메뉴 건너뛰기




Volumn 21, Issue 1, 1998, Pages 25-30

Inhibition of α-ketoglutarate- and pyruvate dehydrogenase complexes in E. coli by a glutathione S-transferase containing a pathological length poly-Q domain: A possible role of energy deficit in neurological diseases associated with poly-Q expansions?

Author keywords

[No Author keywords available]

Indexed keywords

GLUTATHIONE TRANSFERASE; OXOGLUTARATE DEHYDROGENASE; PYRUVATE DEHYDROGENASE;

EID: 0032461376     PISSN: 01619152     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11357-998-0004-x     Document Type: Article
Times cited : (3)

References (30)
  • 2
    • 0029833062 scopus 로고    scopus 로고
    • Spinocerebellar ataxia type-1 and spinocerebellar muscular atrophy gene products interact with glyceraldehyde-phosphate dehydrogenase
    • Koshy B, Matilla T, Burright EN, Merry DE, Fischbeck KH, Orr HT and Zoghbi HY. Spinocerebellar ataxia type-1 and spinocerebellar muscular atrophy gene products interact with glyceraldehyde-phosphate dehydrogenase. Human Mol. Gen. 5: 1311-1318, 1996.
    • (1996) Human Mol. Gen. , vol.5 , pp. 1311-1318
    • Koshy, B.1    Matilla, T.2    Burright, E.N.3    Merry, D.E.4    Fischbeck, K.H.5    Orr, H.T.6    Zoghbi, H.Y.7
  • 6
    • 0030812593 scopus 로고    scopus 로고
    • Transglutaminase-catalyzed inactivation of glyceraldehyde 3-phosphate dehydrogenase and α-ketoglutarate dehydrogenase complex by poly-Q domains of pathological length
    • Cooper AJL, Sheu K-FR, Onodera O, Burke JR, Stritmatter WJ. Roses AD and Blass JP. Transglutaminase-catalyzed inactivation of glyceraldehyde 3-phosphate dehydrogenase and α-ketoglutarate dehydrogenase complex by poly-Q domains of pathological length. Proc. Natl. Acad. Sci. 94: 12604-12609, 1997.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 12604-12609
    • Cooper, A.J.L.1    Sheu, K.-F.R.2    Onodera, O.3    Burke, J.R.4    Stritmatter, W.J.5    Roses, A.D.6    Blass, J.P.7
  • 7
    • 0027507667 scopus 로고
    • Human genetic diseases due to codon reiteration: Relationship to an evolutionary mechanism
    • Green H. Human genetic diseases due to codon reiteration: Relationship to an evolutionary mechanism. Cell 74: 955-956, 1993.
    • (1993) Cell , vol.74 , pp. 955-956
    • Green, H.1
  • 8
    • 0030058208 scopus 로고    scopus 로고
    • Expanded polyglutamine in the Machado-Joseph disease protein induces cell death in vitro and in vivo
    • Ikeda H, Yamaguchi M, Sugai S, Aze Y, Narumia S and Kakizuka A. Expanded polyglutamine in the Machado-Joseph disease protein induces cell death in vitro and in vivo. Nature Gen. 13: 196-202, 1996.
    • (1996) Nature Gen. , vol.13 , pp. 196-202
    • Ikeda, H.1    Yamaguchi, M.2    Sugai, S.3    Aze, Y.4    Narumia, S.5    Kakizuka, A.6
  • 9
    • 0029856046 scopus 로고    scopus 로고
    • Peptides containing glutamine repeats as substrates for transglutaminase-catalyzed cross-linking: Relevance to diseases of the nervous system
    • Kahlem P, Terré C, Green H and Djian P. Peptides containing glutamine repeats as substrates for transglutaminase-catalyzed cross-linking: Relevance to diseases of the nervous system. Proc. Natl. Acad. Sci. U. S. A. 93: 14580-14585, 1996.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 14580-14585
    • Kahlem, P.1    Terré, C.2    Green, H.3    Djian, P.4
  • 10
    • 0030906890 scopus 로고    scopus 로고
    • Polyglutamine domains are substrates of tissue transglutaminase. Does transglutaminase play a role in expanded CAG/poly-Q repeat neurodegenerative diseases?
    • Cooper AJL, Sheu K-FR, Onodera O, Burke JR, Strittmatter WJ, Roses AD and Blass JP. Polyglutamine domains are substrates of tissue transglutaminase. Does transglutaminase play a role in expanded CAG/poly-Q repeat neurodegenerative diseases? J. Neurochem. 69: 431-434, 1997.
    • (1997) J. Neurochem. , vol.69 , pp. 431-434
    • Cooper, A.J.L.1    Sheu, K.-F.R.2    Onodera, O.3    Burke, J.R.4    Strittmatter, W.J.5    Roses, A.D.6    Blass, J.P.7
  • 11
    • 0029059477 scopus 로고
    • Incorporation of glutamine repeats makes protein oligomerize: Implications for neurodegerative diseases
    • Stott K, Blackburn JM, Butler PJG and Perutz M. Incorporation of glutamine repeats makes protein oligomerize: Implications for neurodegerative diseases. Proc. Natl. Acad. Sci. U. S. A. 92: 6509-6513, 1995.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 6509-6513
    • Stott, K.1    Blackburn, J.M.2    Butler, P.J.G.3    Perutz, M.4
  • 12
    • 0015498712 scopus 로고
    • Comparative studies of tissue transglutaminase and factor XIII
    • Chung SI. Comparative studies of tissue transglutaminase and factor XIII. Ann. N. Y. Acad. Sci. 202: 240-255, 1972.
    • (1972) Ann. N. Y. Acad. Sci. , vol.202 , pp. 240-255
    • Chung, S.I.1
  • 14
    • 0014010928 scopus 로고
    • Transglutaminase: Mechanistic features of the active site as determined by kinetic and inhibitor studies
    • Folk JE and Cole PW. Transglutaminase: Mechanistic features of the active site as determined by kinetic and inhibitor studies. Biochim. Biophys. Chim. Acta 122: 244-264, 1966.
    • (1966) Biochim. Biophys. Chim. Acta , vol.122 , pp. 244-264
    • Folk, J.E.1    Cole, P.W.2
  • 16
    • 0028300118 scopus 로고
    • A rapid and simple method for the purification of transglutaminase from Streptoverticullum mobaraense
    • Gerber U, Jucknischke U, Putzien S and Fuchsbauer H-L. A rapid and simple method for the purification of transglutaminase from Streptoverticullum mobaraense. Biochem. J. 299: 825-829, 1994.
    • (1994) Biochem. J. , vol.299 , pp. 825-829
    • Gerber, U.1    Jucknischke, U.2    Putzien, S.3    Fuchsbauer, H.-L.4
  • 17
    • 0029125913 scopus 로고
    • Involvement of transglutaminase in the formation of covalent cross-links in the cell wall of Candida albicans
    • Ruiz-Herrera J, Iranzo M, Elorza MV, Sentanddreu R and Mormeneo S. Involvement of transglutaminase in the formation of covalent cross-links in the cell wall of Candida albicans. Arch. Microbiol. 164: 186-193, 1995.
    • (1995) Arch. Microbiol. , vol.164 , pp. 186-193
    • Ruiz-Herrera, J.1    Iranzo, M.2    Elorza, M.V.3    Sentanddreu, R.4    Mormeneo, S.5
  • 18
    • 0023792365 scopus 로고
    • Energy metabolism in disorders of the nervous system
    • Paris
    • Blass JP, Sheu RK-F, and Cederbaum JM. Energy metabolism in disorders of the nervous system. Rev. Neurol. (Paris) 144: 543-563, 1988.
    • (1988) Rev. Neurol. , vol.144 , pp. 543-563
    • Blass, J.P.1    Sheu, R.K.-F.2    Cederbaum, J.M.3
  • 19
    • 0029125857 scopus 로고
    • Aging, energy metabolism, and oxidative stress in neurodegenerative diseases
    • Beal MF. Aging, energy metabolism, and oxidative stress in neurodegenerative diseases. Ann. Neurol. 38: 357-366, 1995.
    • (1995) Ann. Neurol. , vol.38 , pp. 357-366
    • Beal, M.F.1
  • 20
    • 0342498674 scopus 로고    scopus 로고
    • Energy/glucose metabolism in neurodegenerative diseases
    • (Wasco W, Tanzi RE, eds). Humana Press, NY.
    • Blass JP. Energy/glucose metabolism in neurodegenerative diseases. In: Molecular Mechanisms of Dementia (Wasco W, Tanzi RE, eds). Humana Press, NY. pp. 91-101, 1997.
    • (1997) Molecular Mechanisms of Dementia , pp. 91-101
    • Blass, J.P.1
  • 21
    • 0020685951 scopus 로고
    • Decreased pyruvate dehydrogenase complex activity in Huntintgton and Alzheimer brain
    • Sorbi S, Bird ED, and Blass JP. Decreased pyruvate dehydrogenase complex activity in Huntintgton and Alzheimer brain. Ann. Neurol. 13: 72-78, 1983.
    • (1983) Ann. Neurol. , vol.13 , pp. 72-78
    • Sorbi, S.1    Bird, E.D.2    Blass, J.P.3
  • 23
    • 0023732664 scopus 로고
    • Reduced activities of thiamine-dependent enzymes in the brains and peripheral tissues of patients with Alzheimer's disease
    • Gibson GE, Sheu K-FR, Blass JP, Baker A, Carlson KC, Harding B, and Perion P. Reduced activities of thiamine-dependent enzymes in the brains and peripheral tissues of patients with Alzheimer's disease. Arch. Neurol. 45: 841-845, 1988.
    • (1988) Arch. Neurol. , vol.45 , pp. 841-845
    • Gibson, G.E.1    Sheu, K.-F.R.2    Blass, J.P.3    Baker, A.4    Carlson, K.C.5    Harding, B.6    Perion, P.7
  • 24
    • 0025650037 scopus 로고
    • Thiamine-dependent enzyme changes in the temporal cortex of patients with Alzheimer's disease
    • Butterworth RF, and Besnard AM. Thiamine-dependent enzyme changes in the temporal cortex of patients with Alzheimer's disease. Metab. Brain. Dis. 5: 179-184, 1990.
    • (1990) Metab. Brain. Dis. , vol.5 , pp. 179-184
    • Butterworth, R.F.1    Besnard, A.M.2
  • 25
    • 0029884010 scopus 로고    scopus 로고
    • Brian protein and α-ketoglutarate dehydrogenase complex activity in Alzheimer's disease
    • Mastrogiacomo F, Lindsay JG, Bettendorf L, Rice J, and Kish SJ. Brian protein and α-ketoglutarate dehydrogenase complex activity in Alzheimer's disease. Ann. Neurol. 39: 592-598, 1996.
    • (1996) Ann. Neurol. , vol.39 , pp. 592-598
    • Mastrogiacomo, F.1    Lindsay, J.G.2    Bettendorf, L.3    Rice, J.4    Kish, S.J.5
  • 26
    • 0028387219 scopus 로고
    • Abnormality of the α-ketoglutarate dehydrogenase complex in fibroblasts from familial Alzheimer's disease
    • Sheu K-FR, Cooper AJL, Koike K, Koike M, Lindsay JG, and Blass JP. Abnormality of the α-ketoglutarate dehydrogenase complex in fibroblasts from familial Alzheimer's disease. Ann. Neurol. 35: 312-318, 1994.
    • (1994) Ann. Neurol. , vol.35 , pp. 312-318
    • Sheu, K.-F.R.1    Cooper, A.J.L.2    Koike, K.3    Koike, M.4    Lindsay, J.G.5    Blass, J.P.6
  • 27
    • 0030709194 scopus 로고    scopus 로고
    • Inherent abnormalities in oxidative metabolism in Alzheimer disease: Interaction with vascular abnormalities
    • Blass JP, Sheu K-FR, Piacentini, S, and Sorbi, S. Inherent abnormalities in oxidative metabolism in Alzheimer disease: Interaction with vascular abnormalities. Ann. NY Acad. Sci. 826: 382-385, 1997.
    • (1997) Ann. NY Acad. Sci. , vol.826 , pp. 382-385
    • Blass, J.P.1    Sheu, K.-F.R.2    Piacentini, S.3    Sorbi, S.4
  • 28
    • 0028229120 scopus 로고
    • Cerebellar α-ketoglutarate dehydrogenase activity is reduced in spinocerebellar ataxia type I
    • Mastrogiacomo F, and Kish SJ. Cerebellar α-ketoglutarate dehydrogenase activity is reduced in spinocerebellar ataxia type I. Ann. Neurol. 35: 624-626, 1994.
    • (1994) Ann. Neurol. , vol.35 , pp. 624-626
    • Mastrogiacomo, F.1    Kish, S.J.2
  • 29
    • 0028176592 scopus 로고
    • An immunohistochemical study of α-ketoglutarate dehydrogenase complex in Parkinson's disease
    • Mizuno Y, Matuda S, Yoshino H, Mori H, Hattori N, and Ikebe S. An immunohistochemical study of α-ketoglutarate dehydrogenase complex in Parkinson's disease. Ann. Neurol. 35: 204-210, 1994.
    • (1994) Ann. Neurol. , vol.35 , pp. 204-210
    • Mizuno, Y.1    Matuda, S.2    Yoshino, H.3    Mori, H.4    Hattori, N.5    Ikebe, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.