메뉴 건너뛰기




Volumn 26, Issue 3, 2004, Pages 387-395

Monitoring protein phosphatase 1 isoform levels as a marker for cellular stress

Author keywords

Abeta; Aluminium; Alzheimer's disease; Oxidative stress; Phosphorylation

Indexed keywords

ALUMINUM; HEAT SHOCK PROTEIN; PEPTIDE; PHOSPHOPROTEIN PHOSPHATASE 1; SODIUM AZIDE;

EID: 2042447806     PISSN: 08920362     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ntt.2003.12.007     Document Type: Article
Times cited : (33)

References (45)
  • 1
    • 0030922920 scopus 로고    scopus 로고
    • Spinophilin, a novel protein phosphatase 1 binding protein localized to dendritic spines
    • Allen P.B., Ouimet C.C., Greengard P. Spinophilin, a novel protein phosphatase 1 binding protein localized to dendritic spines. Proc. Natl. Acad. Sci. U. S. A. 94:1997;9956-9961
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 9956-9961
    • Allen, P.B.1    Ouimet, C.C.2    Greengard, P.3
  • 2
    • 2442770824 scopus 로고    scopus 로고
    • Lipid peroxidation facilitates aluminium accumulation in rat brain synaptosomes
    • Amador F.C., Santos M.S., Oliveira C.R. Lipid peroxidation facilitates aluminium accumulation in rat brain synaptosomes. J. Toxicol. Environ. Health. 58:1999;427-435
    • (1999) J. Toxicol. Environ. Health , vol.58 , pp. 427-435
    • Amador, F.C.1    Santos, M.S.2    Oliveira, C.R.3
  • 3
    • 0034793125 scopus 로고    scopus 로고
    • Lipid peroxidation and aluminium effects on the cholinergic system in nerve terminals
    • Amador F.C., Santos M.S., Oliveira C.R. Lipid peroxidation and aluminium effects on the cholinergic system in nerve terminals. Neurotox. Res. 3:2001;223-233
    • (2001) Neurotox. Res. , vol.3 , pp. 223-233
    • Amador, F.C.1    Santos, M.S.2    Oliveira, C.R.3
  • 4
    • 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., Kawabata S., Maruyama K., Koyama M., Silver J., Saitoh T. Overexpressed tau protein in cultured cells is phosphorylated without formation of PHF: implication of phosphoprotein phosphatase involvement. Brain Res. Mol. Brain Res. 34:1995;1-17
    • (1995) Brain Res. Mol. Brain Res. , vol.34 , pp. 1-17
    • Baum, L.1    Seger, R.2    Woodgett, J.R.3    Kawabata, S.4    Maruyama, K.5    Koyama, M.6    Silver, J.7    Saitoh, T.8
  • 5
    • 0037305525 scopus 로고    scopus 로고
    • Aluminum and copper interact in the promotion of oxidative but not inflammatory events: Implications for Alzheimer's disease
    • Becaria A., Bondy S.C., Campbell A. Aluminum and copper interact in the promotion of oxidative but not inflammatory events: implications for Alzheimer's disease. J. Alzheimer's Dis. 5:2003;31-38
    • (2003) J. Alzheimer's Dis. , vol.5 , pp. 31-38
    • Becaria, A.1    Bondy, S.C.2    Campbell, A.3
  • 6
    • 0034680902 scopus 로고    scopus 로고
    • Role of protein phosphatase-2A and 1- in the regulation of GSK-3, cdk5 and cdc2 and the phosphorylation of tau in rat forebrain
    • Bennecib M., Gong C.X., Grundke-Iqbal I., Iqbal K. Role of protein phosphatase-2A and 1- in the regulation of GSK-3, cdk5 and cdc2 and the phosphorylation of tau in rat forebrain. FEBS Lett. 485:2000;87-93
    • (2000) FEBS Lett. , vol.485 , pp. 87-93
    • Bennecib, M.1    Gong, C.X.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 7
    • 0031892689 scopus 로고    scopus 로고
    • Effect of aluminium on acetyl-CoA and acetylcholine metabolism in nerve terminals
    • Bielarczyk H., Tomaszewicz M., Szutowicz A. Effect of aluminium on acetyl-CoA and acetylcholine metabolism in nerve terminals. J. Neurochem. 70:1998;1175-1181
    • (1998) J. Neurochem. , vol.70 , pp. 1175-1181
    • Bielarczyk, H.1    Tomaszewicz, M.2    Szutowicz, A.3
  • 8
    • 0019551730 scopus 로고
    • "Western blotting": Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein a
    • Burnette W.N. "Western blotting": electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal. Biochem. 112:1981;195-203
    • (1981) Anal. Biochem. , vol.112 , pp. 195-203
    • Burnette, W.N.1
  • 9
    • 0035757529 scopus 로고    scopus 로고
    • Beta-amyloid, neuronal death and Alzheimer's disease
    • Carter J., Lippa C.F. Beta-amyloid, neuronal death and Alzheimer's disease. Curr. Mol. Med. 1:2001;733-777
    • (2001) Curr. Mol. Med. , vol.1 , pp. 733-777
    • Carter, J.1    Lippa, C.F.2
  • 10
    • 0036010598 scopus 로고    scopus 로고
    • Regulator-driven functional diversification of protein phosphatase-1 in eukaryotic evolution
    • Ceulemans H., Stalmans W., Bollen M. Regulator-driven functional diversification of protein phosphatase-1 in eukaryotic evolution. Bioessays. 24:2002;371-381
    • (2002) Bioessays , vol.24 , pp. 371-381
    • Ceulemans, H.1    Stalmans, W.2    Bollen, M.3
  • 11
    • 0037135276 scopus 로고    scopus 로고
    • Early chronic aluminium exposure impairs long-term potentiation and depression to the rat dentate gyrus in vivo
    • Chen J., Wang M., Ruan D., She J. Early chronic aluminium exposure impairs long-term potentiation and depression to the rat dentate gyrus in vivo. Neuroscience. 112:2002;879-887
    • (2002) Neuroscience , vol.112 , pp. 879-887
    • Chen, J.1    Wang, M.2    Ruan, D.3    She, J.4
  • 12
    • 0037081563 scopus 로고    scopus 로고
    • Protein phosphatase 1 - Targeted in many directions
    • Cohen P.T.W. Protein phosphatase 1 - targeted in many directions. J. Cell Sci. 115:2002;241-256
    • (2002) J. Cell Sci. , vol.115 , pp. 241-256
    • Cohen, P.T.W.1
  • 14
    • 0029328289 scopus 로고
    • Inhibition of protein phosphatase 1 stimulates secretion of Alzheimer amyloid precursor protein
    • da Cruz e Silva E.F., da Cruz e Silva O.A.B., Zaia C.T.B.V., Greengard P. Inhibition of protein phosphatase 1 stimulates secretion of Alzheimer amyloid precursor protein. Mol. Med. 1:1995;535-541
    • (1995) Mol. Med. , vol.1 , pp. 535-541
    • Da Cruz Silva, E.E.F.1    Da Cruz Silva, E.O.A.B.2    Zaia, C.T.B.V.3    Greengard, P.4
  • 17
    • 0029040355 scopus 로고
    • In situ evidence for DNA fragmentation in Huntington's disease striatum and Alzheimer's disease temporal lobes
    • Dragunow M., Faull R.L., Lawlor P., Beilharz E.J., Singleton K., Walker E.B., Mee E. In situ evidence for DNA fragmentation in Huntington's disease striatum and Alzheimer's disease temporal lobes. NeuroReport. 6:1995;1053-1057
    • (1995) NeuroReport , vol.6 , pp. 1053-1057
    • Dragunow, M.1    Faull, R.L.2    Lawlor, P.3    Beilharz, E.J.4    Singleton, K.5    Walker, E.B.6    Mee, E.7
  • 18
    • 0028200649 scopus 로고
    • Inhibition of energy metabolism alters the processing of amyloid precursor protein and induces a potentially amyloidogenic derivative
    • Gabuzda D., Busciglio J., Chen L.B., Matsudaira P., Yankner B.A. Inhibition of energy metabolism alters the processing of amyloid precursor protein and induces a potentially amyloidogenic derivative. J. Biol. Chem. 269:1994;13623-13628
    • (1994) J. Biol. Chem. , vol.269 , pp. 13623-13628
    • Gabuzda, D.1    Busciglio, J.2    Chen, L.B.3    Matsudaira, P.4    Yankner, B.A.5
  • 21
    • 0035976761 scopus 로고    scopus 로고
    • Abeta(1-42) and aluminum induce stress in the endoplasmic reticulum in rabbit hippocampus, involving nuclear translocation of gadd 153 and NF-kappaB
    • Ghribi O., Herman M.M., DeWitt D.A., Forbes M.S., Savory J. Abeta(1-42) and aluminum induce stress in the endoplasmic reticulum in rabbit hippocampus, involving nuclear translocation of gadd 153 and NF-kappaB. Brain Res. Mol. Brain Res. 30:2001;30-38
    • (2001) Brain Res. Mol. Brain Res. , vol.30 , pp. 30-38
    • Ghribi, O.1    Herman, M.M.2    Dewitt, D.A.3    Forbes, M.S.4    Savory, J.5
  • 22
    • 0035798093 scopus 로고    scopus 로고
    • The neurobiology of slow synaptic transmission
    • Greengard P. The neurobiology of slow synaptic transmission. Science. 294:2001;1024-1030
    • (2001) Science , vol.294 , pp. 1024-1030
    • Greengard, P.1
  • 24
    • 0021610573 scopus 로고
    • Improved technique utilizing nonfat dry milk for analysis of proteins and nucleic acids transferred to nitrocellulose
    • Johnson D.A., Gautsch J.W., Sportsman J.R., Elder J.H. Improved technique utilizing nonfat dry milk for analysis of proteins and nucleic acids transferred to nitrocellulose. Gene Anal. Tech. 1:1984;3
    • (1984) Gene Anal. Tech. , vol.1 , pp. 3
    • Johnson, D.A.1    Gautsch, J.W.2    Sportsman, J.R.3    Elder, J.H.4
  • 25
    • 0037013327 scopus 로고    scopus 로고
    • Intracellular amyloid-beta 1-42, but not extracellular soluble amyloid-beta peptides, induces neuronal apoptosis
    • Kienlen-Campard P., Miolet S., Tasiaux B., Octave J.N. Intracellular amyloid-beta 1-42, but not extracellular soluble amyloid-beta peptides, induces neuronal apoptosis. J. Biol. Chem. 277:2002;15666-15670
    • (2002) J. Biol. Chem. , vol.277 , pp. 15666-15670
    • Kienlen-Campard, P.1    Miolet, S.2    Tasiaux, B.3    Octave, J.N.4
  • 26
    • 0003084580 scopus 로고
    • Mechanisms of aluminium neurotoxicity - Relevance to human disease
    • H. Sigel, & A. Siegel. New York: Marcel Dekker
    • Kruck T.P.A., McLachlan D.R. Mechanisms of aluminium neurotoxicity - relevance to human disease. Sigel H., Siegel A. Metal ions in Biological Systems. 1988;285-314 Marcel Dekker, New York
    • (1988) Metal Ions in Biological Systems , pp. 285-314
    • Kruck, T.P.A.1    McLachlan, D.R.2
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0024341227 scopus 로고
    • A mechanism for the Hebb and the anti-Hebb processes underlying learning and memory
    • Lisman J. A mechanism for the Hebb and the anti-Hebb processes underlying learning and memory. Proc. Natl. Acad. Sci. U. S. A. 86:1989;9574-9578
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 9574-9578
    • Lisman, J.1
  • 29
    • 0027941257 scopus 로고
    • Synaptic plasticity in the hippocampus
    • Malenka R.C. Synaptic plasticity in the hippocampus. Cell. 78:1994;535-538
    • (1994) Cell , vol.78 , pp. 535-538
    • Malenka, R.C.1
  • 30
    • 0032487648 scopus 로고    scopus 로고
    • Amyloid beta-peptide induces apoptosis-related events in synapses and dendrites
    • Mattson M.P., Partin J., Begley J.G. Amyloid beta-peptide induces apoptosis-related events in synapses and dendrites. Brain Res. 807:1998;167-176
    • (1998) Brain Res. , vol.807 , pp. 167-176
    • Mattson, M.P.1    Partin, J.2    Begley, J.G.3
  • 31
    • 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. 17:1997;5726-5737
    • (1997) J. Neurosci. , vol.17 , pp. 5726-5737
    • Merrick, S.E.1    Trojanowski, J.Q.2    Lee, V.M.3
  • 33
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J. Immunol. Methods. 65:1983;55-63
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 34
    • 0036808469 scopus 로고    scopus 로고
    • Gene expression profiles of cholinergic nucleus basalis neurons in Alzheimer's disease
    • Mufson E.J., Counts S.E., Ginsberg S.D. Gene expression profiles of cholinergic nucleus basalis neurons in Alzheimer's disease. Neurochem. Res. 27:2002;1035-1048
    • (2002) Neurochem. Res. , vol.27 , pp. 1035-1048
    • Mufson, E.J.1    Counts, S.E.2    Ginsberg, S.D.3
  • 35
    • 0028176087 scopus 로고
    • Involvement of a calcineurin/inhibitor-1 phosphatase cascade in hippocampal long-term depression
    • Mulkey R.M., Endo S., Shenolikar S., Malenka R. Involvement of a calcineurin/inhibitor-1 phosphatase cascade in hippocampal long-term depression. Nature. 369:1994;486-488
    • (1994) Nature , vol.369 , pp. 486-488
    • Mulkey, R.M.1    Endo, S.2    Shenolikar, S.3    Malenka, R.4
  • 37
    • 0000722956 scopus 로고
    • Aluminum and Alzheimer's disease: Methodologic approaches
    • H. Sigel, & A. Siegel. New York: Marcel Dekker
    • Perl D.P. Aluminum and Alzheimer's disease: methodologic approaches. Sigel H., Siegel A. Metal Ions in Biological Systems. 1988;259-283 Marcel Dekker, New York
    • (1988) Metal Ions in Biological Systems , pp. 259-283
    • Perl, D.P.1
  • 38
    • 0028170809 scopus 로고
    • Protein serine/threonine phosphatases - New avenues for cell regulation
    • Shenolikar S. Protein serine/threonine phosphatases - new avenues for cell regulation. Annu. Rev. Cell Biol. 10:1994;55-86
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 55-86
    • Shenolikar, S.1
  • 40
    • 0028577208 scopus 로고
    • Immunohistochemical evidence for apoptosis in Alzheimer's disease
    • Su J.H., Anderson A.J., Cummings B.J., Cotman C.W. Immunohistochemical evidence for apoptosis in Alzheimer's disease. NeuroReport. 5:1994;2529-2533
    • (1994) NeuroReport , vol.5 , pp. 2529-2533
    • Su, J.H.1    Anderson, A.J.2    Cummings, B.J.3    Cotman, C.W.4
  • 41
    • 0032702875 scopus 로고    scopus 로고
    • Neurotoxic and synaptic effects of okadaic acid, an inhibitor of protein phosphatases
    • Tapia R., Pena F., Árias C. Neurotoxic and synaptic effects of okadaic acid, an inhibitor of protein phosphatases. Neurochem. Res. 24:1999;1423-1430
    • (1999) Neurochem. Res. , vol.24 , pp. 1423-1430
    • Tapia, R.1    Pena, F.2    Árias, C.3
  • 42
    • 0028963501 scopus 로고
    • Aluminium detected in senile plaques and neurofibrillary tangles is contained in lipofuscin granules with silicon, probably as aluminosilicate
    • Tokutake S., Nagase H., Morisaki S., Oyanagi S. Aluminium detected in senile plaques and neurofibrillary tangles is contained in lipofuscin granules with silicon, probably as aluminosilicate. Neurosci. Lett. 185:1995;99-102
    • (1995) Neurosci. Lett. , vol.185 , pp. 99-102
    • Tokutake, S.1    Nagase, H.2    Morisaki, S.3    Oyanagi, S.4
  • 43
    • 0029852587 scopus 로고    scopus 로고
    • In situ labeling of dying cortical neurons in normal aging and in Alzheimer's disease: Correlations with senile plaques and disease progression
    • Troncoso J.C., Sukhov R.R., Kawas C.H., Koliatsos V.E. In situ labeling of dying cortical neurons in normal aging and in Alzheimer's disease: correlations with senile plaques and disease progression. J. Neuropathol. Exp. Neurol. 55:1996;1134-1142
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , pp. 1134-1142
    • Troncoso, J.C.1    Sukhov, R.R.2    Kawas, C.H.3    Koliatsos, V.E.4
  • 44
    • 0034805931 scopus 로고    scopus 로고
    • Deranged expression of molecular chaperones in brains of patients with Alzheimer's disease
    • Yoo B.C., Kim S.H., Cairns N., Fountoulakis M., Lubec G. Deranged expression of molecular chaperones in brains of patients with Alzheimer's disease. Biochem. Biophys. Res. Commun. 280:2001;249-258
    • (2001) Biochem. Biophys. Res. Commun. , vol.280 , pp. 249-258
    • Yoo, B.C.1    Kim, S.H.2    Cairns, N.3    Fountoulakis, M.4    Lubec, G.5
  • 45
    • 0032585829 scopus 로고    scopus 로고
    • Heat-shock protein 70 levels in brain of patients with Down syndrome and Alzheimer's disease
    • Yoo B.C., Seidl R., Cairns N., Lubec G. Heat-shock protein 70 levels in brain of patients with Down syndrome and Alzheimer's disease. J. Neural Transm., Suppl. 57:1999;315-322
    • (1999) J. Neural Transm., Suppl. , vol.57 , pp. 315-322
    • Yoo, B.C.1    Seidl, R.2    Cairns, N.3    Lubec, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.