메뉴 건너뛰기




Volumn 314, Issue 1, 2003, Pages 121-127

Immunocapture and microplate-based activity measurement of mammalian pyruvate dehydrogenase complex

Author keywords

Activity assay; Immunocapture; Phosphorylation; Pyruvate dehydrogenase

Indexed keywords

CELL CULTURE; MAMMALS; MONOCLONAL ANTIBODIES; NEURODEGENERATIVE DISEASES; PHOSPHORYLATION;

EID: 0037333309     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0003-2697(02)00645-0     Document Type: Article
Times cited : (20)

References (45)
  • 2
    • 0028979684 scopus 로고
    • Mammalian alpha-keto acid dehydrogenase complexes: Gene regulation and genetic defects
    • Patel M.S., Harris R.A. Mammalian alpha-keto acid dehydrogenase complexes: Gene regulation and genetic defects. FASEB J. 9:1995;1164-1172.
    • (1995) FASEB J. , vol.9 , pp. 1164-1172
    • Patel, M.S.1    Harris, R.A.2
  • 3
    • 0031973056 scopus 로고    scopus 로고
    • Starvation and diabetes increase the amount of pyruvate dehydrogenase kinase isoenzyme 4 in rat heart
    • Wu P., Sato J., Zhao Y., Jaskiewicz J., Popov K.M., Harris R.A. Starvation and diabetes increase the amount of pyruvate dehydrogenase kinase isoenzyme 4 in rat heart. Biochem. J. 329(Pt 1):1998;197-201.
    • (1998) Biochem. J. , vol.329 , Issue.PART 1 , pp. 197-201
    • Wu, P.1    Sato, J.2    Zhao, Y.3    Jaskiewicz, J.4    Popov, K.M.5    Harris, R.A.6
  • 4
    • 0032983691 scopus 로고    scopus 로고
    • Activities of key glycolytic enzymes in the brains of patients with Alzheimer's disease
    • Bigl M., Bruckner M.K., Arendt T., Bigl V., Eschrich K. Activities of key glycolytic enzymes in the brains of patients with Alzheimer's disease. J. Neural. Transm. 106:1999;499-511.
    • (1999) J. Neural. Transm. , vol.106 , pp. 499-511
    • Bigl, M.1    Bruckner, M.K.2    Arendt, T.3    Bigl, V.4    Eschrich, K.5
  • 5
    • 0032847523 scopus 로고    scopus 로고
    • Sepsis alters pyruvate dehydrogenase kinase activity in skeletal muscle
    • Vary T.C., Hazen S. Sepsis alters pyruvate dehydrogenase kinase activity in skeletal muscle. Mol. Cell. Biochem. 198:1999;113-118.
    • (1999) Mol. Cell. Biochem. , vol.198 , pp. 113-118
    • Vary, T.C.1    Hazen, S.2
  • 6
    • 0034440140 scopus 로고    scopus 로고
    • A unifying hypothesis of Alzheimer's disease. IV. Causation and sequence of events
    • Heininger K. A unifying hypothesis of Alzheimer's disease. IV. Causation and sequence of events, Rev. Neurosci. 11, Spec No, (2000) 213-328.
    • (2000) Rev. Neurosci. , vol.11 , Issue.SPEC. NO. , pp. 213-328
    • Heininger, K.1
  • 9
    • 0022969384 scopus 로고
    • Properties of a newly characterized protein of the bovine kidney pyruvate dehydrogenase complex
    • Jilka J.M., Rahmatullah M., Kazemi M., Roche T.E. Properties of a newly characterized protein of the bovine kidney pyruvate dehydrogenase complex. J. Biol. Chem. 261:1986;1858-1867.
    • (1986) J. Biol. Chem. , vol.261 , pp. 1858-1867
    • Jilka, J.M.1    Rahmatullah, M.2    Kazemi, M.3    Roche, T.E.4
  • 10
    • 0025221771 scopus 로고
    • Molecular biology and biochemistry of pyruvate dehydrogenase complexes
    • Patel M.S., Roche T.E. Molecular biology and biochemistry of pyruvate dehydrogenase complexes. FASEB J. 4:1990;3224-3233.
    • (1990) FASEB J. , vol.4 , pp. 3224-3233
    • Patel, M.S.1    Roche, T.E.2
  • 12
    • 0031972736 scopus 로고    scopus 로고
    • Evidence for existence of tissue-specific regulation of the mammalian pyruvate dehydrogenase complex
    • Bowker-Kinley M.M., Davis W.I., Wu P., Harris R.A., Popov K.M. Evidence for existence of tissue-specific regulation of the mammalian pyruvate dehydrogenase complex. Biochem. J. 329(Pt 1):1998;191-196.
    • (1998) Biochem. J. , vol.329 , Issue.PART 1 , pp. 191-196
    • Bowker-Kinley, M.M.1    Davis, W.I.2    Wu, P.3    Harris, R.A.4    Popov, K.M.5
  • 13
    • 0033571611 scopus 로고    scopus 로고
    • Evidence that pyruvate dehydrogenase kinase belongs to the ATPase/kinase superfamily
    • Bowker-Kinley M., Popov K.M. Evidence that pyruvate dehydrogenase kinase belongs to the ATPase/kinase superfamily. Biochem. J. 344(Pt 1):1999;47-53.
    • (1999) Biochem. J. , vol.344 , Issue.PART 1 , pp. 47-53
    • Bowker-Kinley, M.1    Popov, K.M.2
  • 14
    • 0032792498 scopus 로고    scopus 로고
    • Mechanism responsible for inactivation of skeletal muscle pyruvate dehydrogenase complex in starvation and diabetes
    • Wu P., Inskeep K., Bowker-Kinley M.M., Popov K.M., Harris R.A. Mechanism responsible for inactivation of skeletal muscle pyruvate dehydrogenase complex in starvation and diabetes. Diabetes. 48:1999;1593-1599.
    • (1999) Diabetes , vol.48 , pp. 1593-1599
    • Wu, P.1    Inskeep, K.2    Bowker-Kinley, M.M.3    Popov, K.M.4    Harris, R.A.5
  • 15
    • 0034717278 scopus 로고    scopus 로고
    • Marked differences between two isoforms of human pyruvate dehydrogenase kinase
    • Baker J.C., Yan X., Peng T., Kasten S., Roche T.E. Marked differences between two isoforms of human pyruvate dehydrogenase kinase. J. Biol. Chem. 275:2000;15773-15781.
    • (2000) J. Biol. Chem. , vol.275 , pp. 15773-15781
    • Baker, J.C.1    Yan, X.2    Peng, T.3    Kasten, S.4    Roche, T.E.5
  • 17
    • 0017872490 scopus 로고
    • Phosphorylation of additional sites on pyruvate dehydrogenase inhibits its re-activation by pyruvate dehydrogenase phosphate phosphatase
    • Sugden P.H., Hutson N.J., Kerbey A.L., Randle P.J. Phosphorylation of additional sites on pyruvate dehydrogenase inhibits its re-activation by pyruvate dehydrogenase phosphate phosphatase. Biochem. J. 169:1978;433-435.
    • (1978) Biochem. J. , vol.169 , pp. 433-435
    • Sugden, P.H.1    Hutson, N.J.2    Kerbey, A.L.3    Randle, P.J.4
  • 18
    • 0017808017 scopus 로고
    • Regulation of pig heart pyruvate dehydrogenase by phosphorylation. Studies on the subunit and phosphorylation stoichiometries
    • Sugden P.H., Randle P.J. Regulation of pig heart pyruvate dehydrogenase by phosphorylation. Studies on the subunit and phosphorylation stoichiometries. Biochem. J. 173:1978;659-668.
    • (1978) Biochem. J. , vol.173 , pp. 659-668
    • Sugden, P.H.1    Randle, P.J.2
  • 19
    • 0019320814 scopus 로고
    • Role of multisite phosphorylation in the regulation of ox kidney pyruvate dehydrogenase complex
    • Sugden P.H., Simister N.E. Role of multisite phosphorylation in the regulation of ox kidney pyruvate dehydrogenase complex. FEBS Lett. 111:1980;299-302.
    • (1980) FEBS Lett. , vol.111 , pp. 299-302
    • Sugden, P.H.1    Simister, N.E.2
  • 20
    • 0028927142 scopus 로고
    • The effect of phosphorylation on pyruvate dehydrogenase
    • Korotchkina L.G., Khailova L.S., Severin S.E. The effect of phosphorylation on pyruvate dehydrogenase. FEBS Lett. 364:1995;185-188.
    • (1995) FEBS Lett. , vol.364 , pp. 185-188
    • Korotchkina, L.G.1    Khailova, L.S.2    Severin, S.E.3
  • 21
    • 0033646624 scopus 로고    scopus 로고
    • Morphological correlates of mitochondrial dysfunction in children
    • Chow C.W., Thorburn D.R. Morphological correlates of mitochondrial dysfunction in children. Hum. Reprod. 15(Suppl. 2):2000;68-78.
    • (2000) Hum. Reprod. , vol.15 , Issue.SUPPL. 2 , pp. 68-78
    • Chow, C.W.1    Thorburn, D.R.2
  • 22
    • 0035933049 scopus 로고    scopus 로고
    • Inborn errors of metabolism: A cause of abnormal brain development
    • Nissenkorn A., Michelson M., Ben-Zeev B., Lerman-Sagie T. Inborn errors of metabolism: a cause of abnormal brain development. Neurology. 56:2001;1265-1272.
    • (2001) Neurology , vol.56 , pp. 1265-1272
    • Nissenkorn, A.1    Michelson, M.2    Ben-Zeev, B.3    Lerman-Sagie, T.4
  • 23
    • 0031797717 scopus 로고    scopus 로고
    • Complexities of the pyruvate dehydrogenase complex
    • De Vivo D.C. Complexities of the pyruvate dehydrogenase complex. Neurology. 51:1998;1247-1249.
    • (1998) Neurology , vol.51 , pp. 1247-1249
    • De Vivo, D.C.1
  • 25
    • 0036487988 scopus 로고    scopus 로고
    • Pyruvate dehydrogenase E3 binding protein deficiency
    • Brown R.M., Head R.A., Brown G.K. Pyruvate dehydrogenase E3 binding protein deficiency. Hum. Genet. 110:2002;187-191.
    • (2002) Hum. Genet. , vol.110 , pp. 187-191
    • Brown, R.M.1    Head, R.A.2    Brown, G.K.3
  • 26
    • 0036068958 scopus 로고    scopus 로고
    • Detection of pyruvate dehydrogenase E1 α-subunit deficiencies in females by immunohistochemical demonstration of mosaicism in cultured fibroblasts
    • Lib M.Y., Brown R.M., Brown G.K., Marusich M.F., Capaldi R.A. Detection of pyruvate dehydrogenase E1 α-subunit deficiencies in females by immunohistochemical demonstration of mosaicism in cultured fibroblasts. J. Histochem. Cytochem. 50:2002;877-884.
    • (2002) J. Histochem. Cytochem. , vol.50 , pp. 877-884
    • Lib, M.Y.1    Brown, R.M.2    Brown, G.K.3    Marusich, M.F.4    Capaldi, R.A.5
  • 27
    • 0035044161 scopus 로고    scopus 로고
    • A novel subfractionation approach for mitochondrial proteins: A three-dimensional mitochondrial proteome map
    • Hanson B.J., Schulenberg B., Patton W.F., Capaldi R.A. A novel subfractionation approach for mitochondrial proteins: a three-dimensional mitochondrial proteome map. Electrophoresis. 22:2001;950-959.
    • (2001) Electrophoresis , vol.22 , pp. 950-959
    • Hanson, B.J.1    Schulenberg, B.2    Patton, W.F.3    Capaldi, R.A.4
  • 28
    • 0018857230 scopus 로고
    • Immunological assays of the NADH dehydrogenase content of bovine heart mitochondria and submitochondrial particles
    • Smith S., Cottingham I.R., Ragan C.I. Immunological assays of the NADH dehydrogenase content of bovine heart mitochondria and submitochondrial particles. FEBS Lett. 110:1980;279-282.
    • (1980) FEBS Lett. , vol.110 , pp. 279-282
    • Smith, S.1    Cottingham, I.R.2    Ragan, C.I.3
  • 29
    • 0036605793 scopus 로고    scopus 로고
    • A resarufin-based fluorescent assay for quantifying NADH
    • Batchelor R.H., Zhou M. A resarufin-based fluorescent assay for quantifying NADH. Anal. Biochem. 305:2002;118-119.
    • (2002) Anal. Biochem. , vol.305 , pp. 118-119
    • Batchelor, R.H.1    Zhou, M.2
  • 30
    • 0017693325 scopus 로고
    • Purification of porcine liver pyruvate dehydrogenase complex and characterization of its catalytic and regulatory properties
    • Roche T.E., Cate R.L. Purification of porcine liver pyruvate dehydrogenase complex and characterization of its catalytic and regulatory properties. Arch. Biochem. Biophys. 183:1977;664-677.
    • (1977) Arch. Biochem. Biophys. , vol.183 , pp. 664-677
    • Roche, T.E.1    Cate, R.L.2
  • 32
    • 0019827971 scopus 로고
    • An NADH-linked spectrophotometric assay for pyruvate dehydrogenase complex in crude tissue homogenates
    • Hinman L.M., Blass J.P. An NADH-linked spectrophotometric assay for pyruvate dehydrogenase complex in crude tissue homogenates. J. Biol. Chem. 256:1981;6583-6586.
    • (1981) J. Biol. Chem. , vol.256 , pp. 6583-6586
    • Hinman, L.M.1    Blass, J.P.2
  • 33
    • 0020539394 scopus 로고
    • A sensitive spectrophotometric assay for pyruvate dehydrogenase and oxoglutarate dehydrogenase complexes
    • Gohil K., Jones D.A. A sensitive spectrophotometric assay for pyruvate dehydrogenase and oxoglutarate dehydrogenase complexes. Biochem. Rep. 3:1983;1-9.
    • (1983) Biochem. Rep. , vol.3 , pp. 1-9
    • Gohil, K.1    Jones, D.A.2
  • 34
    • 0022006965 scopus 로고
    • Immunochemical characterization of pyruvate dehydrogenase complex in rat brain
    • Sheu K.F., Lai J.C., Kim Y.T., Dorante G., Bagg J. Immunochemical characterization of pyruvate dehydrogenase complex in rat brain. J. Neurochem. 44:1985;593-599.
    • (1985) J. Neurochem. , vol.44 , pp. 593-599
    • Sheu, K.F.1    Lai, J.C.2    Kim, Y.T.3    Dorante, G.4    Bagg, J.5
  • 35
    • 0022527039 scopus 로고
    • A sensitive spectrophotometric assay of pyruvate dehydrogenase activity
    • Scislowski P.W., Davis E.J. A sensitive spectrophotometric assay of pyruvate dehydrogenase activity. Anal. Biochem. 155:1986;400-404.
    • (1986) Anal. Biochem. , vol.155 , pp. 400-404
    • Scislowski, P.W.1    Davis, E.J.2
  • 36
    • 0023851568 scopus 로고
    • Pyruvate dehydrogenase activity in osmotically shocked rat brain mitochondria: Stimulation by oxaloacetate
    • Haas R.H., Thompson G., Morris B., Conright K., Andrews T. Pyruvate dehydrogenase activity in osmotically shocked rat brain mitochondria: stimulation by oxaloacetate. J. Neurochem. 50:1988;673-680.
    • (1988) J. Neurochem. , vol.50 , pp. 673-680
    • Haas, R.H.1    Thompson, G.2    Morris, B.3    Conright, K.4    Andrews, T.5
  • 37
    • 0023030955 scopus 로고
    • Immunochemical analysis of normal and mutant forms of human pyruvate dehydrogenase
    • Wicking C.A., Scholem R.D., Hunt S.M., Brown G.K. Immunochemical analysis of normal and mutant forms of human pyruvate dehydrogenase. Biochem. J. 239:1986;89-96.
    • (1986) Biochem. J. , vol.239 , pp. 89-96
    • Wicking, C.A.1    Scholem, R.D.2    Hunt, S.M.3    Brown, G.K.4
  • 39
    • 0019131187 scopus 로고
    • An improved method for the assay of platelet pyruvate dehydrogenase
    • Schofield P.J., Griffiths L.R., Rogers S.H., Wise G. An improved method for the assay of platelet pyruvate dehydrogenase. Clin. Chim. Acta. 108:1980;219-227.
    • (1980) Clin. Chim. Acta , vol.108 , pp. 219-227
    • Schofield, P.J.1    Griffiths, L.R.2    Rogers, S.H.3    Wise, G.4
  • 40
    • 0027199318 scopus 로고
    • An improvement in the pyruvate dehydrogenase complex assay: A high-yield method for purifying acrylamine acetyltransferase
    • Brooks S.P., Storey K.B. An improvement in the pyruvate dehydrogenase complex assay: a high-yield method for purifying acrylamine acetyltransferase. Anal. Biochem. 212:1993;452-456.
    • (1993) Anal. Biochem. , vol.212 , pp. 452-456
    • Brooks, S.P.1    Storey, K.B.2
  • 41
    • 0017115996 scopus 로고
    • The elementary reactions of the pig heart pyruvate dehydrogenase complex: A study of the inhibition by phosphorylation
    • Walsh D.A., Cooper R.H., Denton R.M., Bridges B.J., Randle P.J. The elementary reactions of the pig heart pyruvate dehydrogenase complex: a study of the inhibition by phosphorylation. Biochem. J. 157:1976;41-67.
    • (1976) Biochem. J. , vol.157 , pp. 41-67
    • Walsh, D.A.1    Cooper, R.H.2    Denton, R.M.3    Bridges, B.J.4    Randle, P.J.5
  • 42
    • 0034974261 scopus 로고    scopus 로고
    • Monomethylarsonous acid (MMA(III)) and arsenite: LD(50) in hamsters and in vitro inhibition of pyruvate dehydrogenase
    • Petrick J.S., Jagadish B., Mash E.A., Aposhian H.V. Monomethylarsonous acid (MMA(III)) and arsenite: LD(50) in hamsters and in vitro inhibition of pyruvate dehydrogenase. Chem. Res. Toxicol. 14:2001;651-656.
    • (2001) Chem. Res. Toxicol. , vol.14 , pp. 651-656
    • Petrick, J.S.1    Jagadish, B.2    Mash, E.A.3    Aposhian, H.V.4
  • 43
    • 0019973214 scopus 로고
    • Dichloroacetate tissue concentration and its relationship to hypolactatemia and pyruvate dehydrogenase activation
    • Evans O.B. Dichloroacetate tissue concentration and its relationship to hypolactatemia and pyruvate dehydrogenase activation. Biochem. Pharmacol. 31:1982;3124-3126.
    • (1982) Biochem. Pharmacol. , vol.31 , pp. 3124-3126
    • Evans, O.B.1
  • 44
    • 0020518065 scopus 로고
    • Effects of dichloroacetate on brain tissue pyruvate dehydrogenase
    • Evans O.B. Effects of dichloroacetate on brain tissue pyruvate dehydrogenase. J. Neurochem. 41:1983;1052-1056.
    • (1983) J. Neurochem. , vol.41 , pp. 1052-1056
    • Evans, O.B.1
  • 45
    • 0032806174 scopus 로고    scopus 로고
    • PDH activation by dichloroacetate reduces TCA cycle intermediates at rest but not during exercise in humans
    • Gibala M.J., Saltin B. PDH activation by dichloroacetate reduces TCA cycle intermediates at rest but not during exercise in humans. Am. J. Physiol. 277:1999;33-38.
    • (1999) Am. J. Physiol. , vol.277 , pp. 33-38
    • Gibala, M.J.1    Saltin, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.