메뉴 건너뛰기




Volumn 13, Issue 4, 2003, Pages 440-451

A1 Adenosine Receptors Accumulate in Neurodegenerative Structures in Alzheimer Disease and Mediate Both Amyloid Precursor Protein Processing and Tau Phosphorylation and Translocation

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE A1 RECEPTOR; ADENOSINE A2A RECEPTOR; AMYLOID BETA PROTEIN; AMYLOID BETAA4 PROTEIN; AMYLOID PRECURSOR PROTEIN; METABOTROPIC RECEPTOR; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN KINASE C; PROTEIN P21; TAU PROTEIN; UNCLASSIFIED DRUG;

EID: 0242416171     PISSN: 10156305     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1750-3639.2003.tb00475.x     Document Type: Article
Times cited : (158)

References (44)
  • 1
    • 0000135440 scopus 로고    scopus 로고
    • Temporal sequence of Alzheimer's disease-related pathology
    • A Peters and JH Morrison (eds.), Kluwer Academic/Plenum Publishers, New York, Boston, Dordrecht, London, Moscow
    • Braak H, Braak E (1999) Temporal sequence of Alzheimer's disease-related pathology. In Cerebral cortex vol 14; Neurodegenerative and age-related changes in structure and function of cerebral cortex. A Peters and JH Morrison (eds.), Kluwer Academic/Plenum Publishers, New York, Boston, Dordrecht, London, Moscow. pp. 475-512.
    • (1999) Cerebral Cortex Vol 14; Neurodegenerative and Age-Related Changes in Structure and Function of Cerebral Cortex , vol.14 , pp. 475-512
    • Braak, H.1    Braak, E.2
  • 4
    • 0033758105 scopus 로고    scopus 로고
    • Microtubule-affinity regulating kinase (MARK) is tightly associated with neurofibrillary tangles in Alzheimer brain: A fluorescence resonance energy transfer study
    • Chin JY, Knowles RB, Schneider A, Drewes G, Mandelkow EM, Hyman BT (2000) Microtubule-affinity regulating kinase (MARK) is tightly associated with neurofibrillary tangles in Alzheimer brain: a fluorescence resonance energy transfer study. J Neuropathol Exp Neurol 59:966-971.
    • (2000) J Neuropathol Exp Neurol , vol.59 , pp. 966-971
    • Chin, J.Y.1    Knowles, R.B.2    Schneider, A.3    Drewes, G.4    Mandelkow, E.M.5    Hyman, B.T.6
  • 7
    • 0034049944 scopus 로고    scopus 로고
    • Proteolytic processing and cell biological functions of the amyloid precursor protein
    • De Strooper B, Annaert W (2000) Proteolytic processing and cell biological functions of the amyloid precursor protein. J Cell Sci 113:1857-1870.
    • (2000) J Cell Sci , vol.113 , pp. 1857-1870
    • De Strooper, B.1    Annaert, W.2
  • 8
    • 0031055415 scopus 로고    scopus 로고
    • Minimal Ras-binding domain of Raf1 can be used as an activation-specific probe for Ras
    • De Rooij J, Bos JL (1997) Minimal Ras-binding domain of Raf1 can be used as an activation-specific probe for Ras. Oncogene 14:623-625.
    • (1997) Oncogene , vol.14 , pp. 623-625
    • De Rooij, J.1    Bos, J.L.2
  • 10
    • 0034923094 scopus 로고    scopus 로고
    • The role and regulation of adenosine in the central nervous system
    • Dunwiddie TV, Masino SA (2001) The role and regulation of adenosine in the central nervous system. Annu Rev Neurosci 24:31-55.
    • (2001) Annu Rev Neurosci , vol.24 , pp. 31-55
    • Dunwiddie, T.V.1    Masino, S.A.2
  • 11
    • 0035659377 scopus 로고    scopus 로고
    • Phosphorylated mitogen-activated protein kinase (MAPK/ERK-P), protein kinase of 38 kDa (p38-P), stress-activated protein kinase (SAPK/JNK-P), and calcium/calmodulin-dependent kinase II (CaM kinase II) are differentially expressed in tau deposits in neurons and glial cells in tauopathies
    • Ferrer I, Blanco R, Carmona M, Puig B (2001a) Phosphorylated mitogen-activated protein kinase (MAPK/ERK-P), protein kinase of 38 kDa (p38-P), stress-activated protein kinase (SAPK/JNK-P), and calcium/calmodulin-dependent kinase II (CaM kinase II) are differentially expressed in tau deposits in neurons and glial cells in tauopathies. J Neural Transm 108:1397-1415.
    • (2001) J Neural Transm , vol.108 , pp. 1397-1415
    • Ferrer, I.1    Blanco, R.2    Carmona, M.3    Puig, B.4
  • 12
    • 0035094403 scopus 로고    scopus 로고
    • Phosphorylated MAP kinase (ERK, ERK2) expression is associated with early tau deposition in neurones and glial cells, but not with increased nuclear DNA vulnerability and cell death, in Alzheimer's disease, Pick's disease, progressive supranuclear palsy and corticobasal degenerationn
    • Ferrer I, Blanco R, Carmona M, Ribera R, Goutan E, Puig B, Rey MJ, Cardozo A, Viñals F, Ribalta T (2001 b) Phosphorylated MAP kinase (ERK, ERK2) expression is associated with early tau deposition in neurones and glial cells, but not with increased nuclear DNA vulnerability and cell death, in Alzheimer's disease, Pick's disease, progressive supranuclear palsy and corticobasal degenerationn. Brain Pathol 11:144-158.
    • (2001) Brain Pathol , vol.11 , pp. 144-158
    • Ferrer, I.1    Blanco, R.2    Carmona, M.3    Ribera, R.4    Goutan, E.5    Puig, B.6    Rey, M.J.7    Cardozo, A.8    Viñals, F.9    Ribalta, T.10
  • 14
    • 0036469258 scopus 로고    scopus 로고
    • Loss of stimulatory effect of guanosine triphosphate on [35S]GTPgammaS binding correlates with Alzheimer disease neurofibrillary pathology intentorhinal cortex and CA1 hippocampal subfield
    • García-Jiménez A, Cowburn RF, Ohm TG, Lasn H, Winblad B, Bogdanovic N, Fastbom J (2002) Loss of stimulatory effect of guanosine triphosphate on [35S]GTPgammaS binding correlates with Alzheimer disease neurofibrillary pathology intentorhinal cortex and CA1 hippocampal subfield. J Neurosci Res 67:388-398
    • (2002) J Neurosci Res , vol.67 , pp. 388-398
    • García-Jiménez, A.1    Cowburn, R.F.2    Ohm, T.G.3    Lasn, H.4    Winblad, B.5    Bogdanovic, N.6    Fastbom, J.7
  • 17
    • 0026784416 scopus 로고
    • p42 MAP kinase phosphorylation sites in microtubule-associated protein tau are dephosphorylated by protein phosphatase 2A1
    • Goedert M, Cohen ES, Jakes R, Cohen P (1992) p42 MAP kinase phosphorylation sites in microtubule-associated protein tau are dephosphorylated by protein phosphatase 2A1. FEBS Lett 312:95-99.
    • (1992) FEBS Lett , vol.312 , pp. 95-99
    • Goedert, M.1    Cohen, E.S.2    Jakes, R.3    Cohen, P.4
  • 18
    • 0037052633 scopus 로고    scopus 로고
    • MPP+ increases alpha-synuclein expression and ERK/MAP-kinase phosphorylation in human neuroblastoma SH-SY5Y cells
    • Gomez-Santos C, Ferrer I, Reiriz J, Vinals F, Barrachina M, Ambrosio S (2002) MPP+ increases alpha-synuclein expression and ERK/MAP-kinase phosphorylation in human neuroblastoma SH-SY5Y cells. Brain Res 935:32-39.
    • (2002) Brain Res , vol.935 , pp. 32-39
    • Gomez-Santos, C.1    Ferrer, I.2    Reiriz, J.3    Vinals, F.4    Barrachina, M.5    Ambrosio, S.6
  • 19
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy J, Selkoe DJ (2002) The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297:353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 20
    • 0036468772 scopus 로고    scopus 로고
    • Alzheimer's disease and Down's syndrome: Roles of APP, trophic factors and ACh
    • Isacson O, Seo H, Lin L, Albeck D, Granholm AC (2002) Alzheimer's disease and Down's syndrome: roles of APP, trophic factors and ACh. Trends Neurosci 25:79-84.
    • (2002) Trends Neurosci , vol.25 , pp. 79-84
    • Isacson, O.1    Seo, H.2    Lin, L.3    Albeck, D.4    Granholm, A.C.5
  • 22
    • 0034650631 scopus 로고    scopus 로고
    • Modulation of tau phosphorylation and intracellular localization by cellular stress
    • Jenkins SM, Zinnerman M, Garner C, Johnson GVW (2000) Modulation of tau phosphorylation and intracellular localization by cellular stress. Biochem J 345:263-270.
    • (2000) Biochem J , vol.345 , pp. 263-270
    • Jenkins, S.M.1    Zinnerman, M.2    Garner, C.3    Johnson, G.V.W.4
  • 23
    • 0034642236 scopus 로고    scopus 로고
    • Protein kinase C regulation of intracellular and cell surface amyloid precursor protein (APP) cleavage in CHO695 cells
    • Jolly-Tornetta C, Wolf B (2000) Protein kinase C regulation of intracellular and cell surface amyloid precursor protein (APP) cleavage in CHO695 cells. Biochemistry 39:15282-15290.
    • (2000) Biochemistry , vol.39 , pp. 15282-15290
    • Jolly-Tornetta, C.1    Wolf, B.2
  • 24
    • 0035957946 scopus 로고    scopus 로고
    • alpha 7 nicotinic receptor transduces signals to phosphatidylinositol 3-kinase to block A beta-amyloid-induced neurotoxicity
    • Kihara T, Shimohama S, Sawada H, Honda K, Nakamizo T, Shibasaki H, Kume T, Akaike A (2001) alpha 7 nicotinic receptor transduces signals to phosphatidylinositol 3-kinase to block A beta-amyloid-induced neurotoxicity. J Biol Chem 276:13541-13546.
    • (2001) J Biol Chem , vol.276 , pp. 13541-13546
    • Kihara, T.1    Shimohama, S.2    Sawada, H.3    Honda, K.4    Nakamizo, T.5    Shibasaki, H.6    Kume, T.7    Akaike, A.8
  • 25
    • 0036142817 scopus 로고    scopus 로고
    • Adenosine receptors: G protein-mediated signalling and the role of accessory proteins
    • Klinger M, Freissmuth M, Nanoff C (2002) Adenosine receptors: G protein-mediated signalling and the role of accessory proteins. Cell Signalling 14:99-108.
    • (2002) Cell Signalling , vol.14 , pp. 99-108
    • Klinger, M.1    Freissmuth, M.2    Nanoff, C.3
  • 26
    • 0032851485 scopus 로고    scopus 로고
    • Demonstration by fluorescence resonance energy transfer of a close association between activated MAP kinase and neurofibrillary tangles: Implications for MAP kinase activation in Alzheimer disease
    • Knowles RB, Chin J, Ruff CT, Hyman BT (1999) Demonstration by fluorescence resonance energy transfer of a close association between activated MAP kinase and neurofibrillary tangles: Implications for MAP kinase activation in Alzheimer disease. J Neuropathol Exp Neurol 58:1090-1098.
    • (1999) J Neuropathol Exp Neurol , vol.58 , pp. 1090-1098
    • Knowles, R.B.1    Chin, J.2    Ruff, C.T.3    Hyman, B.T.4
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, UK (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0026694067 scopus 로고
    • Implication of cdc2 and MAP2 kinases in the phosphorylation of tau proteins in Alzheimer's disease
    • Ledesma MD, Correas I, Avila J, Diaz-Nido J (1992) Implication of cdc2 and MAP2 kinases in the phosphorylation of tau proteins in Alzheimer's disease. FEBS Lett 308:218-224.
    • (1992) FEBS Lett , vol.308 , pp. 218-224
    • Ledesma, M.D.1    Correas, I.2    Avila, J.3    Diaz-Nido, J.4
  • 29
    • 0029147583 scopus 로고
    • Amyloid precursor protein processing is stimulated by metabotropic glutamate receptors
    • Lee RK, Wurtman RJ, Cox AJ, Nitsch RM (1995) Amyloid precursor protein processing is stimulated by metabotropic glutamate receptors. Proc Natl Acad Sci U S A 92:8083-8087.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 8083-8087
    • Lee, R.K.1    Wurtman, R.J.2    Cox, A.J.3    Nitsch, R.M.4
  • 30
    • 0030937952 scopus 로고    scopus 로고
    • The phosphorylation of tau: A critical stage in neurodevelopment and neurodegenerative processes
    • Lovestone S, Reynolds CH (1997) The phosphorylation of tau: a critical stage in neurodevelopment and neurodegenerative processes. Neuroscience 78:309-324.
    • (1997) Neuroscience , vol.78 , pp. 309-324
    • Lovestone, S.1    Reynolds, C.H.2
  • 32
    • 0036150827 scopus 로고    scopus 로고
    • Alzheimer's disease -do tauists and baptists finally shake hands?
    • Mudher A, Lovestone S (2002) Alzheimer's disease -do tauists and baptists finally shake hands? Trends Neurosci 25:22-26.
    • (2002) Trends Neurosci , vol.25 , pp. 22-26
    • Mudher, A.1    Lovestone, S.2
  • 33
    • 0030790252 scopus 로고    scopus 로고
    • Metabotropic glutamate receptor subtype mGluRlalpha stimulates the secretion of the amyloid beta-protein precursor ectodomain
    • Nitsch RM, Deng A, Wurtman RJ, Growdon JH (1997) Metabotropic glutamate receptor subtype mGluRlalpha stimulates the secretion of the amyloid beta-protein precursor ectodomain. J Neurochem 69:704-712.
    • (1997) J Neurochem , vol.69 , pp. 704-712
    • Nitsch, R.M.1    Deng, A.2    Wurtman, R.J.3    Growdon, J.H.4
  • 35
    • 0033944602 scopus 로고    scopus 로고
    • The heat shock cognate protein hsc73 assembles with A(1) adenosine receptors to form functional modules in the cell membrane
    • Sarrio S, Casado V, Escriche M, Ciruela F, Mallol J, Canela EI, Lluis O, Franco R (2000) The heat shock cognate protein hsc73 assembles with A(1) adenosine receptors to form functional modules in the cell membrane. Mol Cell Biol 20:5164-5174.
    • (2000) Mol Cell Biol , vol.20 , pp. 5164-5174
    • Sarrio, S.1    Casado, V.2    Escriche, M.3    Ciruela, F.4    Mallol, J.5    Canela, E.I.6    Lluis, O.7    Franco, R.8
  • 37
    • 0033851227 scopus 로고    scopus 로고
    • Human adenosine A1, A2A, A2b and A3 receptors expressed in Chinese hamster ovary cells all mediate the phosphorylation of extracellular-regulated kinase 1/2
    • Schulte G, Fredholm BB (2000) Human adenosine A1, A2A, A2b and A3 receptors expressed in Chinese hamster ovary cells all mediate the phosphorylation of extracellular-regulated kinase 1/2. Mol Pharmacol 58:477-482.
    • (2000) Mol Pharmacol , vol.58 , pp. 477-482
    • Schulte, G.1    Fredholm, B.B.2
  • 38
    • 0033613129 scopus 로고    scopus 로고
    • Cellular mechanisms of beta-amyloid production and secretion
    • Sinha S, Lieberburg I (1999) Cellular mechanisms of beta-amyloid production and secretion. Proc Natl Acad Sci U S A 96:11049-11053.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 11049-11053
    • Sinha, S.1    Lieberburg, I.2
  • 39
    • 0032101953 scopus 로고    scopus 로고
    • Metabotropic glutamate receptor activation in vivo induces intraneuronal amyloid immunoreactivity in guinea pig hippocampus
    • Stephenson DT, Clemens JA (1998) Metabotropic glutamate receptor activation in vivo induces intraneuronal amyloid immunoreactivity in guinea pig hippocampus. Neurochem Int 33:83-93.
    • (1998) Neurochem Int , vol.33 , pp. 83-93
    • Stephenson, D.T.1    Clemens, J.A.2
  • 40
    • 0035950188 scopus 로고    scopus 로고
    • New frontiers in Alzheimer's disease genetics
    • Tanzi RE, Bertram L (2001) New frontiers in Alzheimer's disease genetics. Neuron 25:181-184.
    • (2001) Neuron , vol.25 , pp. 181-184
    • Tanzi, R.E.1    Bertram, L.2
  • 41
    • 0032100631 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases (Erk1, 2) phosphorylate Lys-Ser-Pro (KSP) repeats in neurofilament proteins NF-H and NF-M
    • Veeranna GJ, Amin ND, Ahn NG, Jaffe J, Winters CA, Grant P, Pant HC (1998) Mitogen-activated protein kinases (Erk1, 2) phosphorylate Lys-Ser-Pro (KSP) repeats in neurofilament proteins NF-H and NF-M. J Neurosci 18:4008-4021.
    • (1998) J Neurosci , vol.18 , pp. 4008-4021
    • Veeranna, G.J.1    Amin, N.D.2    Ahn, N.G.3    Jaffe, J.4    Winters, C.A.5    Grant, P.6    Pant, H.C.7
  • 42
    • 0035477333 scopus 로고    scopus 로고
    • The cell biology of Alzheimer's disease: Uncovering the secrets of secretases
    • Walter J, Kaether C, Steiner H, Haass C (2001) The cell biology of Alzheimer's disease: uncovering the secrets of secretases. Curr Opin Neurobiol 11:585-590.
    • (2001) Curr Opin Neurobiol , vol.11 , pp. 585-590
    • Walter, J.1    Kaether, C.2    Steiner, H.3    Haass, C.4
  • 43
    • 0033782845 scopus 로고    scopus 로고
    • Activation of p38 kinase links tau phosphorylation, oxidative stress, and cell cycle-related events in Alzheimer disease
    • Zhu X, Rottkamp CA, Boux H, Takeda A, Perry G, Smith MA (2000) Activation of p38 kinase links tau phosphorylation, oxidative stress, and cell cycle-related events in Alzheimer disease. J Neuropathol Exp Neurol 59:880-888.
    • (2000) J Neuropathol Exp Neurol , vol.59 , pp. 880-888
    • Zhu, X.1    Rottkamp, C.A.2    Boux, H.3    Takeda, A.4    Perry, G.5    Smith, M.A.6
  • 44
    • 0035142804 scopus 로고    scopus 로고
    • Activation and re-distribution of c-Jun N-terminal kinase/stress activated protein kinase in degenerating neurons in Alzheimer's disease
    • Zhu X, Raina AK, Rottkamp CA, Aliev G, Perry G, Boux H, Smith MA (2001) Activation and re-distribution of c-Jun N-terminal kinase/stress activated protein kinase in degenerating neurons in Alzheimer's disease. J Neurochem 76:435-441.
    • (2001) J Neurochem , vol.76 , pp. 435-441
    • Zhu, X.1    Raina, A.K.2    Rottkamp, C.A.3    Aliev, G.4    Perry, G.5    Boux, H.6    Smith, M.A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.