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Volumn 10, Issue 11, 2007, Pages 1407-1413

Mechanism suppressing glycogen synthesis in neurons and its demise in progressive myoclonus epilepsy

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; GLYCOGEN; GLYCOGEN SYNTHASE; LAFORIN; MALIN; PHOSPHOPROTEIN PHOSPHATASE 1; PROTEASOME; PROTEIN; UNCLASSIFIED DRUG;

EID: 35548995067     PISSN: 10976256     EISSN: None     Source Type: Journal    
DOI: 10.1038/nn1998     Document Type: Article
Times cited : (287)

References (46)
  • 1
    • 2042420664 scopus 로고    scopus 로고
    • Brain glycogen re-awakened
    • Brown, A.M. Brain glycogen re-awakened. J. Neurochem. 89, 537-552 (2004).
    • (2004) J. Neurochem , vol.89 , pp. 537-552
    • Brown, A.M.1
  • 2
    • 0032937953 scopus 로고    scopus 로고
    • Corpora-amylacea and the family of polyglucosan diseases
    • Cavanagh, J.B. Corpora-amylacea and the family of polyglucosan diseases. Brain Res. Brain Res. Rev. 29, 265-295 (1999).
    • (1999) Brain Res. Brain Res. Rev , vol.29 , pp. 265-295
    • Cavanagh, J.B.1
  • 3
    • 0023005321 scopus 로고
    • Progressive myoclonus epilepsies: Specific causes and diagnosis
    • Berkovic, S.F., Andermann, F., Carpenter, S. & Wolfe, L.S. Progressive myoclonus epilepsies: specific causes and diagnosis. N. Engl. J. Med. 315, 296-305 (1986).
    • (1986) N. Engl. J. Med , vol.315 , pp. 296-305
    • Berkovic, S.F.1    Andermann, F.2    Carpenter, S.3    Wolfe, L.S.4
  • 4
    • 0000665044 scopus 로고
    • Über das corkommen amyloider körperchen im innern der ganglienzellen; zugliech ein zum studium der amyloiden substanz im nervensystem.
    • Lafora, G.R. Über das corkommen amyloider körperchen im innern der ganglienzellen; zugliech ein zum studium der amyloiden substanz im nervensystem. Virchows Arch. Pathol. Anat. 205, 294-303 (1911).
    • (1911) Virchows Arch. Pathol. Anat , vol.205 , pp. 294-303
    • Lafora, G.R.1
  • 5
    • 51849175000 scopus 로고
    • Beitrag zur histogpathologie der myoklonischen epilepsie.
    • Lafora, G.R. & Glueck, B. Beitrag zur histogpathologie der myoklonischen epilepsie. Z. Gesamte Neurol. Psychiatr. 6, 1-14 (1911).
    • (1911) Z. Gesamte Neurol. Psychiatr , vol.6 , pp. 1-14
    • Lafora, G.R.1    Glueck, B.2
  • 6
    • 0014333534 scopus 로고
    • Myoclonus epilepsy with Lafora bodies. An ultrastructural and cytochemical study
    • Collins, G.H., Cowden, R.R. & Nevis, A.H. Myoclonus epilepsy with Lafora bodies. An ultrastructural and cytochemical study. Arch. Pathol. 86, 239-254 (1968).
    • (1968) Arch. Pathol , vol.86 , pp. 239-254
    • Collins, G.H.1    Cowden, R.R.2    Nevis, A.H.3
  • 7
    • 0014739101 scopus 로고
    • Studies in myoclonus epilepsy (Lafora body form). II. Polyglucosans in the systemic deposits of myoclonus epilepsy and in corpora amylacea
    • Sakai, M., Austin, J., Witmer, F. & Trueb, L. Studies in myoclonus epilepsy (Lafora body form). II. Polyglucosans in the systemic deposits of myoclonus epilepsy and in corpora amylacea. Neurology 20, 160-176 (1970).
    • (1970) Neurology , vol.20 , pp. 160-176
    • Sakai, M.1    Austin, J.2    Witmer, F.3    Trueb, L.4
  • 8
    • 0028944639 scopus 로고
    • Familial progressive myoclonus epilepsy: Clinical and electrophysiologic observations
    • Acharya, J.N., Satishchandra, P. & Shankar, S.K. Familial progressive myoclonus epilepsy: clinical and electrophysiologic observations. Epilepsia 36, 429-434 (1995).
    • (1995) Epilepsia , vol.36 , pp. 429-434
    • Acharya, J.N.1    Satishchandra, P.2    Shankar, S.K.3
  • 9
    • 0027314930 scopus 로고
    • Progressive myoclonus epilepsies: Clinical and genetic aspects
    • Berkovic, S.F., Cochius, J., Andermann, E. & Andermann, F. Progressive myoclonus epilepsies: clinical and genetic aspects. Epilepsia 34 (Suppl 3): S19-S30 (1993).
    • (1993) Epilepsia , vol.34 , Issue.SUPPL. 3
    • Berkovic, S.F.1    Cochius, J.2    Andermann, E.3    Andermann, F.4
  • 10
    • 0025209930 scopus 로고
    • Longitudinal clinicoelectrophysiologic study of a case of Lafora disease proven by skin biopsy
    • Kobayashi, K., Iyoda, K., Ohtsuka, Y., Ohtahara, S. & Yamada, M. Longitudinal clinicoelectrophysiologic study of a case of Lafora disease proven by skin biopsy. Epilepsia 31, 194-201 (1990).
    • (1990) Epilepsia , vol.31 , pp. 194-201
    • Kobayashi, K.1    Iyoda, K.2    Ohtsuka, Y.3    Ohtahara, S.4    Yamada, M.5
  • 11
    • 0034907260 scopus 로고    scopus 로고
    • Lafora's disease: Towards a clinical, pathologic andmolecular synthesis
    • Minassian, B.A. Lafora's disease: towards a clinical, pathologic andmolecular synthesis. Pediatr. Neurol. 25, 21-29 (2001).
    • (2001) Pediatr. Neurol , vol.25 , pp. 21-29
    • Minassian, B.A.1
  • 12
    • 15044357259 scopus 로고    scopus 로고
    • Progressive myoclonic epilepsies: A review of genetic and therapeutic aspects
    • Shahwan, A., Farrell, M. & Delanty, N. Progressive myoclonic epilepsies: a review of genetic and therapeutic aspects. Lancet Neurol. 4, 239-248 (2005).
    • (2005) Lancet Neurol , vol.4 , pp. 239-248
    • Shahwan, A.1    Farrell, M.2    Delanty, N.3
  • 13
    • 0001617608 scopus 로고
    • Lafora disease, a form of progressive myoclonues epilepsy
    • Van Heycop Ten Ham, M.W. Lafora disease, a form of progressive myoclonues epilepsy. Handb. Clin. Neurol. 15, 382-422 (1974).
    • (1974) Handb. Clin. Neurol , vol.15 , pp. 382-422
    • Van Heycop Ten Ham, M.W.1
  • 14
    • 17344362307 scopus 로고    scopus 로고
    • Mutations in a gene encoding a novel protein tyrosine phosphatase cause progressive myoclonus epilepsy
    • Minassian, B.A. et al. Mutations in a gene encoding a novel protein tyrosine phosphatase cause progressive myoclonus epilepsy. Nat. Genet. 20, 171-174 (1998).
    • (1998) Nat. Genet , vol.20 , pp. 171-174
    • Minassian, B.A.1
  • 15
    • 0033842001 scopus 로고    scopus 로고
    • Mutation spectrum and predicted function of laforin in Lafora's progressive myoclonus epilepsy
    • Minassian, B.A. et al. Mutation spectrum and predicted function of laforin in Lafora's progressive myoclonus epilepsy. Neurology 55, 341-346 (2000).
    • (2000) Neurology , vol.55 , pp. 341-346
    • Minassian, B.A.1
  • 16
    • 0344359726 scopus 로고    scopus 로고
    • A novel protein tyrosine phosphatase gene is mutated in progressive myoclonus epilepsy of the Lafora type (EPM2)
    • Serratosa, J.M. et al. A novel protein tyrosine phosphatase gene is mutated in progressive myoclonus epilepsy of the Lafora type (EPM2). Hum. Mol. Genet. 8, 345-352 (1999).
    • (1999) Hum. Mol. Genet , vol.8 , pp. 345-352
    • Serratosa, J.M.1
  • 17
    • 0037169553 scopus 로고    scopus 로고
    • A unique carbohydrate binding domain targets the lafora disease phosphatase to glycogen
    • Wang, J., Stuckey, J.A., Wishart, M.J. & Dixon, J.E. A unique carbohydrate binding domain targets the lafora disease phosphatase to glycogen. J. Biol. Chem. 277, 2377-2380 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 2377-2380
    • Wang, J.1    Stuckey, J.A.2    Wishart, M.J.3    Dixon, J.E.4
  • 18
    • 31544471203 scopus 로고    scopus 로고
    • Recent advances in the molecular basis of Lafora's progressive myoclonus epilepsy
    • Ganesh, S., Puri, R., Singh, S., Mittal, S. & Dubey, D. Recent advances in the molecular basis of Lafora's progressive myoclonus epilepsy. J. Hum. Genet. 51, 1-8 (2006).
    • (2006) J. Hum. Genet , vol.51 , pp. 1-8
    • Ganesh, S.1    Puri, R.2    Singh, S.3    Mittal, S.4    Dubey, D.5
  • 19
    • 0141618459 scopus 로고    scopus 로고
    • Mutations in NHLRC1 cause progressive myoclonus epilepsy
    • Chan, E.M. et al. Mutations in NHLRC1 cause progressive myoclonus epilepsy. Nat. Genet. 35, 125-127 (2003).
    • (2003) Nat. Genet , vol.35 , pp. 125-127
    • Chan, E.M.1
  • 20
    • 20844463813 scopus 로고    scopus 로고
    • Insights into Lafora disease: Malin is an E3 ubiquitin ligase that ubiquitinates and promotes the degradation of laforin
    • Gentry, M.S., Worby, C.A. & Dixon, J.E. Insights into Lafora disease: malin is an E3 ubiquitin ligase that ubiquitinates and promotes the degradation of laforin. Proc. Natl. Acad. Sci. USA 102, 8501-8506 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 8501-8506
    • Gentry, M.S.1    Worby, C.A.2    Dixon, J.E.3
  • 21
    • 0038199736 scopus 로고    scopus 로고
    • Control of glycogen deposition
    • Ferrer, J.C. et al. Control of glycogen deposition. FEBS Lett. 546, 127-132 (2003).
    • (2003) FEBS Lett , vol.546 , pp. 127-132
    • Ferrer, J.C.1
  • 22
    • 0037189486 scopus 로고    scopus 로고
    • Liver glycogen synthase but not the muscle isoform differentiates between glucose 6-phosphate produced by glucokinase or hexokinase
    • Gomis, R.R., Cid, E., Garcia-Rocha, M., Ferrer, J.C. & Guinovart, J.J. Liver glycogen synthase but not the muscle isoform differentiates between glucose 6-phosphate produced by glucokinase or hexokinase. J. Biol. Chem. 277, 23246-23252 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 23246-23252
    • Gomis, R.R.1    Cid, E.2    Garcia-Rocha, M.3    Ferrer, J.C.4    Guinovart, J.J.5
  • 23
    • 0033921912 scopus 로고    scopus 로고
    • Glycogen synthase sensitivity to insulin and glucose-6-phosphate is mediated by both NH2- and COOH-terminal phosphorylation sites
    • Skurat, A.V., Dietrich, A.D. & Roach, P.J. Glycogen synthase sensitivity to insulin and glucose-6-phosphate is mediated by both NH2- and COOH-terminal phosphorylation sites. Diabetes 49, 1096-1100 (2000).
    • (2000) Diabetes , vol.49 , pp. 1096-1100
    • Skurat, A.V.1    Dietrich, A.D.2    Roach, P.J.3
  • 24
    • 0030853642 scopus 로고    scopus 로고
    • Muscle glycogen synthase translocates from the cell nucleus to the cystosol in response to glucose
    • Ferrer, J.C., Baque, S. & Guinovart, J.J. Muscle glycogen synthase translocates from the cell nucleus to the cystosol in response to glucose. FEBS Lett. 415, 249-252 (1997).
    • (1997) FEBS Lett , vol.415 , pp. 249-252
    • Ferrer, J.C.1    Baque, S.2    Guinovart, J.J.3
  • 25
    • 21344433617 scopus 로고    scopus 로고
    • Determinants of the nucleocytoplasmic shuttling of muscle glycogen synthase
    • Cid, E., Cifuentes, D., Baque, S., Ferrer, J.C. & Guinovart, J.J. Determinants of the nucleocytoplasmic shuttling of muscle glycogen synthase. FEBS J. 272, 3197-3213 (2005).
    • (2005) FEBS J , vol.272 , pp. 3197-3213
    • Cid, E.1    Cifuentes, D.2    Baque, S.3    Ferrer, J.C.4    Guinovart, J.J.5
  • 26
    • 0028072751 scopus 로고
    • Rabbit skeletalmuscle glycogen synthase expressed in COS cells. Identification of regulatory phosphorylation sites
    • Skurat, A.V., Wang, Y. & Roach, P.J. Rabbit skeletalmuscle glycogen synthase expressed in COS cells. Identification of regulatory phosphorylation sites. J. Biol. Chem. 269, 25534-25542 (1994).
    • (1994) J. Biol. Chem , vol.269 , pp. 25534-25542
    • Skurat, A.V.1    Wang, Y.2    Roach, P.J.3
  • 27
    • 0141558915 scopus 로고    scopus 로고
    • Use of lithium and SB-415286 to explore the role of glycogen synthase kinase-3 in the regulation of glucose transport and glycogen synthase
    • MacAulay, K. et al. Use of lithium and SB-415286 to explore the role of glycogen synthase kinase-3 in the regulation of glucose transport and glycogen synthase. Eur. J. Biochem. 270, 3829-3838 (2003).
    • (2003) Eur. J. Biochem , vol.270 , pp. 3829-3838
    • MacAulay, K.1
  • 28
    • 0030614364 scopus 로고    scopus 로고
    • PTG, a protein phosphatase 1-binding protein with a role in glycogen metabolism
    • Printen, J.A., Brady, M.J. & Saltiel, A.R. PTG, a protein phosphatase 1-binding protein with a role in glycogen metabolism. Science 275, 1475-1478 (1997).
    • (1997) Science , vol.275 , pp. 1475-1478
    • Printen, J.A.1    Brady, M.J.2    Saltiel, A.R.3
  • 29
    • 0034634568 scopus 로고    scopus 로고
    • Identification of binding sites on protein targeting to glycogen for enzymes of glycogen metabolism
    • Fong, N.M. et al. Identification of binding sites on protein targeting to glycogen for enzymes of glycogen metabolism. J. Biol. Chem. 275, 35034-35039 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 35034-35039
    • Fong, N.M.1
  • 30
    • 0032500691 scopus 로고    scopus 로고
    • Overexpression of protein targeting to glycogen (PTG) in rat hepatocytes causes profound activation of glycogen synthesis independent of normal hormone- and substrate-mediated regulatory mechanisms
    • Berman, H.K., O'Doherty, R.M., Anderson, P. & Newgard, C.B. Overexpression of protein targeting to glycogen (PTG) in rat hepatocytes causes profound activation of glycogen synthesis independent of normal hormone- and substrate-mediated regulatory mechanisms. J. Biol. Chem. 273, 26421-26425 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 26421-26425
    • Berman, H.K.1    O'Doherty, R.M.2    Anderson, P.3    Newgard, C.B.4
  • 31
    • 17644444332 scopus 로고    scopus 로고
    • Laforin, the dual-phosphatase responsible for Lafora disease, interacts with R5 (PTG), a regulatory subunit of protein phosphatase 1 that enhances glycogen accumulation
    • Fernandez-Sanchez, M.E. et al. Laforin, the dual-phosphatase responsible for Lafora disease, interacts with R5 (PTG), a regulatory subunit of protein phosphatase 1 that enhances glycogen accumulation. Hum. Mol. Genet. 12, 3161-3171 (2003).
    • (2003) Hum. Mol. Genet , vol.12 , pp. 3161-3171
    • Fernandez-Sanchez, M.E.1
  • 32
    • 0034038905 scopus 로고    scopus 로고
    • Protein targeting to glycogen mRNA expression is stimulated by noradrenaline in mouse cortical astrocytes
    • Allaman, I., Pellerin, L. & Magistretti, P.J. Protein targeting to glycogen mRNA expression is stimulated by noradrenaline in mouse cortical astrocytes. Glia 30, 382-391 (2000).
    • (2000) Glia , vol.30 , pp. 382-391
    • Allaman, I.1    Pellerin, L.2    Magistretti, P.J.3
  • 33
    • 35548963842 scopus 로고
    • On the nature of rabbit liver glycogen. II. Iodine absorption spectrum
    • Schlamowitz, M. On the nature of rabbit liver glycogen. II. Iodine absorption spectrum. J. Biol. Chem. 190, 519-527 (1951).
    • (1951) J. Biol. Chem , vol.190 , pp. 519-527
    • Schlamowitz, M.1
  • 34
    • 0032189348 scopus 로고    scopus 로고
    • Proteasome inhibitors: Valuable new tools for cell biologists
    • Lee, D.H. & Goldberg, A.L. Proteasome inhibitors: valuable new tools for cell biologists. Trends Cell Biol. 8, 397-403 (1998).
    • (1998) Trends Cell Biol , vol.8 , pp. 397-403
    • Lee, D.H.1    Goldberg, A.L.2
  • 35
    • 0030997893 scopus 로고    scopus 로고
    • The role of glucose-6-phosphate in the control of glycogen synthase
    • Villar-Palasi, C. & Guinovart, J.J. The role of glucose-6-phosphate in the control of glycogen synthase. FASEB J. 11, 544-558 (1997).
    • (1997) FASEB J , vol.11 , pp. 544-558
    • Villar-Palasi, C.1    Guinovart, J.J.2
  • 36
    • 33846026714 scopus 로고    scopus 로고
    • Reelin induces the detachment of postnatal subventricular zone cells and the expression of the Egr-1 through Erk1/2 activation
    • Simo, S. et al. Reelin induces the detachment of postnatal subventricular zone cells and the expression of the Egr-1 through Erk1/2 activation. Cereb. Cortex 17, 294-303 (2007).
    • (2007) Cereb. Cortex , vol.17 , pp. 294-303
    • Simo, S.1
  • 37
    • 0029796293 scopus 로고    scopus 로고
    • Glucose-6-phosphate produced by glucokinase, but not hexokinase I, promotes the activation of hepatic glycogen synthase
    • Seoane, J. et al. Glucose-6-phosphate produced by glucokinase, but not hexokinase I, promotes the activation of hepatic glycogen synthase. J. Biol. Chem. 271, 23756-23760 (1996).
    • (1996) J. Biol. Chem , vol.271 , pp. 23756-23760
    • Seoane, J.1
  • 38
    • 0028690027 scopus 로고
    • Use of recombinant adenovirus for metabolic engineering of mammalian cells
    • Becker, T.C. et al. Use of recombinant adenovirus for metabolic engineering of mammalian cells. Methods Cell Biol. 43 (Pt A): 161-189 (1994).
    • (1994) Methods Cell Biol , vol.43 , Issue.PART A , pp. 161-189
    • Becker, T.C.1
  • 39
    • 0023883716 scopus 로고
    • A simple technique for the rescue of early region I mutations into infectious human adenovirus type 5
    • McGrory, W.J., Bautista, D.S. & Graham, F.L. A simple technique for the rescue of early region I mutations into infectious human adenovirus type 5. Virology 163, 614-617 (1988).
    • (1988) Virology , vol.163 , pp. 614-617
    • McGrory, W.J.1    Bautista, D.S.2    Graham, F.L.3
  • 40
    • 0038321327 scopus 로고    scopus 로고
    • Increased phosphorylation of skeletal muscle glycogen synthase at NH2-terminal sites during physiological hyperinsulinemia in type 2 diabetes
    • Hojlund, K. et al. Increased phosphorylation of skeletal muscle glycogen synthase at NH2-terminal sites during physiological hyperinsulinemia in type 2 diabetes. Diabetes 52, 1393-1402 (2003).
    • (2003) Diabetes , vol.52 , pp. 1393-1402
    • Hojlund, K.1
  • 41
    • 0027619327 scopus 로고
    • Production of monoclonal antibody that recognizes glycogen and its application for immunohistochemistry.]
    • Baba, O. [Production of monoclonal antibody that recognizes glycogen and its application for immunohistochemistry.]. Kokubyo Gakkai Zasshi. 60, 264-287 (1993).
    • (1993) Kokubyo Gakkai Zasshi , vol.60 , pp. 264-287
    • Baba, O.1
  • 42
    • 0017159024 scopus 로고
    • A rapid method for the determination of glycogen content and radioactivity in small quantities of tissue or isolated hepatocytes
    • Chan, T.M. & Exton, J.H. A rapid method for the determination of glycogen content and radioactivity in small quantities of tissue or isolated hepatocytes. Anal. Biochem. 71, 96-105 (1976).
    • (1976) Anal. Biochem , vol.71 , pp. 96-105
    • Chan, T.M.1    Exton, J.H.2
  • 43
    • 0001010238 scopus 로고
    • D-glucose-6-phosphate and D-Fructose-6-phosphate
    • ed. Bergmeyer, H. U, Academic Press, New York
    • Lang, G. & Michal, G. D-glucose-6-phosphate and D-Fructose-6-phosphate. in Methods of Enzymatic Analysis (ed. Bergmeyer, H. U.) 1238-1242 (Academic Press, New York, 1974).
    • (1974) Methods of Enzymatic Analysis , pp. 1238-1242
    • Lang, G.1    Michal, G.2
  • 44
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254 (1976).
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 45
    • 0014428937 scopus 로고
    • A rapid filter paper assay for UDPglucose-glycogen glucosyltransferase, including an improved biosynthesis of UDP-14C-glucose
    • Thomas, J.A., Schlender, K.K. & Larner, J. A rapid filter paper assay for UDPglucose-glycogen glucosyltransferase, including an improved biosynthesis of UDP-14C-glucose. Anal. Biochem. 25, 486-499 (1968).
    • (1968) Anal. Biochem , vol.25 , pp. 486-499
    • Thomas, J.A.1    Schlender, K.K.2    Larner, J.3
  • 46
    • 0018636503 scopus 로고
    • Glycogen synthase: A new activity ratio assay expressing a high sensitivity to the phosphorylation state
    • Guinovart, J.J. et al. Glycogen synthase: a new activity ratio assay expressing a high sensitivity to the phosphorylation state. FEBS Lett. 106, 284-288 (1979).
    • (1979) FEBS Lett , vol.106 , pp. 284-288
    • Guinovart, J.J.1


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