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Volumn 850, Issue 1-2, 1999, Pages 179-188

Regulation of GTPase and adenylate cyclase activity by amyloid β-peptide and its fragments in rat brain tissue

Author keywords

Adenylate cyclase; Alzheimer's disease; Amyloid peptide; GTPase

Indexed keywords

ACETYLCYSTEINE; ADENYLATE CYCLASE; AMYLOID BETA PROTEIN; GLUTATHIONE; GUANOSINE TRIPHOSPHATASE; PEPTIDE FRAGMENT;

EID: 0032758498     PISSN: 00068993     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-8993(99)02142-3     Document Type: Article
Times cited : (17)

References (53)
  • 1
    • 0025613886 scopus 로고
    • Immunochemical and immunohistochemical localization of the G-protein Gi1 in rat central nervous tissues
    • Asano T., Shinohara H., Morshita R., Kato K. Immunochemical and immunohistochemical localization of the G-protein Gi1 in rat central nervous tissues. J. Biochem. 108:1990;988-994.
    • (1990) J. Biochem. , vol.108 , pp. 988-994
    • Asano, T.1    Shinohara, H.2    Morshita, R.3    Kato, K.4
  • 3
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid β protein toxicity
    • Behl C., Davis J.B., Lesley R., Schubert D. Hydrogen peroxide mediates amyloid β protein toxicity. Cell. 77:1994;817-827.
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 5
    • 0015465805 scopus 로고
    • Saturation assay for cyclic AMP using endogenous binding protein
    • Brown B.L., Ekins R.P., Albano J.D. Saturation assay for cyclic AMP using endogenous binding protein. Adv. Cyclic Nucleotide Res. 2:1972;25-40.
    • (1972) Adv. Cyclic Nucleotide Res. , vol.2 , pp. 25-40
    • Brown, B.L.1    Ekins, R.P.2    Albano, J.D.3
  • 7
    • 0028178837 scopus 로고
    • β-amyloid peptide free radical fragments initiate synaptosomal lipoperoxidation in a sequence-specific fashion: Implications to Alzheimer's disease
    • Butterfield D.A., Hensley K., Harris M., Mattson M.P., Carney J.M. β-amyloid peptide free radical fragments initiate synaptosomal lipoperoxidation in a sequence-specific fashion: implications to Alzheimer's disease. Biochem. Biophys. Res. Commun. 200:1994;710-715.
    • (1994) Biochem. Biophys. Res. Commun. , vol.200 , pp. 710-715
    • Butterfield, D.A.1    Hensley, K.2    Harris, M.3    Mattson, M.P.4    Carney, J.M.5
  • 8
    • 0030928406 scopus 로고    scopus 로고
    • β-Amyloid-generated free radical oxidative stress and neurotoxicity: Implications for Alzheimer's disease
    • Butterfield D.A. β-Amyloid-generated free radical oxidative stress and neurotoxicity: implications for Alzheimer's disease. Chem. Res. Toxicol. 10:1997;518-526.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 518-526
    • Butterfield, D.A.1
  • 9
    • 0017199526 scopus 로고
    • Catecholamine stimulated GTPase activity in turkey erythrocyte membranes
    • Cassel D., Selinger Z. Catecholamine stimulated GTPase activity in turkey erythrocyte membranes. Biochim. Biophys. Acta. 452:1976;538-551.
    • (1976) Biochim. Biophys. Acta , vol.452 , pp. 538-551
    • Cassel, D.1    Selinger, Z.2
  • 10
    • 0033515564 scopus 로고    scopus 로고
    • Amyloid β peptides do not form peptide-derived free radicals spontaneously, but can enhance metal-catalysed oxidation of hydroxylamines to nitroxides
    • Dikalov S.I., Vitek M.P., Maples K.R., Mason R.P. Amyloid β peptides do not form peptide-derived free radicals spontaneously, but can enhance metal-catalysed oxidation of hydroxylamines to nitroxides. J. Biol. Chem. 274:1999;9392-9399.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9392-9399
    • Dikalov, S.I.1    Vitek, M.P.2    Maples, K.R.3    Mason, R.P.4
  • 11
    • 0028919316 scopus 로고
    • Attenuation of muscarinic receptor-G-protein interaction in Alzheimer disease
    • Ferrari-DiLeo G., Mash D.C., Flynn D.D. Attenuation of muscarinic receptor-G-protein interaction in Alzheimer disease. Mol. Chem. Neuropathol. 24:1995;69-91.
    • (1995) Mol. Chem. Neuropathol. , vol.24 , pp. 69-91
    • Ferrari-Dileo, G.1    Mash, D.C.2    Flynn, D.D.3
  • 12
    • 0028037404 scopus 로고
    • Amyloid β protein-induced irreversible current in rat cortical neurones
    • Furukawa K., Abe Y., Akaike N. Amyloid β protein-induced irreversible current in rat cortical neurones. NeuroReport. 5:1994;2016-2018.
    • (1994) NeuroReport , vol.5 , pp. 2016-2018
    • Furukawa, K.1    Abe, Y.2    Akaike, N.3
  • 13
    • 44949277996 scopus 로고
    • A PFG NMR experiment for accurate diffusion and flow studies in the presence of Eddy currents
    • Gibbs S.J., Johnson C.S. Jr. A PFG NMR experiment for accurate diffusion and flow studies in the presence of Eddy currents. J. Magn. Reson. 93:1991;395-402.
    • (1991) J. Magn. Reson. , vol.93 , pp. 395-402
    • Gibbs, S.J.1    Johnson C.S., Jr.2
  • 14
    • 0023201169 scopus 로고
    • Stimulation and inhibition of cAMP accumulation by glucagon in canine hepatocytes
    • Grady T., Fickova M., Tager H.S., Trivedi D., Hruby J. Stimulation and inhibition of cAMP accumulation by glucagon in canine hepatocytes. J. Biol. Chem. 262:1987;15514-15520.
    • (1987) J. Biol. Chem. , vol.262 , pp. 15514-15520
    • Grady, T.1    Fickova, M.2    Tager, H.S.3    Trivedi, D.4    Hruby, J.5
  • 15
    • 0031724393 scopus 로고    scopus 로고
    • A novel, synergistic interaction between 17-beta-estradiol and glutathione in the protection of neurons against beta-amyloid (25-35)-induced toxicity in vitro
    • Gridely K.E., Green P.S., Simpkins J.W. A novel, synergistic interaction between 17-beta-estradiol and glutathione in the protection of neurons against beta-amyloid (25-35)-induced toxicity in vitro. Mol. Pharmacol. 54:1998;874-880.
    • (1998) Mol. Pharmacol. , vol.54 , pp. 874-880
    • Gridely, K.E.1    Green, P.S.2    Simpkins, J.W.3
  • 16
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimers's disease and Scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • Harper J.D., Lansbury P.T. Models of amyloid seeding in Alzheimers's disease and Scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu. Rev. Biochem. 66:1997;385-407.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury, P.T.2
  • 18
    • 0023918551 scopus 로고
    • Mastoparan, a peptide toxin from wasp venom, mimics receptors by activating GTP-binding regulatory proteins (G proteins)
    • Higashijima T., Uzu S., Nakajima T., Ross E.M. Mastoparan, a peptide toxin from wasp venom, mimics receptors by activating GTP-binding regulatory proteins (G proteins). J. Biol. Chem. 263:1988;6491-6494.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6491-6494
    • Higashijima, T.1    Uzu, S.2    Nakajima, T.3    Ross, E.M.4
  • 19
    • 0027244664 scopus 로고
    • Altered beta-adrenergic receptor-stimulated cAMP formation in cultured skin fibroblasts from Alzheimer donors
    • Huang H.M., Gibson G.E. Altered beta-adrenergic receptor-stimulated cAMP formation in cultured skin fibroblasts from Alzheimer donors. J. Biol. Chem. 268:1993;14616-14621.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14616-14621
    • Huang, H.M.1    Gibson, G.E.2
  • 23
    • 0032498829 scopus 로고    scopus 로고
    • Vitamin E protects against Alzheimer's amyloid peptide (25-35)-induced changes in neocortical synaptosomal membrane lipid structure and composition
    • Koppal T., Subramaniam R., Drake J., Prasad M.R., Dhillon H., Butterfield D.A. Vitamin E protects against Alzheimer's amyloid peptide (25-35)-induced changes in neocortical synaptosomal membrane lipid structure and composition. Brain Res. 786:1998;270-273.
    • (1998) Brain Res. , vol.786 , pp. 270-273
    • Koppal, T.1    Subramaniam, R.2    Drake, J.3    Prasad, M.R.4    Dhillon, H.5    Butterfield, D.A.6
  • 24
    • 0026762561 scopus 로고
    • Design of chimeric peptide ligands to galanin receptors and substance P receptors
    • Langel Ü., Land T., Bartfai T. Design of chimeric peptide ligands to galanin receptors and substance P receptors. Int. J. Pept. Protein Res. 39:1992;516-522.
    • (1992) Int. J. Pept. Protein Res. , vol.39 , pp. 516-522
    • Langel, Ü.1    Land, T.2    Bartfai, T.3
  • 25
    • 33947473108 scopus 로고
    • The mutual diffusion of light and heavy water
    • Longsworth L.G. The mutual diffusion of light and heavy water. J. Phys. Chem. 64:1960;1914-1917.
    • (1960) J. Phys. Chem. , vol.64 , pp. 1914-1917
    • Longsworth, L.G.1
  • 27
    • 0029441611 scopus 로고
    • In vitro analysis of G-protein functions
    • Ma H., Weiss C.A. In vitro analysis of G-protein functions. Methods Cell Biol. 49:1951;471-485.
    • (1951) Methods Cell Biol. , vol.49 , pp. 471-485
    • Ma, H.1    Weiss, C.A.2
  • 28
    • 0023741142 scopus 로고
    • Thrombin exerts a dual effect on stimulated adenylate cyclase in hamster fibroblasts, an inhibition via a GTP-binding protein and potentiation via activation of protein kinase C
    • Magnaldo I., Pouyssegur J., Paris S. Thrombin exerts a dual effect on stimulated adenylate cyclase in hamster fibroblasts, an inhibition via a GTP-binding protein and potentiation via activation of protein kinase C. Biochem. J. 253:1988;711-719.
    • (1988) Biochem. J. , vol.253 , pp. 711-719
    • Magnaldo, I.1    Pouyssegur, J.2    Paris, S.3
  • 29
    • 0031020993 scopus 로고    scopus 로고
    • Amyloid β-peptide impairs glucose transport in hippocampal and cortical neurons: Involvement of membrane lipid peroxidation
    • Mark R.J., Pang Z., Geddes J.W., Uchida K., Mattson M.P. Amyloid β-peptide impairs glucose transport in hippocampal and cortical neurons: involvement of membrane lipid peroxidation. J. Neurosci. 17:1997;1046-1054.
    • (1997) J. Neurosci. , vol.17 , pp. 1046-1054
    • Mark, R.J.1    Pang, Z.2    Geddes, J.W.3    Uchida, K.4    Mattson, M.P.5
  • 31
    • 0030609125 scopus 로고    scopus 로고
    • Aβ25-35 induced rapid lysis of red blood cells: Contrast with Aβ1-42 and examination of underlying mechanisms
    • Mattson M.P., Begley J.G., Mark R.J., Furukawa K. Aβ25-35 induced rapid lysis of red blood cells: contrast with Aβ1-42 and examination of underlying mechanisms. Brain Res. 771:1997;147-153.
    • (1997) Brain Res. , vol.771 , pp. 147-153
    • Mattson, M.P.1    Begley, J.G.2    Mark, R.J.3    Furukawa, K.4
  • 32
    • 0001770310 scopus 로고
    • Basic techniques to study G-protein function
    • in: G. Milligan (Ed.), Oxford University Press, Oxford
    • F.R. McKenzie, Basic techniques to study G-protein function, in: G. Milligan (Ed.), Signal Transduction. A Practical Approach, Oxford University Press, Oxford, 1992, pp. 31-56.
    • (1992) Signal Transduction. a Practical Approach , pp. 31-56
    • McKenzie, F.R.1
  • 33
    • 0025162326 scopus 로고
    • G protein activation: A receptor-independent mode of action for cationic amphiphilic neuropeptides and venom peptides
    • Mousli M., Bueb J.-L., Bronner C., Rouot B., Landry Y. G protein activation: a receptor-independent mode of action for cationic amphiphilic neuropeptides and venom peptides. Trends Pharmacol. Sci. 11:1990;358-362.
    • (1990) Trends Pharmacol. Sci. , vol.11 , pp. 358-362
    • Mousli, M.1    Bueb, J.-L.2    Bronner, C.3    Rouot, B.4    Landry, Y.5
  • 35
    • 0028935717 scopus 로고
    • Ligand-dependent G protein coupling function of amyloid transmembrane precursor
    • Okamoto T., Takeda S., Murayama Y., Ogata E., Nishimoto I. Ligand-dependent G protein coupling function of amyloid transmembrane precursor. J. Biol. Chem. 270:1995;4205-4208.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4205-4208
    • Okamoto, T.1    Takeda, S.2    Murayama, Y.3    Ogata, E.4    Nishimoto, I.5
  • 36
    • 0027279564 scopus 로고
    • Alterations in the activity of adenylate cyclase and high affinity GTPase in Alzheimer's disease
    • Ross B.M., McLaughlin M., Roberts M., Milligan G., McCulloch J., Knowler J.T. Alterations in the activity of adenylate cyclase and high affinity GTPase in Alzheimer's disease. Brain Res. 622:1993;35-42.
    • (1993) Brain Res. , vol.622 , pp. 35-42
    • Ross, B.M.1    McLaughlin, M.2    Roberts, M.3    Milligan, G.4    McCulloch, J.5    Knowler, J.T.6
  • 37
    • 0028224211 scopus 로고
    • Adenylyl cyclase activity in Alzheimer's disease brain: Stimulatory and inhibitory signal transduction pathways are differently affected
    • Schnecko A., Witte K., Bohl J., Ohm T., Lemmer B. Adenylyl cyclase activity in Alzheimer's disease brain: stimulatory and inhibitory signal transduction pathways are differently affected. Brain Res. 644:1994;291-296.
    • (1994) Brain Res. , vol.644 , pp. 291-296
    • Schnecko, A.1    Witte, K.2    Bohl, J.3    Ohm, T.4    Lemmer, B.5
  • 39
    • 0026738860 scopus 로고
    • Inhibitory and stimulatory effects of neuropeptide Y (17-36) on rat cardiac adenylate cyclase activity
    • Sheriff S., Balasubramaniam A. Inhibitory and stimulatory effects of neuropeptide Y (17-36) on rat cardiac adenylate cyclase activity. J. Biol. Chem. 267:1992;4680-4685.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4680-4685
    • Sheriff, S.1    Balasubramaniam, A.2
  • 40
    • 0028004187 scopus 로고
    • Effects of amphiphilic peptides mastoparan and adenoregulin on receptor binding, G-proteins, phosphoinositide breakdown, cyclic AMP generation, and calcium influx
    • Shin Y., Moni R.W., Lueders J.E., Daly J.W. Effects of amphiphilic peptides mastoparan and adenoregulin on receptor binding, G-proteins, phosphoinositide breakdown, cyclic AMP generation, and calcium influx. Cell. Mol. Neurobiol. 14:1994;133-157.
    • (1994) Cell. Mol. Neurobiol. , vol.14 , pp. 133-157
    • Shin, Y.1    Moni, R.W.2    Lueders, J.E.3    Daly, J.W.4
  • 42
    • 0031873102 scopus 로고    scopus 로고
    • β-Sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: Implications for Alzheimer's therapy
    • Soto C., Sigurdsson E.M., Morelli L., Kumar R.A., Castano E.M., Frangione B. β-Sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: Implications for Alzheimer's therapy. Nature Medicine. 4:1998;822-826.
    • (1998) Nature Medicine , vol.4 , pp. 822-826
    • Soto, C.1    Sigurdsson, E.M.2    Morelli, L.3    Kumar, R.A.4    Castano, E.M.5    Frangione, B.6
  • 43
    • 33646376290 scopus 로고
    • Spin diffusion measurements: Spin echoes in the presence of a time-dependent field gradient
    • Stejskal E.O., Tanner J.E. Spin diffusion measurements: spin echoes in the presence of a time-dependent field gradient. J. Chem. Phys. 42:1965;288-292.
    • (1965) J. Chem. Phys. , vol.42 , pp. 288-292
    • Stejskal, E.O.1    Tanner, J.E.2
  • 44
    • 0028982292 scopus 로고
    • Self-association of beta-amyloid peptide (1-40) in solution and binding to lipid membranes
    • Terzi E., Holzemann G., Seelig J. Self-association of beta-amyloid peptide (1-40) in solution and binding to lipid membranes. J. Mol. Biol. 252:1995;633-642.
    • (1995) J. Mol. Biol. , vol.252 , pp. 633-642
    • Terzi, E.1    Holzemann, G.2    Seelig, J.3
  • 48
    • 0027389045 scopus 로고
    • Reduced density of adenosine A1 receptors and preserved coupling of adenosine A1 receptors to G proteins in Alzheimer hippocampus: A quantitative autoradiographic study
    • Ulas J., Brunner L.C., Nguyen L., Cotman C.W. Reduced density of adenosine A1 receptors and preserved coupling of adenosine A1 receptors to G proteins in Alzheimer hippocampus: a quantitative autoradiographic study. Neuroscience. 52:1993;843-854.
    • (1993) Neuroscience , vol.52 , pp. 843-854
    • Ulas, J.1    Brunner, L.C.2    Nguyen, L.3    Cotman, C.W.4
  • 49
    • 0028928494 scopus 로고
    • Differential regulation of adenylate cyclase activity in rat ventral and dorsal hippocampus by rat galanin
    • Valkna A., Juréus A., Karelson E., Zilmer M., Bartfai T., Langel Ü. Differential regulation of adenylate cyclase activity in rat ventral and dorsal hippocampus by rat galanin. Neurosci. Lett. 187:1995;75-78.
    • (1995) Neurosci. Lett. , vol.187 , pp. 75-78
    • Valkna, A.1    Juréus, A.2    Karelson, E.3    Zilmer, M.4    Bartfai, T.5    Langel, Ü.6
  • 50
    • 16944365745 scopus 로고    scopus 로고
    • Enhanced production and oligomerization of the 42-residue amyloid β-protein by chinese hamster ovary cells stably expressing mutant presenilins
    • Xia W., Zhang J., Kholodenko D., Citron M., Podlisny M.B., Teplow D.B., Haas C., Seubert P., Koo E.H., Selkoe D.J. Enhanced production and oligomerization of the 42-residue amyloid β-protein by chinese hamster ovary cells stably expressing mutant presenilins. J. Biol. Chem. 272:1997;7977-7982.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7977-7982
    • Xia, W.1    Zhang, J.2    Kholodenko, D.3    Citron, M.4    Podlisny, M.B.5    Teplow, D.B.6    Haas, C.7    Seubert, P.8    Koo, E.H.9    Selkoe, D.J.10
  • 51
    • 0032936688 scopus 로고    scopus 로고
    • The antioxidant vitamin E modulates amyloid β-peptide induced creatine kinase activity inhibition and increased protein oxidation: Implications for the free radical hypothesis of Alzheimer's disease
    • Yatin S.M., Aksenov M., Butterfield D.A. The antioxidant vitamin E modulates amyloid β-peptide induced creatine kinase activity inhibition and increased protein oxidation: implications for the free radical hypothesis of Alzheimer's disease. Neurochem. Res. 24:1999;427-435.
    • (1999) Neurochem. Res. , vol.24 , pp. 427-435
    • Yatin, S.M.1    Aksenov, M.2    Butterfield, D.A.3
  • 52
    • 0033583252 scopus 로고    scopus 로고
    • Alzheimer's amyloid β-peptide associated free radicals increase rat embryonic neuronal polyamine uptake and ornithine decarboxylase activity: Protective effect of vitamin E
    • Yatin S.M., Yatin M., Aulick T., Ain K.B., Butterfield D.A. Alzheimer's amyloid β-peptide associated free radicals increase rat embryonic neuronal polyamine uptake and ornithine decarboxylase activity: protective effect of vitamin E. Neurosci. Lett. 263:1999;17-20.
    • (1999) Neurosci. Lett. , vol.263 , pp. 17-20
    • Yatin, S.M.1    Yatin, M.2    Aulick, T.3    Ain, K.B.4    Butterfield, D.A.5
  • 53


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