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Volumn 48, Issue 4, 2004, Pages 379-386

Localization of enolase in synaptic plasma membrane as an αγ heterodimer in rat brain

Author keywords

Enolase; Glycolytic enzyme; Immunoelectron microscopy; Membrane association; SPM; Synaptosome

Indexed keywords

MAGNESIUM ION; NEURON SPECIFIC ENOLASE; TRITON X 100;

EID: 1642326678     PISSN: 01680102     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neures.2003.12.006     Document Type: Article
Times cited : (29)

References (30)
  • 2
    • 84942221732 scopus 로고
    • Standardization of the reaction temperature for the determination of enzyme activity
    • Bergmeyer H.U. Standardization of the reaction temperature for the determination of enzyme activity. Z. Klin. Chem. Klin. Biochem. 11:1973;39-45.
    • (1973) Z. Klin. Chem. Klin. Biochem. , vol.11 , pp. 39-45
    • Bergmeyer, H.U.1
  • 3
    • 0018070988 scopus 로고
    • A rapid method for the preparation of relatively pure metabolically competent synaptosomes from rat brain
    • Booth R.F., Clark J.B. A rapid method for the preparation of relatively pure metabolically competent synaptosomes from rat brain. Biochem. J. 176:1978;365-370.
    • (1978) Biochem. J. , vol.176 , pp. 365-370
    • Booth, R.F.1    Clark, J.B.2
  • 4
    • 0015196699 scopus 로고
    • Subcellular fractionation of cultured glial cells
    • Cotman C., Herschman H., Taylor D. Subcellular fractionation of cultured glial cells. J. Neurobiol. 2:1971;169-180.
    • (1971) J. Neurobiol. , vol.2 , pp. 169-180
    • Cotman, C.1    Herschman, H.2    Taylor, D.3
  • 5
    • 0027930332 scopus 로고
    • Synthetic peptide corresponding to 30 amino acids of the C-terminal of neuron-specific enolase promotes survival of neocortical neurons in culture
    • Hattori T., Ohsawa K., Mizuno Y., Kato K., Kohsaka S. Synthetic peptide corresponding to 30 amino acids of the C-terminal of neuron-specific enolase promotes survival of neocortical neurons in culture. Biochem. Biophys. Res. Commun. 202:1994;25-30.
    • (1994) Biochem. Biophys. Res. Commun. , vol.202 , pp. 25-30
    • Hattori, T.1    Ohsawa, K.2    Mizuno, Y.3    Kato, K.4    Kohsaka, S.5
  • 6
    • 0028899956 scopus 로고
    • Neurotrophic and neuroprotective effects of neuron-specific enolase on cultured neurons from embryonic rat brain
    • Hattori T., Takei N., Mizuno Y., Kato K., Kohsaka S. Neurotrophic and neuroprotective effects of neuron-specific enolase on cultured neurons from embryonic rat brain. Neurosci. Res. 21:1995;191-198.
    • (1995) Neurosci. Res. , vol.21 , pp. 191-198
    • Hattori, T.1    Takei, N.2    Mizuno, Y.3    Kato, K.4    Kohsaka, S.5
  • 7
    • 0033678175 scopus 로고    scopus 로고
    • Discriminating between cell surface and intracellular plasminogen-binding proteins: Heterogeneity in profibrinolytic plasminogen-binding proteins on monocytoid cells
    • Hawley S.B., Green M.A., Miles L.A. Discriminating between cell surface and intracellular plasminogen-binding proteins: heterogeneity in profibrinolytic plasminogen-binding proteins on monocytoid cells. Thromb. Haemost. 84:2000;882-890.
    • (2000) Thromb. Haemost. , vol.84 , pp. 882-890
    • Hawley, S.B.1    Green, M.A.2    Miles, L.A.3
  • 8
    • 0020955120 scopus 로고
    • Synapsin I (protein I), a nerve terminal-specific phosphoprotein, its association with synaptic vesicles studied in a highly purified synaptic vesicle preparation
    • Huttner W.B., Schiebler W., Greengard P., De Camilli P. Synapsin I (protein I), a nerve terminal-specific phosphoprotein, its association with synaptic vesicles studied in a highly purified synaptic vesicle preparation. J. Cell. Biol. 96:1983;1374-1388.
    • (1983) J. Cell. Biol. , vol.96 , pp. 1374-1388
    • Huttner, W.B.1    Schiebler, W.2    Greengard, P.3    De Camilli, P.4
  • 9
    • 0019903951 scopus 로고
    • αγ-enolase in the rat: Ontogeny and tissue distribution
    • Jorgensen O.S., Centervall G. αγ-enolase in the rat: ontogeny and tissue distribution. J. Neurochem. 39:1982;537-542.
    • (1982) J. Neurochem. , vol.39 , pp. 537-542
    • Jorgensen, O.S.1    Centervall, G.2
  • 10
    • 0020083446 scopus 로고
    • Distribution of nervous system-specific forms of enolase in peripheral tissues
    • Kato K., Ishiguro Y., Suzuki F., Ito A., Semba R. Distribution of nervous system-specific forms of enolase in peripheral tissues. Brain Res. 237:1982;441-448.
    • (1982) Brain Res. , vol.237 , pp. 441-448
    • Kato, K.1    Ishiguro, Y.2    Suzuki, F.3    Ito, A.4    Semba, R.5
  • 11
    • 0019782243 scopus 로고
    • Determination of brain enolase isozymes with an enzyme immunoassay at the level of single neurons
    • Kato K., Suzuki F., Semba R. Determination of brain enolase isozymes with an enzyme immunoassay at the level of single neurons. J. Neurochem. 37:1981;998-1005.
    • (1981) J. Neurochem. , vol.37 , pp. 998-1005
    • Kato, K.1    Suzuki, F.2    Semba, R.3
  • 12
    • 0017912933 scopus 로고
    • Association of glycolytic enzymes with particulate fractions from nerve endings
    • Knull H.R. Association of glycolytic enzymes with particulate fractions from nerve endings. Biochim. Biophys. Acta. 522:1978;1-9.
    • (1978) Biochim. Biophys. Acta , vol.522 , pp. 1-9
    • Knull, H.R.1
  • 13
    • 0022251611 scopus 로고
    • Extraction of glycolytic enzymes: Myo-inositol as a marker of membrane porosity
    • Knull H.R. Extraction of glycolytic enzymes: myo-inositol as a marker of membrane porosity. J. Neurochem. 45:1985;1433-1440.
    • (1985) J. Neurochem. , vol.45 , pp. 1433-1440
    • Knull, H.R.1
  • 15
    • 0026489887 scopus 로고
    • Association of glycolytic enzymes with the cytoskeleton
    • Knull H.R., Walsh J.L. Association of glycolytic enzymes with the cytoskeleton. Curr. Top. Cell Regul. 33:1992;15-30.
    • (1992) Curr. Top. Cell Regul. , vol.33 , pp. 15-30
    • Knull, H.R.1    Walsh, J.L.2
  • 16
    • 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
  • 17
    • 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;1177-1182.
    • (1983) J. Neurochem. , vol.41 , pp. 1177-1182
    • Lim, L.1    Hall, C.2    Leung, T.3    Mahadevan, L.4    Whatley, S.5
  • 19
    • 0018874798 scopus 로고
    • An improved method of preparing rat brain synaptic membranes. Elimination of a contaminating membrane containing 2′, 3′-cyclic nucleotide 3′-phosphohydrolase activity
    • Mena E.E., Hoeser C.A., Moore B.W. An improved method of preparing rat brain synaptic membranes. Elimination of a contaminating membrane containing 2′, 3′-cyclic nucleotide 3′-phosphohydrolase activity. Brain Res. 188:1980;207-231.
    • (1980) Brain Res. , vol.188 , pp. 207-231
    • Mena, E.E.1    Hoeser, C.A.2    Moore, B.W.3
  • 20
    • 0021904921 scopus 로고
    • Early adrenalectomy increases myelin content of the rat brain
    • Meyer J.S., Fairman K.R. Early adrenalectomy increases myelin content of the rat brain. Brain Res. 349:1985;1-9.
    • (1985) Brain Res. , vol.349 , pp. 1-9
    • Meyer, J.S.1    Fairman, K.R.2
  • 21
    • 0019800463 scopus 로고
    • Silver stain for proteins in polyacrylamide gels: A modified procedure with enhanced uniform sensitivity
    • Morrissey J.H. Silver stain for proteins in polyacrylamide gels: a modified procedure with enhanced uniform sensitivity. Anal. Biochem. 117:1981;307-310.
    • (1981) Anal. Biochem. , vol.117 , pp. 307-310
    • Morrissey, J.H.1
  • 23
    • 0015857284 scopus 로고
    • Myelination in rat brain: Method of myelin isolation
    • Norton W.T., Poduslo S.E. Myelination in rat brain: method of myelin isolation. J. Neurochem. 21:1973;749-757.
    • (1973) J. Neurochem. , vol.21 , pp. 749-757
    • Norton, W.T.1    Poduslo, S.E.2
  • 25
    • 0034947535 scopus 로고    scopus 로고
    • Multifunctional α-enolase: Its role in diseases
    • Pancholi V. Multifunctional α-enolase: its role in diseases. Cell. Mol. Life Sci. 58:2001;902-920.
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 902-920
    • Pancholi, V.1
  • 26
    • 0018163442 scopus 로고
    • Neurone-specific enolase is a molecular marker for peripheral and central neuroendocrine cells
    • Schmechel D., Marangos P.J., Brightman M. Neurone-specific enolase is a molecular marker for peripheral and central neuroendocrine cells. Nature. 276:1978a;834-836.
    • (1978) Nature , vol.276 , pp. 834-836
    • Schmechel, D.1    Marangos, P.J.2    Brightman, M.3
  • 28
    • 0032973950 scopus 로고    scopus 로고
    • New insights into an old protein: The functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase
    • Sirover M.A. New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase. Biochim. Biophys. Acta. 1432:1999;159-184.
    • (1999) Biochim. Biophys. Acta , vol.1432 , pp. 159-184
    • Sirover, M.A.1
  • 29
    • 0020466660 scopus 로고
    • Effects of maternal protein deficiency on synaptic plasma membranes in offspring
    • Smith D.M., Druse M.J. Effects of maternal protein deficiency on synaptic plasma membranes in offspring. Dev. Neurosci. 5:1982;403-411.
    • (1982) Dev. Neurosci. , vol.5 , pp. 403-411
    • Smith, D.M.1    Druse, M.J.2
  • 30
    • 0026435998 scopus 로고
    • Interactions of glycolytic enzymes with cellular membranes
    • Uyeda K. Interactions of glycolytic enzymes with cellular membranes. Curr. Top. Cell. Regul. 33:1992;31-46.
    • (1992) Curr. Top. Cell. Regul. , vol.33 , pp. 31-46
    • Uyeda, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.