메뉴 건너뛰기




Volumn 66, Issue 3, 1996, Pages 928-935

Evidence that glyceraldehyde-3-phosphate dehydrogenase is involved in age-induced apoptosis in mature cerebellar neurons in culture

Author keywords

Antisense oligodeoxynucleotide; Cerebellar granule cells; Glyceraldehyde 3 phosphate dehydrogenase; Neuronal apoptosis; Overexpression

Indexed keywords

ANTISENSE OLIGONUCLEOTIDE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE;

EID: 0030045251     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1996.66030928.x     Document Type: Article
Times cited : (196)

References (43)
  • 3
    • 0028125811 scopus 로고
    • Comparison of glyceraldehyde-3-phosphate dehydrogenase and 28S-ribosomal RNA gene expression as RNA loading controls for northern blot analysis of cell lines of varying malignant potential
    • Bhatia P., Taylor W. R., Greenberg A. H., and Wright J. A. (1994) Comparison of glyceraldehyde-3-phosphate dehydrogenase and 28S-ribosomal RNA gene expression as RNA loading controls for northern blot analysis of cell lines of varying malignant potential. Anal. Biochem. 216, 223-226.
    • (1994) Anal. Biochem. , vol.216 , pp. 223-226
    • Bhatia, P.1    Taylor, W.R.2    Greenberg, A.H.3    Wright, J.A.4
  • 4
    • 0345074492 scopus 로고
    • Anti-oxidants and NMDA receptor antagonists protect against age-induced apoptosis in cerebellar granule cells
    • Chuang D.-M., Leeds P., Zhang K.-G., Gao X.-M., and Ishitani R. (1995) Anti-oxidants and NMDA receptor antagonists protect against age-induced apoptosis in cerebellar granule cells. Soc. Neurosci. Abstr. 21, 1553.
    • (1995) Soc. Neurosci. Abstr. , vol.21 , pp. 1553
    • Chuang, D.-M.1    Leeds, P.2    Zhang, K.-G.3    Gao, X.-M.4    Ishitani, R.5
  • 7
    • 0025948399 scopus 로고
    • Identification of low molecular weight GTP-binding proteins and their sites of interaction in subcellular fractions from skeletal muscle
    • Doucet J.-P. and Tuana B. S. (1991) Identification of low molecular weight GTP-binding proteins and their sites of interaction in subcellular fractions from skeletal muscle. J. Biol. Chem. 266, 17613-17620.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17613-17620
    • Doucet, J.-P.1    Tuana, B.S.2
  • 9
    • 0026015948 scopus 로고
    • Expression and agonist-induced down-regulation of mRNAs of m2- And m3-muscarinic acetylcholine receptors in cultured cerebellar granule cells
    • Fukamauchi F., Hough C., and Chuang D.-M. (1991) Expression and agonist-induced down-regulation of mRNAs of m2- and m3-muscarinic acetylcholine receptors in cultured cerebellar granule cells. J. Neurochem. 56, 716-719.
    • (1991) J. Neurochem. , vol.56 , pp. 716-719
    • Fukamauchi, F.1    Hough, C.2    Chuang, D.-M.3
  • 10
    • 0026006943 scopus 로고
    • Identification, purification, and characterization of a calcium-dependent endonuclease (NUC18) from apoptotic rat thymocytes
    • Gaido M. L. and Cidlowski J. A. (1991) Identification, purification, and characterization of a calcium-dependent endonuclease (NUC18) from apoptotic rat thymocytes. J. Biol. Chem. 266, 18580-18585.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18580-18585
    • Gaido, M.L.1    Cidlowski, J.A.2
  • 11
    • 0023244774 scopus 로고
    • The role of depolarization in the survival and differentiation of cerebellar granule cells in culture
    • Gallo V., Kingsbury A., Balázs R., and Jørgensen O. S. (1987) The role of depolarization in the survival and differentiation of cerebellar granule cells in culture. J. Neurosci. 7, 2203-2213.
    • (1987) J. Neurosci. , vol.7 , pp. 2203-2213
    • Gallo, V.1    Kingsbury, A.2    Balázs, R.3    Jørgensen, O.S.4
  • 12
    • 0027971167 scopus 로고
    • Regulation of endothehal cell glyceraldehyde-3-phosphate dehydrogenase expression by hypoxia
    • Graven K. K., Troxler R. F., Kornfeld H., Panchenko M. V., and Farber H. W (1994) Regulation of endothehal cell glyceraldehyde-3-phosphate dehydrogenase expression by hypoxia. J. Biol. Chem. 269, 24446-24453.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24446-24453
    • Graven, K.K.1    Troxler, R.F.2    Kornfeld, H.3    Panchenko, M.V.4    Farber, H.W.5
  • 13
    • 0025204548 scopus 로고
    • Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death
    • Hockenbery D., Nuñez G., Milliman C., Schreiber R. D., and Korsmeyer S. J. (1990) Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death. Nature 348, 334-336.
    • (1990) Nature , vol.348 , pp. 334-336
    • Hockenbery, D.1    Nuñez, G.2    Milliman, C.3    Schreiber, R.D.4    Korsmeyer, S.J.5
  • 14
    • 0022359757 scopus 로고
    • Bundling of microtubules by glyceraldehyde-3-phosphate dehydrogenase and its modulation by ATP
    • Huitorel P and Pantaloni D. (1985) Bundling of microtubules by glyceraldehyde-3-phosphate dehydrogenase and its modulation by ATP. Eur. J. Biochem. 150, 265-269.
    • (1985) Eur. J. Biochem. , vol.150 , pp. 265-269
    • Huitorel, P.1    Pantaloni, D.2
  • 15
    • 5244229688 scopus 로고
    • Evidence that glyceraldehyde-3-phosphate dehydrogenase mediates age-induced apoptosis in mature cerebellar neurons in culture
    • Ishitani R., Sunaga K., Hirano A., Katsube N., Saunders P., and Chuang D.-M. (1995) Evidence that glyceraldehyde-3-phosphate dehydrogenase mediates age-induced apoptosis in mature cerebellar neurons in culture. Soc. Neurosci. Abstr. 21, 1554.
    • (1995) Soc. Neurosci. Abstr. , vol.21 , pp. 1554
    • Ishitani, R.1    Sunaga, K.2    Hirano, A.3    Katsube, N.4    Saunders, P.5    Chuang, D.-M.6
  • 16
    • 0025250111 scopus 로고
    • 3H-1,2-Benzodithiol-3-one 1,1-dioxide as an improved sulfurizing reagent in the solid-phase synthesis of oligodeoxyribonucleoside phosphorothioates
    • Iyer R. P., Egan W., Regan J. B., and Beaucage S. L. (1990) 3H-1,2-Benzodithiol-3-one 1,1-dioxide as an improved sulfurizing reagent in the solid-phase synthesis of oligodeoxyribonucleoside phosphorothioates. J. Am. Chem Soc. 112, 1253-1254.
    • (1990) J. Am. Chem Soc. , vol.112 , pp. 1253-1254
    • Iyer, R.P.1    Egan, W.2    Regan, J.B.3    Beaucage, S.L.4
  • 17
    • 0021925444 scopus 로고
    • An improved method to determine cell viability by simultaneous staining with fluorescein diacetate-propidium iodide
    • Jones K. H. and Senft J. A. (1985) An improved method to determine cell viability by simultaneous staining with fluorescein diacetate-propidium iodide. J. Histochem. Cytochem. 33, 77-79.
    • (1985) J. Histochem. Cytochem. , vol.33 , pp. 77-79
    • Jones, K.H.1    Senft, J.A.2
  • 18
    • 0022477471 scopus 로고
    • Autophosphorylation of glyceraldehydephosphate dehydrogenase and phosphorylation of protein from skeletal muscle microsomes
    • Kawamoto R. M. and Caswell A. H. (1986) Autophosphorylation of glyceraldehydephosphate dehydrogenase and phosphorylation of protein from skeletal muscle microsomes. Biochemistry 25, 656-661.
    • (1986) Biochemistry , vol.25 , pp. 656-661
    • Kawamoto, R.M.1    Caswell, A.H.2
  • 19
    • 5244293444 scopus 로고
    • Antisense oligodeoxynucleotide to glyceraldehyde-3-phosphate dehydrogenase (GAPDH) blocks age-induced apoptosis in cerebro-cortical neurons in culture
    • Kimura M., Chuang D.-M., and Ishitani R. (1995) Antisense oligodeoxynucleotide to glyceraldehyde-3-phosphate dehydrogenase (GAPDH) blocks age-induced apoptosis in cerebro-cortical neurons in culture. Soc. Neurosci. Abstr. 21, 1554.
    • (1995) Soc. Neurosci. Abstr. , vol.21 , pp. 1554
    • Kimura, M.1    Chuang, D.-M.2    Ishitani, R.3
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. (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.K.1
  • 21
    • 0028240526 scopus 로고
    • Programmed cell death: Implications for neuropsychiatric disorders
    • Margolis R. L., Chuang D.-M., and Post R. M. (1994) Programmed cell death: implications for neuropsychiatric disorders. Biol. Psychiatry 35, 946-956.
    • (1994) Biol. Psychiatry , vol.35 , pp. 946-956
    • Margolis, R.L.1    Chuang, D.-M.2    Post, R.M.3
  • 22
    • 0023851503 scopus 로고
    • Inhibitors of protein synthesis and RNA synthesis prevent neuronal death caused by nerve growth factor deprivation
    • Martin D. P., Schmidt R. E., DiStefano P. S., Lowry O. H., Carter J. G., and Johnson E M. Jr. (1988) Inhibitors of protein synthesis and RNA synthesis prevent neuronal death caused by nerve growth factor deprivation. J. Cell Biol. 106, 829-844.
    • (1988) J. Cell Biol. , vol.106 , pp. 829-844
    • Martin, D.P.1    Schmidt, R.E.2    Distefano, P.S.3    Lowry, O.H.4    Carter, J.G.5    Johnson Jr., E.M.6
  • 23
    • 0027264855 scopus 로고
    • Stimulation by nitric oxide of an NAD linkage to glyceraldehyde-3-phosphate dehydrogenase
    • McDonald L. J. and Moss J. (1993) Stimulation by nitric oxide of an NAD linkage to glyceraldehyde-3-phosphate dehydrogenase. Proc. Natl. Acad. Sci. USA 90, 6238-6241.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6238-6241
    • McDonald, L.J.1    Moss, J.2
  • 24
    • 0026070055 scopus 로고
    • A human nuclear uracil DNA glycosylase is the 37-kDa subunit of glyceraldehyde-3-phosphate dehydrogenase
    • Meyer-Siegler K., Mauro D. J., Seal G., Wurzer J., deRiel J. K., and Sirover M. A. (1991) A human nuclear uracil DNA glycosylase is the 37-kDa subunit of glyceraldehyde-3-phosphate dehydrogenase. Proc. Natl. Acad. Sci. USA 88, 8460-8464.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8460-8464
    • Meyer-Siegler, K.1    Mauro, D.J.2    Seal, G.3    Wurzer, J.4    DeRiel, J.K.5    Sirover, M.A.6
  • 25
    • 0022535636 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase is a nonhistone protein and a possible activator of transcription in neurons
    • Morgenegg G., Winkler G. C., Hübscher U., Heizmann C. W., Mous J., and Kuenzle C. C. (1986) Glyceraldehyde-3-phosphate dehydrogenase is a nonhistone protein and a possible activator of transcription in neurons. J. Neurochem. 47, 54-62.
    • (1986) J. Neurochem. , vol.47 , pp. 54-62
    • Morgenegg, G.1    Winkler, G.C.2    Hübscher, U.3    Heizmann, C.W.4    Mous, J.5    Kuenzle, C.C.6
  • 26
    • 0022516186 scopus 로고
    • The activation of inositol phospholipid metabolism as a signal-transducing system for excitatory amino acids in primary cultures of cerebellar granule cells
    • Nicoletti F., Wroblewski J. T., Novelli A., Alho H., Guidotti A., and Costa E. (1986) The activation of inositol phospholipid metabolism as a signal-transducing system for excitatory amino acids in primary cultures of cerebellar granule cells. J. Neurosci. 6, 1905-1911.
    • (1986) J. Neurosci. , vol.6 , pp. 1905-1911
    • Nicoletti, F.1    Wroblewski, J.T.2    Novelli, A.3    Alho, H.4    Guidotti, A.5    Costa, E.6
  • 27
    • 0026058318 scopus 로고
    • Cell death during development of the nervous system
    • Oppenheim R. W. (1991) Cell death during development of the nervous system. Annu. Rev. Neurosci. 14, 453-501.
    • (1991) Annu. Rev. Neurosci. , vol.14 , pp. 453-501
    • Oppenheim, R.W.1
  • 28
    • 0027373764 scopus 로고
    • Programmed cell death and the control of cell survival: Lessons from the nervous system
    • Raff M. C., Barres B. A., Burne J F., Coles H. S., Ishizaki Y., and Jacobson M. D. (1993) Programmed cell death and the control of cell survival: lessons from the nervous system. Science 262, 695-700.
    • (1993) Science , vol.262 , pp. 695-700
    • Raff, M.C.1    Barres, B.A.2    Burne, J.F.3    Coles, H.S.4    Ishizaki, Y.5    Jacobson, M.D.6
  • 29
    • 0024549766 scopus 로고
    • Association of glyceraldehyde-3-phosphate dehydrogenase with the plasma membrane of the intact human red blood cell
    • Rogalski A. A., Steck T. L., and Waseem A. (1989) Association of glyceraldehyde-3-phosphate dehydrogenase with the plasma membrane of the intact human red blood cell. J. Biol. Chem. 264, 6438-6446.
    • (1989) J. Biol. Chem. , vol.264 , pp. 6438-6446
    • Rogalski, A.A.1    Steck, T.L.2    Waseem, A.3
  • 30
    • 0028006683 scopus 로고
    • Putative synaptic vesicle nucleotide transporter identified as glyceraldehyde-3-phosphate dehydrogenase
    • Schlafer M., Volknandt W., and Zimmermann H. (1994) Putative synaptic vesicle nucleotide transporter identified as glyceraldehyde-3-phosphate dehydrogenase. J. Neurochem. 63, 1924-1931.
    • (1994) J. Neurochem. , vol.63 , pp. 1924-1931
    • Schlafer, M.1    Volknandt, W.2    Zimmermann, H.3
  • 31
    • 0025139268 scopus 로고
    • Serum and depolarizing agents cause acute neurotoxicity in cultured cerebellar granule cells: Role of the glutamate receptor responsive to N-methyl-D-aspartate
    • Schramm M , Eimerl S , and Costa E. (1990) Serum and depolarizing agents cause acute neurotoxicity in cultured cerebellar granule cells: role of the glutamate receptor responsive to N-methyl-D-aspartate. Proc. Natl. Acad. Sci. USA 87, 1193-1197.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1193-1197
    • Schramm, M.1    Eimerl, S.2    Costa, E.3
  • 32
    • 0027314334 scopus 로고
    • Rat brain glyceraldehyde-3-phosphate dehydrogenase interacts with the recombinant cytoplasmic domain of Alzheimer's β-amyloid precursor protein
    • Schulze H., Schuler A., Stüber D., Döbeli H., Langen H., and Huber G. (1993) Rat brain glyceraldehyde-3-phosphate dehydrogenase interacts with the recombinant cytoplasmic domain of Alzheimer's β-amyloid precursor protein. J. Neurochem. 60, 1915-1922.
    • (1993) J. Neurochem. , vol.60 , pp. 1915-1922
    • Schulze, H.1    Schuler, A.2    Stüber, D.3    Döbeli, H.4    Langen, H.5    Huber, G.6
  • 33
    • 0027518424 scopus 로고
    • Sequence-specific binding of transfer RNA by glyceraldehyde-3-phosphate dehydrogenase
    • Singh R. and Green M. R. (1993) Sequence-specific binding of transfer RNA by glyceraldehyde-3-phosphate dehydrogenase. Science 259, 365-368.
    • (1993) Science , vol.259 , pp. 365-368
    • Singh, R.1    Green, M.R.2
  • 34
    • 0027332622 scopus 로고
    • 2-, muscarinic acetylcholine receptor mRNA levels in differentiating cerebellar granule cells
    • 2-, muscarinic acetylcholine receptor mRNA levels in differentiating cerebellar granule cells. Neurosci. Lett. 163, 27-30.
    • (1993) Neurosci. Lett. , vol.163 , pp. 27-30
    • Sunaga, K.1    Chuang, D.-M.2    Ishitani, R.3
  • 37
    • 0028296553 scopus 로고
    • Synthesis of specific proteins in trophic factor-deprived neurons undergoing apoptosis
    • Villa P., Miehe M., Sensenbrenner M., and Pettmann B. (1994) Synthesis of specific proteins in trophic factor-deprived neurons undergoing apoptosis. J. Neurochem. 62, 1468-1475.
    • (1994) J. Neurochem. , vol.62 , pp. 1468-1475
    • Villa, P.1    Miehe, M.2    Sensenbrenner, M.3    Pettmann, B.4
  • 38
    • 0027172322 scopus 로고
    • Molecular regulation of apoptosis: Genetic controls on cell death
    • Williams G. T. and Smith C. A. (1993) Molecular regulation of apoptosis: genetic controls on cell death. Cell 74, 777-779.
    • (1993) Cell , vol.74 , pp. 777-779
    • Williams, G.T.1    Smith, C.A.2
  • 40
    • 0023909030 scopus 로고
    • Elimination of neurons from the rhesus monkey's lateral geniculate nucleus during development
    • Williams R. W. and Rakic P. (1988) Elimination of neurons from the rhesus monkey's lateral geniculate nucleus during development J. Comp. Neurol. 272, 424-436.
    • (1988) J. Comp. Neurol. , vol.272 , pp. 424-436
    • Williams, R.W.1    Rakic, P.2
  • 41
    • 0027495786 scopus 로고
    • In situ labeling of granule cells for apoptosis-associated DNA fragmentation reveals different mechanisms of cell loss in developing cerebellum
    • Wood K. A., Dipasquale B., and Youle R. J. (1993) In situ labeling of granule cells for apoptosis-associated DNA fragmentation reveals different mechanisms of cell loss in developing cerebellum. Neuron 11, 621-632.
    • (1993) Neuron , vol.11 , pp. 621-632
    • Wood, K.A.1    Dipasquale, B.2    Youle, R.J.3
  • 42
    • 0018830636 scopus 로고
    • Glucocorticoid-induced thymocyte apoptosis is associated with endogenous endonuclease activation
    • Wyllie A. H. (1980) Glucocorticoid-induced thymocyte apoptosis is associated with endogenous endonuclease activation. Nature 284, 555-556.
    • (1980) Nature , vol.284 , pp. 555-556
    • Wyllie, A.H.1
  • 43
    • 0026686667 scopus 로고
    • Nitric oxide stimulates auto-ADP-ribosylation of glyceraldehyde-3-phosphate dehydrogenase
    • Zhang J. and Snyder S H. (1992) Nitric oxide stimulates auto-ADP-ribosylation of glyceraldehyde-3-phosphate dehydrogenase. Proc. Natl. Acad. Sci. USA 89, 9382-9385.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9382-9385
    • Zhang, J.1    Snyder, S.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.