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Volumn 54, Issue 2, 1998, Pages 276-287

Abnormal properties of creatine kinase in Alzheimer's disease brain: Correlation of reduced enzyme activity and active site photolabeling with aberrant cytosol-membrane partitioning

Author keywords

Activity; Alzheimer's; Creatine kinase; Microtubule; Nucleotidylation; Partitioning; Photoaffinity

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; BRAIN ENZYME; CREATINE KINASE; GUANOSINE TRIPHOSPHATE; NUCLEOTIDE; PHOSPHORUS 32; TUBULIN;

EID: 0032030854     PISSN: 0169328X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0169-328X(97)00343-4     Document Type: Article
Times cited : (125)

References (53)
  • 1
    • 0021891892 scopus 로고
    • The creatine-creatine phosphate energy shuttle
    • Bessman S.P., Carpenter C.L. The creatine-creatine phosphate energy shuttle. Ann. Rev. Biochem. 54:1985;831-863.
    • (1985) Ann. Rev. Biochem. , vol.54 , pp. 831-863
    • Bessman, S.P.1    Carpenter, C.L.2
  • 2
    • 0025788513 scopus 로고
    • Coupled in vivo activity of creatine phosphokinase and the membrane bound (Na, K)-ATPase in the resting and stimulated electric organ of the electric fish Narcine brasiliensis
    • Blum H., Balschi J.A., Johnson R.G. Coupled in vivo activity of creatine phosphokinase and the membrane bound (Na, K)-ATPase in the resting and stimulated electric organ of the electric fish Narcine brasiliensis. J. Biol. Chem. 266:1991;10254-10259.
    • (1991) J. Biol. Chem. , vol.266 , pp. 10254-10259
    • Blum, H.1    Balschi, J.A.2    Johnson, R.G.3
  • 3
    • 0021885863 scopus 로고
    • Reduced proteins in the temporal cortex in Alzheimer's disease: An electrophoretic study
    • Borthwick N.M., Yates C.M., Gordon A. Reduced proteins in the temporal cortex in Alzheimer's disease: An electrophoretic study. J. Neurochem. 44(5):1985;1436-1441.
    • (1985) J. Neurochem. , vol.44 , Issue.5 , pp. 1436-1441
    • Borthwick, N.M.1    Yates, C.M.2    Gordon, A.3
  • 5
    • 0026577487 scopus 로고
    • Decreased level of creatine kinase BB in the frontal cortex of Alzheimer patients
    • Burbaeva G.S., Aksenova M.V., Makarenko I.G. Decreased level of creatine kinase BB in the frontal cortex of Alzheimer patients. Dementia. 3:1992;91-94.
    • (1992) Dementia , vol.3 , pp. 91-94
    • Burbaeva, G.S.1    Aksenova, M.V.2    Makarenko, I.G.3
  • 6
    • 0018401885 scopus 로고
    • Synthesis and use of azido photoaffinity analogs of adenine and guanine nucleotides
    • Czarneki J., Geahlen R.T., Haley B.E. Synthesis and use of azido photoaffinity analogs of adenine and guanine nucleotides. Methods Enzymol. 60:1979;642-653.
    • (1979) Methods Enzymol. , vol.60 , pp. 642-653
    • Czarneki, J.1    Geahlen, R.T.2    Haley, B.E.3
  • 7
    • 0023959399 scopus 로고    scopus 로고
    • Energy metabolism and quantal acetylcholine release: Effects of botulinium toxin, 1-fluoro 2,4-dinitrobenzene and diamide in the torpedo electric organ
    • Dunant Y., Loctin F., Marsal J., Muller D., Parducz A., Rabasseda X. Energy metabolism and quantal acetylcholine release: Effects of botulinium toxin, 1-fluoro 2,4-dinitrobenzene and diamide in the torpedo electric organ. J. Neurochem. 50:1998;431-439.
    • (1998) J. Neurochem. , vol.50 , pp. 431-439
    • Dunant, Y.1    Loctin, F.2    Marsal, J.3    Muller, D.4    Parducz, A.5    Rabasseda, X.6
  • 8
    • 0017367189 scopus 로고
    • Creatine kinase isoenzyme associated with synaptosomal membrane and synaptic vesicles
    • Friedhoff A.J., Lerner M.H. Creatine kinase isoenzyme associated with synaptosomal membrane and synaptic vesicles. Life Sci. 20:1977;867-873.
    • (1977) Life Sci. , vol.20 , pp. 867-873
    • Friedhoff, A.J.1    Lerner, M.H.2
  • 10
    • 0018582775 scopus 로고
    • Use of a GTP photoaffinity probe to resolve aspects of the mechanism of tubulin polymerization
    • Geahlen R.L., Haley B.E. Use of a GTP photoaffinity probe to resolve aspects of the mechanism of tubulin polymerization. J. Biol. Chem. 254:1979;11982-11987.
    • (1979) J. Biol. Chem. , vol.254 , pp. 11982-11987
    • Geahlen, R.L.1    Haley, B.E.2
  • 11
    • 0027724210 scopus 로고
    • Kinetics of assembly and dissociation of the mitochondrial creatine kinase octamer, a fluorescence study
    • Gross M., Wallimann T. Kinetics of assembly and dissociation of the mitochondrial creatine kinase octamer, a fluorescence study. Biochemistry. 32:1993;13933-13940.
    • (1993) Biochemistry , vol.32 , pp. 13933-13940
    • Gross, M.1    Wallimann, T.2
  • 12
    • 0027080730 scopus 로고
    • Detection of glutamine synthetase in cerebrospinal fluid of Alzheimer's diseased patients: A potential diagnostic biochemical marker
    • Gunnersen D., Haley B.E. Detection of glutamine synthetase in cerebrospinal fluid of Alzheimer's diseased patients: A potential diagnostic biochemical marker. Proc. Natl. Acad. Sci. USA. 89:1992;11949-11953.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11949-11953
    • Gunnersen, D.1    Haley, B.E.2
  • 13
    • 0029101502 scopus 로고
    • Autophosphorylation of creatine kinase: Characterization and identification of a specifically phosphorylated peptide
    • Hemmer W., Furter-Graves E.M., Frank G., Walliman T., Furter R. Autophosphorylation of creatine kinase: Characterization and identification of a specifically phosphorylated peptide. Biochim. Biophys. Acta. 1251:1995;81-90.
    • (1995) Biochim. Biophys. Acta , vol.1251 , pp. 81-90
    • Hemmer, W.1    Furter-Graves, E.M.2    Frank, G.3    Walliman, T.4    Furter, R.5
  • 17
    • 0021750299 scopus 로고
    • Creatine kinase as an intracellular regulator
    • Iyengar M.R. Creatine kinase as an intracellular regulator. J. Muscle Res. Cell Motil. 5:1984;527-534.
    • (1984) J. Muscle Res. Cell Motil. , vol.5 , pp. 527-534
    • Iyengar, M.R.1
  • 19
    • 0010624422 scopus 로고
    • Aberrant guanine triphosphate β-tubulin interaction in Alzheimer's disease
    • Khatoon S., Campbell S.R., Haley B.E., Slevin J.T. Aberrant guanine triphosphate β-tubulin interaction in Alzheimer's disease. Ann. Neurol. 19:1990;371-376.
    • (1990) Ann. Neurol. , vol.19 , pp. 371-376
    • Khatoon, S.1    Campbell, S.R.2    Haley, B.E.3    Slevin, J.T.4
  • 20
    • 0027297291 scopus 로고
    • The effect of changes in iron redox state on the activity of enzymes sensitive to modification of SH groups
    • Korge P., Campbell K.B. The effect of changes in iron redox state on the activity of enzymes sensitive to modification of SH groups. Arch. Biochem. Biophys. 304:1993;420-428.
    • (1993) Arch. Biochem. Biophys. , vol.304 , pp. 420-428
    • Korge, P.1    Campbell, K.B.2
  • 21
    • 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
  • 22
    • 0025117913 scopus 로고
    • Creatine kinase activity of urinary bladder and skeletal muscle from control and streptozotocin-diabetic rats
    • Levin R.M., Longhurst P.A., Levin S.S., Hangaard N., Wein A.J. Creatine kinase activity of urinary bladder and skeletal muscle from control and streptozotocin-diabetic rats. Mol. Cell. Biochem. 97:1990;153-159.
    • (1990) Mol. Cell. Biochem. , vol.97 , pp. 153-159
    • Levin, R.M.1    Longhurst, P.A.2    Levin, S.S.3    Hangaard, N.4    Wein, A.J.5
  • 23
    • 0020550405 scopus 로고
    • Neurone-specific enolase and creatine phosphokinase are protein components of rat brain synaptic plasma membranes
    • Lim L., Hall C., Leung T., Mahadevan L., Whatley S. Neurone-specific enolase and creatine phosphokinase are protein components of rat brain synaptic plasma membranes. J. Neurochem. 41:1983;1177-1181.
    • (1983) J. Neurochem. , vol.41 , pp. 1177-1181
    • Lim, L.1    Hall, C.2    Leung, T.3    Mahadevan, L.4    Whatley, S.5
  • 24
    • 0025943550 scopus 로고
    • Creatine kinase activity in postnatal rat brain development and in cultured neurons, astrocytes, and oligodendrocytes
    • Manos P., Bryan G.K., Edmund J. Creatine kinase activity in postnatal rat brain development and in cultured neurons, astrocytes, and oligodendrocytes. J. Neurochem. 56:1991;2101-2107.
    • (1991) J. Neurochem. , vol.56 , pp. 2101-2107
    • Manos, P.1    Bryan, G.K.2    Edmund, J.3
  • 28
    • 0026636023 scopus 로고
    • Calcium as sculptor and destroyer of neural circuitry
    • Mattson M.P. Calcium as sculptor and destroyer of neural circuitry. Exp. Gerontol. 27:1992;29-49.
    • (1992) Exp. Gerontol. , vol.27 , pp. 29-49
    • Mattson, M.P.1
  • 30
    • 0027988440 scopus 로고
    • Photoaffinity labeling of creatine kinase with 2-azido- and 8-azidoadenosine triphosphate: Identification of two peptides from the ATP-binding domain
    • Olcott M.C., Bradley M.L., Haley B.E. Photoaffinity labeling of creatine kinase with 2-azido- and 8-azidoadenosine triphosphate: Identification of two peptides from the ATP-binding domain. Biochemistry. 33:1994;11935-11941.
    • (1994) Biochemistry , vol.33 , pp. 11935-11941
    • Olcott, M.C.1    Bradley, M.L.2    Haley, B.E.3
  • 32
    • 0345512210 scopus 로고
    • Anatomial correlations of the distribution of the pathological changes in the neocortex in Alzheimer's disease
    • Pearson R.C., Esiri M.M., Hiorns R.W., Wilcock G.K., Powell T.P.S. Anatomial correlations of the distribution of the pathological changes in the neocortex in Alzheimer's disease. Proc. Natl. Acad. Sci. USA. 82:1985;4531-4534.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4531-4534
    • Pearson, R.C.1    Esiri, M.M.2    Hiorns, R.W.3    Wilcock, G.K.4    Powell, T.P.S.5
  • 33
    • 0010553716 scopus 로고
    • Mercury-EDTA complex specifically blocks brain β-tubulin-GTP interactions: Similarity to observations in Alzheimer's disease
    • in: L.T. Friberg, G.N. Schrauzer (Eds.) Georg Thieme Verlag, Stuttgart
    • J.C. Pendergrass, B.E. Haley, Mercury-EDTA complex specifically blocks brain β-tubulin-GTP interactions: Similarity to observations in Alzheimer's disease, in: L.T. Fribergs, G.N. Schrauzer (Eds.), Status Quo and Perspective of Amalgam and Other Dental Materials, Int. Symposium Proc., Georg Thieme Verlag, Stuttgart, 1995, pp. 98-105.
    • (1995) Status Quo and Perspective of Amalgam and Other Dental Materials, Int. Symposium Proc. , pp. 98-105
    • Pendergrass, J.C.1    Haley, B.E.2
  • 34
    • 0030823798 scopus 로고    scopus 로고
    • Mercury vapor inhalation inhibits binding of GTP to tubulin in rat brain: Similarity to a molecular lesion in Alzheimer's diseased brain
    • Pendergrass J.C., Haley B., Vimy M., Winfield S., Lorscheider F. Mercury vapor inhalation inhibits binding of GTP to tubulin in rat brain: Similarity to a molecular lesion in Alzheimer's diseased brain. Neurotoxicology. 18(2):1997;1-10.
    • (1997) Neurotoxicology , vol.18 , Issue.2 , pp. 1-10
    • Pendergrass, J.C.1    Haley, B.2    Vimy, M.3    Winfield, S.4    Lorscheider, F.5
  • 35
    • 0028326937 scopus 로고
    • Alterations of cerebral metabolism in probable Alzheimer's disease: A preliminary study
    • Pettegrew J.W., Panchalingam K., Klunk W.E., McLure R.J., Muenz L.R. Alterations of cerebral metabolism in probable Alzheimer's disease: A preliminary study. Neurobiol. Aging. 15:1994;117-132.
    • (1994) Neurobiol. Aging , vol.15 , pp. 117-132
    • Pettegrew, J.W.1    Panchalingam, K.2    Klunk, W.E.3    McLure, R.J.4    Muenz, L.R.5
  • 36
    • 0020687726 scopus 로고
    • Nucleotide binding sites with 8-azido purine analogs: Techniques and applications
    • Potter R., Haley B.E. Nucleotide binding sites with 8-azido purine analogs: Techniques and applications. Methods Enzymol. 91:1983;613-633.
    • (1983) Methods Enzymol. , vol.91 , pp. 613-633
    • Potter, R.1    Haley, B.E.2
  • 37
    • 0024996554 scopus 로고
    • Phosphorylation of chicken brain-type creatine kinase affects a physiologically important kinetic parameter and gives rise to protein microheterogeneity in vivo
    • Quest A.F.G., Soldati T., Hemmer W., Perriard J.C., Eppenberger H.M., Walliman T. Phosphorylation of chicken brain-type creatine kinase affects a physiologically important kinetic parameter and gives rise to protein microheterogeneity in vivo. FEBS Lett. 269(2):1990;457-464.
    • (1990) FEBS Lett. , vol.269 , Issue.2 , pp. 457-464
    • Quest, A.F.G.1    Soldati, T.2    Hemmer, W.3    Perriard, J.C.4    Eppenberger, H.M.5    Walliman, T.6
  • 38
    • 0026750820 scopus 로고
    • Identification of peptides from the adenine binding domain of ATP and AMP in adenylate kinase: Isolation of photoaffinity labeled peptides by metal chelate chromatography
    • Salvucci M., Chavan A., Haley B.E. Identification of peptides from the adenine binding domain of ATP and AMP in adenylate kinase: Isolation of photoaffinity labeled peptides by metal chelate chromatography. Biochemistry. 31:1992;884-891.
    • (1992) Biochemistry , vol.31 , pp. 884-891
    • Salvucci, M.1    Chavan, A.2    Haley, B.E.3
  • 39
    • 0031009863 scopus 로고    scopus 로고
    • A comparison of changes in nucleotide-protein interactions in the striatal, hippocampus and paramedian cortex after cerebral ischemia and reperfusion: Correlations to regional vulnerability
    • in press.
    • B. Sankaran, J. Clemens, B. Haley, A comparison of changes in nucleotide-protein interactions in the striatal, hippocampus and paramedian cortex after cerebral ischemia and reperfusion: Correlations to regional vulnerability, Mol. Brain Res., 1997, in press.
    • (1997) Mol. Brain Res.
    • Sankaran, B.1    Clemens, J.2    Haley, B.3
  • 43
    • 0017197647 scopus 로고
    • Creatine kinase in serum: Determination of optimum reaction conditions
    • Szaz G., Gruber W., Bernt E. Creatine kinase in serum: Determination of optimum reaction conditions. Clin. Chem. 22:1979;650.
    • (1979) Clin. Chem. , vol.22 , pp. 650
    • Szaz, G.1    Gruber, W.2    Bernt, E.3
  • 45
    • 0023262939 scopus 로고
    • Human creatine kinase: Isolation and sequence analysis of cDNA clones for the β-subunit, development of subunit specific probes and determination of gene copy number
    • Villarreal-Levy G., Ma T.S., Kerner S.A., Roberts R., Perryman M.B. Human creatine kinase: Isolation and sequence analysis of cDNA clones for the β-subunit, development of subunit specific probes and determination of gene copy number. Biochem. Biophys. Res. Commun. 108:1987;1116-1127.
    • (1987) Biochem. Biophys. Res. Commun. , vol.108 , pp. 1116-1127
    • Villarreal-Levy, G.1    Ma, T.S.2    Kerner, S.A.3    Roberts, R.4    Perryman, M.B.5
  • 46
    • 0026585611 scopus 로고
    • Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: The 'phosphocreatine circuit' for cellular energy homeostasis
    • Walliman T., Wyss M., Brdiczka D., Nicolay K., Eppenberger H.M. Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: The 'phosphocreatine circuit' for cellular energy homeostasis. Biochem. J. 281:1992;21-40.
    • (1992) Biochem. J. , vol.281 , pp. 21-40
    • Walliman, T.1    Wyss, M.2    Brdiczka, D.3    Nicolay, K.4    Eppenberger, H.M.5
  • 47
    • 0026035791 scopus 로고
    • Profiles of creatine kinase isoenzyme compositions in single muscle fibres of different types
    • Yamashita K., Yoshioka T. Profiles of creatine kinase isoenzyme compositions in single muscle fibres of different types. J. Muscle Res. Cell Motil. 12:1991;37-44.
    • (1991) J. Muscle Res. Cell Motil. , vol.12 , pp. 37-44
    • Yamashita, K.1    Yoshioka, T.2
  • 48
    • 0020577262 scopus 로고
    • Immunohistochemical localization of creatine kinase BB-isoenzyme in human brain: Comparison with tubulin and astroprotein
    • Yoshimine T., Morimoto K., Homberger H.A., Yanagihara T. Immunohistochemical localization of creatine kinase BB-isoenzyme in human brain: Comparison with tubulin and astroprotein. Brain Res. 265:1983;101-108.
    • (1983) Brain Res. , vol.265 , pp. 101-108
    • Yoshimine, T.1    Morimoto, K.2    Homberger, H.A.3    Yanagihara, T.4
  • 49
    • 0029999787 scopus 로고    scopus 로고
    • Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules
    • Alonso A., Grundke-Iqbal I., Iqbal K. Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules. Nature Med. 2:1996;783-787.
    • (1996) Nature Med. , vol.2 , pp. 783-787
    • Alonso, A.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 51
    • 0028852644 scopus 로고
    • Guanosine triphosphate binding to β-subunit of tubulin in Alzheimer's disease brain: Role of microtubule-associated protein τ
    • Khatoon S., Grundke-Iqbal I., Iqbal K. Guanosine triphosphate binding to β-subunit of tubulin in Alzheimer's disease brain: role of microtubule-associated protein τ J. Neurochem. 64:1995;777-787.
    • (1995) J. Neurochem. , vol.64 , pp. 777-787
    • Khatoon, S.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 53
    • 0030638741 scopus 로고    scopus 로고
    • Inhibition of brain tubulin-guanosine 5′-triphosphate interactions by mercury: Similarity to observations in Alzheimer's disease brain
    • in: H. Sigel, A. Sigel (Eds.) Chap. 16, Marcel Dekker, New York
    • J.C. Pendergrass, B.E. Haley, Inhibition of brain tubulin-guanosine 5′-triphosphate interactions by mercury: Similarity to observations in Alzheimer's disease brain, in: H. Sigel, A. Sigel (Eds.), Metal Ions in Biological Systems V34, Mercury and its Effects on Environment and Biology, Chap. 16, Marcel Dekker, New York, 1996, 461-478.
    • (1996) Metal Ions in Biological Systems V34, Mercury and its Effects on Environment and Biology , pp. 461-478
    • Pendergrass, J.C.1    Haley, B.E.2


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