide and mediates neurotoxicity in Alzheimer's disease. Nature 1997;389:689-95.
    • (1997) Nature , vol.389 , pp. 689-695
    • Yan, S.D.1    Fu, J.2    Soto, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.