메뉴 건너뛰기




Volumn 24, Issue 3, 1999, Pages 427-435

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

Author keywords

Alzheimer's disease; Amyloid; Creatine kinase; Free radicals; Protein oxidation; Vitamin E

Indexed keywords

ALPHA TOCOPHEROL; AMYLOID BETA PROTEIN; CREATINE KINASE; FREE RADICAL;

EID: 0032936688     PISSN: 03643190     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1020997903147     Document Type: Article
Times cited : (109)

References (56)
  • 1
    • 0025911018 scopus 로고
    • Advances in Alzheimer's disease
    • Katzman, R. and Saitoh, T. 1991. Advances in Alzheimer's disease. FASEB J. 4:278-286.
    • (1991) FASEB J , vol.4 , pp. 278-286
    • Katzman, R.1    Saitoh, T.2
  • 2
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • Selkoe, D. J. 1991 The molecular pathology of Alzheimer's disease. Neuron 6:487-498.
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.J.1
  • 3
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebravascular amyloid protein
    • Glenner, G. G., and Wong, C. W. 1984. Alzheimer's disease: Initial report of the purification and characterization of a novel cerebravascular amyloid protein. Biochem. Biophys. Res. Commun. 120:885-890.
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 4
    • 0029784838 scopus 로고    scopus 로고
    • Amyloidß-protein and genetics of Alzheimer's disease
    • Selkoe, D. J. 1996 Amyloidß-protein and genetics of Alzheimer's disease. J. Biol. Chem. 271:18295-18298.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18295-18298
    • Selkoe, D.J.1
  • 5
  • 7
    • 0028908516 scopus 로고
    • Direct evidence of oxidative injury produced by the Alzheimer's amyloid beta-peptide (1-40) in cultured hippocampal neurons
    • Harris, M., Hensley, K., Butterfield, D. A., Leedle, R. A., and Carney, J. M. 1995. Direct evidence of oxidative injury produced by the Alzheimer's amyloid beta-peptide (1-40) in cultured hippocampal neurons. Exp. Neurol. 131:193-202.
    • (1995) Exp. Neurol. , vol.131 , pp. 193-202
    • Harris, M.1    Hensley, K.2    Butterfield, D.A.3    Leedle, R.A.4    Carney, J.M.5
  • 8
    • 0030612106 scopus 로고    scopus 로고
    • Disruption of brain cell ion homeostasis in Alzheimer's disease by oxyradicals, and signaling pathways that protect therefrom
    • Mattson, M. P., Mark, R. J., Furukawa, K., and Bruce, A. J. 1997. Disruption of brain cell ion homeostasis in Alzheimer's disease by oxyradicals, and signaling pathways that protect therefrom. Chem Res. Toxicol. 10:507-517.
    • (1997) Chem Res. Toxicol. , vol.10 , pp. 507-517
    • Mattson, M.P.1    Mark, R.J.2    Furukawa, K.3    Bruce, A.J.4
  • 9
    • 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., and Carney, J. M. 1994. β-Amyloid peptide free radical fragments initiate synaptosomal lipoperoxidation in a sequence-specific fashion: implications to Alzheimer's disease. Biochem. Biophys. Res. Commun. 200:710-715.
    • (1994) Biochem. Biophys. Res. Commun. , vol.200 , pp. 710-715
    • Butterfield, D.A.1    Hensley, K.2    Harris, M.3    Mattson, M.4    Carney, J.M.5
  • 10
    • 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. and Butterfield, D. A. 1998. Vitamin E protects against Alzheimer's amyloid peptide (25-35)-induced changes in neocortical synaptosomal membrane lipid structure and composition. Brain Res. 786:270-273.
    • (1998) Brain Res. , vol.786 , pp. 270-273
    • Koppal, T.1    Subramaniam, R.2    Drake, J.3    Prasad, M.R.4    Butterfield, D.A.5
  • 11
    • 0031962324 scopus 로고    scopus 로고
    • Bcl-2 protects isolated plasma and mitochondrial membranes against lipid peroxidation induced by hydrogen peroxide and amyloid beta-peptide
    • Bruce-Keller, A. J., Begley, J. G., Fu, W., Butterfield, D. A., Bredesen, D. E., Hutchins, J. B., Hensley, K., and Mattson, M. P. 1998. Bcl-2 protects isolated plasma and mitochondrial membranes against lipid peroxidation induced by hydrogen peroxide and amyloid beta-peptide. J. Neurochem. 70:31-39.
    • (1998) J. Neurochem. , vol.70 , pp. 31-39
    • Bruce-Keller, A.J.1    Begley, J.G.2    Fu, W.3    Butterfield, D.A.4    Bredesen, D.E.5    Hutchins, J.B.6    Hensley, K.7    Mattson, M.P.8
  • 12
    • 0031741578 scopus 로고    scopus 로고
    • The free radical antioxidant vitamin e protects cortical synaptosomal membranes from amyloid beta-peptide (25-35) toxicity but not from hydroxynonenal toxicity: Relevance to the free radical hypothesis of Alzheimer's disease
    • Subramaniam, R., Koppal, T., Green, M., Yatin, S., Jordan, B., Drake, J., and Butterfield, D. A. 1998. The free radical antioxidant vitamin E protects cortical synaptosomal membranes from amyloid beta-peptide (25-35) toxicity but not from hydroxynonenal toxicity: Relevance to the free radical hypothesis of Alzheimer's disease. Neurochem. Res. 23:1403-1410.
    • (1998) Neurochem. Res. , vol.23 , pp. 1403-1410
    • Subramaniam, R.1    Koppal, T.2    Green, M.3    Yatin, S.4    Jordan, B.5    Drake, J.6    Butterfield, D.A.7
  • 13
    • 0026316233 scopus 로고
    • The Alzheimer amyloid precursor is associated with the detergent-insoluble cytoskeleton
    • Refelo, L. M., Wittenberg, I., Friedrich, V. L. Jr., and Robakis, N. K. 1991. The Alzheimer amyloid precursor is associated with the detergent-insoluble cytoskeleton. J. Neurosci. 11:3888-3897.
    • (1991) J. Neurosci. , vol.11 , pp. 3888-3897
    • Refelo, L.M.1    Wittenberg, I.2    Friedrich V.L., Jr.3    Robakis, N.K.4
  • 14
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid β-protein: Reversal by Tachykinin neuropeptides
    • Yankner, B. A., Duffy, L. K., and Kirschnier, D. A. 1990. Neurotrophic and neurotoxic effects of amyloid β-protein: Reversal by Tachykinin neuropeptides. Science 250:279-282.
    • (1990) Science , vol.250 , pp. 279-282
    • Yankner, B.A.1    Duffy, L.K.2    Kirschnier, D.A.3
  • 15
  • 16
    • 0030928406 scopus 로고    scopus 로고
    • β-Amyloid-associated free radical oxidative stress and neurotoxicity: Implications for Alzheimer's disease
    • Butterfield, D. A. 1997. β-amyloid-associated free radical oxidative stress and neurotoxicity: Implications for Alzheimer's disease. Chem. Res. Toxicol. 10:495-506.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 495-506
    • Butterfield, D.A.1
  • 17
    • 0025992927 scopus 로고
    • Action of amyloid beta-protein on protein kinase C activity
    • Chauhan, A., Chauhan, V. P., Brockerhoff, H., and Wisniewski, H. M. 1991. Action of amyloid beta-protein on protein kinase C activity. Life Sci. 49:1555-1562.
    • (1991) Life Sci. , vol.49 , pp. 1555-1562
    • Chauhan, A.1    Chauhan, V.P.2    Brockerhoff, H.3    Wisniewski, H.M.4
  • 19
  • 20
    • 0028148893 scopus 로고
    • Effects of Alzheimer's disease-related beta amyloid protein fragments on enzyme metabolizing, phosphoinositides in brain
    • Wallace, M. A. 1994. Effects of Alzheimer's disease-related beta amyloid protein fragments on enzyme metabolizing, phosphoinositides in brain. Biochim. Biophys. Acta 1227:183-187.
    • (1994) Biochim. Biophys. Acta , vol.1227 , pp. 183-187
    • Wallace, M.A.1
  • 21
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid βprotein toxicity
    • Behl, C., Davis, J. B., Lesley, R., and Schubert, D. 1994. Hydrogen peroxide mediates amyloid βprotein toxicity. Cell 77:817-827.
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 23
    • 0021891892 scopus 로고
    • The creatine-creatine phosphate energy shuttle
    • Bessman, S. P. and Carpenter, C. L. 1985. The creatine-creatine phosphate energy shuttle. Annu. Rev. Biochem. 54:831-862.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 831-862
    • Bessman, S.P.1    Carpenter, C.L.2
  • 24
    • 0024201304 scopus 로고
    • Inactivation of creatine phosphokinase by superoxide during reperfusion injury
    • Simic, K. A., Word, J. F., and Von Sonntag, C. (eds.) Plenum Press New York
    • McCord, J. M. and Russell, W. J. 1988. Inactivation of creatine phosphokinase by superoxide during reperfusion injury. Pages 869-873, in Simic, K. A., Word, J. F., and Von Sonntag, C. (eds.) Oxygen Radicals in Biology and Medicine, Plenum Press New York.
    • (1988) Oxygen Radicals in Biology and Medicine , pp. 869-873
    • McCord, J.M.1    Russell, W.J.2
  • 25
    • 0026436761 scopus 로고
    • Inactivation of rabbit muscle creatine kinase by hydrogen peroxide
    • Suzuki, Y. J., Edmondson, J. D. and Ford, G. D. 1992. Inactivation of rabbit muscle creatine kinase by hydrogen peroxide. Free Radic. Res. Commun. 16:131-136.
    • (1992) Free Radic. Res. Commun. , vol.16 , pp. 131-136
    • Suzuki, Y.J.1    Edmondson, J.D.2    Ford, G.D.3
  • 27
    • 0028129137 scopus 로고
    • Evidence of an oxidative challenge in the Alzheimer's brain
    • Balazs, L. and Leon, M. 1994. Evidence of an oxidative challenge in the Alzheimer's brain. Neurochem. Res. 19:1131-1137.
    • (1994) Neurochem. Res. , vol.19 , pp. 1131-1137
    • Balazs, L.1    Leon, M.2
  • 28
    • 4243493901 scopus 로고
    • Increased lipid peroxidation and antioxidant enzyme activity in the brain in Alzheimer's disease
    • Markesbery, W. R., Lovell, M. A., and Ehmann, W. D. 1994. Increased lipid peroxidation and antioxidant enzyme activity in the brain in Alzheimer's disease. Neurobiol. Aging. 15:S139-S140.
    • (1994) Neurobiol. Aging , vol.15
    • Markesbery, W.R.1    Lovell, M.A.2    Ehmann, W.D.3
  • 29
    • 0030915855 scopus 로고    scopus 로고
    • Oxidative stress hypothesis in Alzheimer's disease
    • Markesbery, W. R. 1997. Oxidative stress hypothesis in Alzheimer's disease. Free Radic. Biol. Med. 23:134-147.
    • (1997) Free Radic. Biol. Med. , vol.23 , pp. 134-147
    • Markesbery, W.R.1
  • 30
    • 0029073455 scopus 로고
    • Elevated thiobarbituric acid-reactive substances and antioxidant activity in the brain in Alzheimer's disease
    • Lovell, M. A., Ehmann, W. D., Buttler, S. M., and Markesbery, W. R. 1995. Elevated thiobarbituric acid-reactive substances and antioxidant activity in the brain in Alzheimer's disease. Neurology 45:1594-1601.
    • (1995) Neurology , vol.45 , pp. 1594-1601
    • Lovell, M.A.1    Ehmann, W.D.2    Buttler, S.M.3    Markesbery, W.R.4
  • 31
    • 0030714092 scopus 로고    scopus 로고
    • Elevated 4-hydroxynonenal in ventricular fluid in Alzheimer's disease
    • Lovell, M. A., Ehmann, W. D., Mattson, M. P., and Markesbery, W. R. 1997. Elevated 4-hydroxynonenal in ventricular fluid in Alzheimer's disease. Neurobiol. Aging 18:457-461.
    • (1997) Neurobiol. Aging , vol.18 , pp. 457-461
    • Lovell, M.A.1    Ehmann, W.D.2    Mattson, M.P.3    Markesbery, W.R.4
  • 32
    • 0030746621 scopus 로고    scopus 로고
    • The lipid peroxidation product, 4-hydroxy-2-trans-nonenal, alters conformation of cortical synaptosomal membrane products
    • Subramaniam, R., Roediger, F., Jordan, B., Mattson, M. P., Keller, J. N., Waeg, G., and Butterfield, D. A. 1997. The lipid peroxidation product, 4-hydroxy-2-trans-nonenal, alters conformation of cortical synaptosomal membrane products. J. Neurochem. 69: 1161-1169.
    • (1997) J. Neurochem. , vol.69 , pp. 1161-1169
    • Subramaniam, R.1    Roediger, F.2    Jordan, B.3    Mattson, M.P.4    Keller, J.N.5    Waeg, G.6    Butterfield, D.A.7
  • 33
    • 0029866991 scopus 로고    scopus 로고
    • β-Amyloid toxicity in organotypic hippocampal cultures: Protection by EUK-8, a synthetic catalytic free radical scavenger
    • Bruce, A. J., Malfroy, B., and Baudry, M. 1996. β-Amyloid toxicity in organotypic hippocampal cultures: protection by EUK-8, a synthetic catalytic free radical scavenger. Proc. Natl. Acad. Sci. USA 93:2312-2316.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2312-2316
    • Bruce, A.J.1    Malfroy, B.2    Baudry, M.3
  • 37
    • 0027988579 scopus 로고
    • Inhibitors of free radical formation fail to attenuate direct β-amyloid 25-35 peptide mediated neurotoxicity in rat hippocampal cultures
    • Lockhart, B. P., Benicourt, C., Junien, J. L., and Privat, A. 1994. Inhibitors of free radical formation fail to attenuate direct β-amyloid 25-35 peptide mediated neurotoxicity in rat hippocampal cultures. J. Neurosci. Res. 39:494-505.
    • (1994) J. Neurosci. Res. , vol.39 , pp. 494-505
    • Lockhart, B.P.1    Benicourt, C.2    Junien, J.L.3    Privat, A.4
  • 38
    • 0030924506 scopus 로고    scopus 로고
    • β-Amyloid neurotoxicity in vitro: Evidence of oxidative stress but not protection by antioxidants
    • Pike, C. J., Ramezan-Arab, N., Cotman, C. W. 1997. β-amyloid neurotoxicity in vitro: Evidence of oxidative stress but not protection by antioxidants. J. Neurochem. 69:1601-1611.
    • (1997) J. Neurochem. , vol.69 , pp. 1601-1611
    • Pike, C.J.1    Ramezan-Arab, N.2    Cotman, C.W.3
  • 39
    • 0028291974 scopus 로고
    • Carbonyl assays for determination of oxidatively modified proteins
    • Levine, R. L., Williams, J. A., Stadtman, E. R., and Shacter, E. 1994. Carbonyl assays for determination of oxidatively modified proteins. Methods Enzymol. 233:346-357.
    • (1994) Methods Enzymol. , vol.233 , pp. 346-357
    • Levine, R.L.1    Williams, J.A.2    Stadtman, E.R.3    Shacter, E.4
  • 40
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. 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.1
  • 41
    • 0022764985 scopus 로고
    • Antibody probing on Western blots have been stained with India ink
    • Glenney, J. R. 1986. Antibody probing on Western blots have been stained with India ink. Anal. Biochem. 156:315-318.
    • (1986) Anal. Biochem. , vol.156 , pp. 315-318
    • Glenney, J.R.1
  • 42
    • 0026554428 scopus 로고
    • Evaluation of the probe 2′,7′-dichlorofluorescin as an indicator of reactive oxygen species formation and oxidative stress
    • LeBel, C. P., Ischiropoulus, H. and Bondy, S. C. 1992. Evaluation of the probe 2′,7′-dichlorofluorescin as an indicator of reactive oxygen species formation and oxidative stress. Chem. Res. Toxicol. 5:227-231.
    • (1992) Chem. Res. Toxicol. , vol.5 , pp. 227-231
    • LeBel, C.P.1    Ischiropoulus, H.2    Bondy, S.C.3
  • 45
    • 0028981219 scopus 로고
    • Structure-activity analysis of β-amyloid peptides: Contributions of the Aβ(25-35) region to aggregation and neurotoxicity
    • Pike, C. J., Walencewicz-Wasserman, A. J., Kosmoski, J., Cribbs, D. H., Glabe, C. G., and Cotman, C. W. 1995. Structure-activity analysis of β-amyloid peptides: contributions of the Aβ(25-35) region to aggregation and neurotoxicity. J. Neurochem. 64:253-265.
    • (1995) J. Neurochem. , vol.64 , pp. 253-265
    • Pike, C.J.1    Walencewicz-Wasserman, A.J.2    Kosmoski, J.3    Cribbs, D.H.4    Glabe, C.G.5    Cotman, C.W.6
  • 48
    • 0025309904 scopus 로고
    • Oxidative damage to brain proteins, loss of glutamine synthetase activity, and production of free radicals during ischemia/reperfusion-induced injury to gerbil brain
    • Oliver C. N., Starke-Reed P. E., Stadtman E. R., Liu G. J., Carney J. M., Floyd R. A. 1990. Oxidative damage to brain proteins, loss of glutamine synthetase activity, and production of free radicals during ischemia/reperfusion-induced injury to gerbil brain. Proc. Natl. Acad. Sci. USA 87:5144-5147.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5144-5147
    • Oliver, C.N.1    Starke-Reed, P.E.2    Stadtman, E.R.3    Liu, G.J.4    Carney, J.M.5    Floyd, R.A.6
  • 49
    • 77956832045 scopus 로고    scopus 로고
    • Protein oxidation process in aging brain
    • Mattson, M. P., and Geddes, J. W. (eds.), JAI Press, Greenwich, CT
    • Butterfield, D. A. and Stadtman, E. R. 1997. Protein oxidation process in aging brain. Pages 161-191, in Mattson, M. P., and Geddes, J. W. (eds.), The Aging Brain, JAI Press, Greenwich, CT.
    • (1997) The Aging Brain , pp. 161-191
    • Butterfield, D.A.1    Stadtman, E.R.2
  • 50
    • 0031010333 scopus 로고    scopus 로고
    • Reactive oxygen-mediated protein oxidation in aging and disease
    • Stadtman E. R. and Berlett B. S. 1997. Reactive oxygen-mediated protein oxidation in aging and disease. Chem. Res. Toxicol. 10: 485-494.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 485-494
    • Stadtman, E.R.1    Berlett, B.S.2
  • 51
    • 0028143826 scopus 로고
    • Differential susceptibility of plasma proteins to oxidative modifications: Examination by Western blot immunoassay
    • Shacter, E., Williams, J. A., Lim, M., and Levine, R. L. 1994. Differential susceptibility of plasma proteins to oxidative modifications: examination by Western blot immunoassay. Free Rad. Biol. Med. 17:429-437.
    • (1994) Free Rad. Biol. Med. , vol.17 , pp. 429-437
    • Shacter, E.1    Williams, J.A.2    Lim, M.3    Levine, R.L.4
  • 53
    • 0029863551 scopus 로고    scopus 로고
    • Inhibition of amyloid beta protein aggregation and neurotoxicity by rifampicin. Its possible function as a hydroxy radical scavenger
    • Tomiyama, T., Shaji, A., Kataoka, K., Suwa, Y., Asano, S., Kaneko, H., and Endo, N. 1996. Inhibition of amyloid beta protein aggregation and neurotoxicity by rifampicin. Its possible function as a hydroxy radical scavenger. J. Biol. Chem. 271:6839-6844.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6839-6844
    • Tomiyama, T.1    Shaji, A.2    Kataoka, K.3    Suwa, Y.4    Asano, S.5    Kaneko, H.6    Endo, N.7
  • 54
    • 0017353168 scopus 로고
    • Creatine kinase: Stability, inactivation and reactivation
    • Morin, L. G. 1977. Creatine kinase: Stability, inactivation and reactivation. Clin Chem. 23:646-652.
    • (1977) Clin Chem. , vol.23 , pp. 646-652
    • Morin, L.G.1
  • 55
    • 0028326937 scopus 로고
    • Alterations of cerebral metabolism in probable Alzheimer's disease: A preliminary study
    • Pettegrew, J. M., Panchalingam, K., Klunk, W. E., McClure, R. J., and Muenz, L. R. 1994. Alterations of cerebral metabolism in probable Alzheimer's disease: A preliminary study. Neurobiol. Aging 15:117-132.
    • (1994) Neurobiol. Aging , vol.15 , pp. 117-132
    • Pettegrew, J.M.1    Panchalingam, K.2    Klunk, W.E.3    McClure, R.J.4    Muenz, L.R.5
  • 56
    • 0026979972 scopus 로고
    • The action of acute alcoholic intoxication on the antioxidant system and creatin kinase activity in the brain of rat embryos
    • Burmistrov, S. O., Mashek, O. P. and Kotin, A. M. 1992. The action of acute alcoholic intoxication on the antioxidant system and creatin kinase activity in the brain of rat embryos. Eksp. Klin. Farmakol. 55:54-56.
    • (1992) Eksp. Klin. Farmakol. , vol.55 , pp. 54-56
    • Burmistrov, S.O.1    Mashek, O.P.2    Kotin, A.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.