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Volumn 21, Issue 7, 2012, Pages 1521-1533

Lafora bodies and neurological defects in malin-deficient mice correlate with impaired autophagy

(19)  Criado, Olga a,h   Aguado, Carmen b,h   Gayarre, Javier a,h   Duran Trio, Lara a,c,h   Garcia Cabrero, Ana M d,h   Vernia, Santiago e,h   San Millán, Beatriz f   Heredia, Miguel e,h   Romá Mateo, Carlos e,h   Mouron, Silvana a,h   Juana López, Lucía a,h   Domínguez, Mercedes g   Navarro, Carmen f,h   Serratosa, Jose M d,h   Sanchez, Marina d,h   Sanz, Pascual e,h   Bovolenta, Paola c,h   Knecht, Erwin b,h   de Cordoba, Santiago Rodriguez a,h  


Author keywords

[No Author keywords available]

Indexed keywords

LAFORIN; MALIN; PROTEIN; UNCLASSIFIED DRUG;

EID: 84858183902     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddr590     Document Type: Article
Times cited : (118)

References (50)
  • 1
    • 0004452545 scopus 로고
    • Progressive familial myoclonic epilepsy in three families: its clinical features and pathological basis
    • Harriman, D.G.F., Millar, J.H.D. and Stevenson, A.C. (1955) Progressive familial myoclonic epilepsy in three families: its clinical features and pathological basis. Brain, 78, 325-349.
    • (1955) Brain , vol.78 , pp. 325-349
    • Harriman, D.G.F.1    Millar, J.H.D.2    Stevenson, A.C.3
  • 2
    • 0014306984 scopus 로고
    • Studies in myoclonus epilepsy (Lafora body form) I. Isolation and preliminary characterization of lafora bodies in two cases
    • Yokoi, S., Austin, J., Witmer, F. and Sakai, M. (1968) Studies in myoclonus epilepsy (Lafora body form) I. Isolation and preliminary characterization of lafora bodies in two cases. Arch. Neurol., 19, 15-33.
    • (1968) Arch. Neurol. , vol.19 , pp. 15-33
    • Yokoi, S.1    Austin, J.2    Witmer, F.3    Sakai, M.4
  • 3
    • 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. and Trueb, L. (1970) 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) Neurology , vol.20 , pp. 160-176
    • Sakai, M.1    Austin, J.2    Witmer, F.3    Trueb, L.4
  • 4
    • 51849175000 scopus 로고
    • Beitrag zur Histopathologie der myoklonischen Epilepsie
    • Lafora, G.R. and Glueck, B. (1911) Beitrag zur Histopathologie der myoklonischen Epilepsie. Z. Gesamte Neurol. Psychatr., 6, 1-14.
    • (1911) Z. Gesamte Neurol. Psychatr. , vol.6 , pp. 1-14
    • Lafora, G.R.1    Glueck, B.2
  • 5
    • 0001970565 scopus 로고
    • The presence of amyloid bodies in the protoplasm of the ganglion cells: a contribution to the study of the amyloid substance in the nervous system
    • Lafora, G.R. (1911) The presence of amyloid bodies in the protoplasm of the ganglion cells: a contribution to the study of the amyloid substance in the nervous system. Bull. Gov. Hosp. Insane, 3, 83-92.
    • (1911) Bull. Gov. Hosp. Insane , vol.3 , pp. 83-92
    • Lafora, G.R.1
  • 6
    • 0023005321 scopus 로고
    • Progressive myoclonus epilepsies: specific causes and diagnosis
    • Berkovic, S.F., Andermann, F., Carpenter, S. and Wolfe, L.S. (1986) Progressive myoclonus epilepsies: specific causes and diagnosis. N. Engl. J. Med., 315, 296-305.
    • (1986) N. Engl. J. Med. , vol.315 , pp. 296-305
    • Berkovic, S.F.1    Andermann, F.2    Carpenter, S.3    Wolfe, L.S.4
  • 9
    • 2942737274 scopus 로고    scopus 로고
    • Laforin preferentially binds the neurotoxic starch-like polyglucosans, which form in its absence in progressive myoclonus epilepsy
    • Chan, E.M., Ackerley, C.A., Lohi, H., Ianzano, L., Cortez, M.A., Shannon, P., Scherer, S.W. and Minassian, B.A. (2004) Laforin preferentially binds the neurotoxic starch-like polyglucosans, which form in its absence in progressive myoclonus epilepsy. Hum. Mol. Genet., 13, 1117-1129.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1117-1129
    • Chan, E.M.1    Ackerley, C.A.2    Lohi, H.3    Ianzano, L.4    Cortez, M.A.5    Shannon, P.6    Scherer, S.W.7    Minassian, B.A.8
  • 11
    • 0037169553 scopus 로고    scopus 로고
    • A unique carbohydrate binding domain targets the Lafora disease phosphatase to glycogen
    • Wang, J., Stucket, J.A., Wishart, M.J. and Dixon, J.E. (2002) A unique carbohydrate binding domain targets the Lafora disease phosphatase to glycogen. J. Biol. Chem., 277, 2377-2380.
    • (2002) J. Biol. Chem. , vol.277 , pp. 2377-2380
    • Wang, J.1    Stucket, J.A.2    Wishart, M.J.3    Dixon, J.E.4
  • 13
    • 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. and Dixon, J.E. (2005) 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) Proc. Natl Acad. Sci. USA , vol.102 , pp. 8501-8506
    • Gentry, M.S.1    Worby, C.A.2    Dixon, J.E.3
  • 16
    • 57249096594 scopus 로고    scopus 로고
    • Advances in genetics of juvenile myoclonic epilepsies
    • Delgado-Escueta, A. (2007) Advances in genetics of juvenile myoclonic epilepsies. Epilepsy Curr., 7, 61-67.
    • (2007) Epilepsy Curr. , vol.7 , pp. 61-67
    • Delgado-Escueta, A.1
  • 17
    • 3543124150 scopus 로고    scopus 로고
    • Progressive myoclonus epilepsy with polyglucosans (Lafora disease): evidence for a third locus
    • Chan, E.M., Omer, S., Ahmed, M., Bridges, L.R., Bennett, C., Scherer, S.W. and Minassian, B.A. (2004) Progressive myoclonus epilepsy with polyglucosans (Lafora disease): evidence for a third locus. Neurology, 63, 565-567.
    • (2004) Neurology , vol.63 , pp. 565-567
    • Chan, E.M.1    Omer, S.2    Ahmed, M.3    Bridges, L.R.4    Bennett, C.5    Scherer, S.W.6    Minassian, B.A.7
  • 18
    • 66749165935 scopus 로고    scopus 로고
    • Lafora progressive myoclonus epilepsy: a meta-analysis of reported mutations in the first decade following the discovery of the EPM2A and NHLRC1 genes
    • Singh, S. and Ganesh, S. (2009) Lafora progressive myoclonus epilepsy: a meta-analysis of reported mutations in the first decade following the discovery of the EPM2A and NHLRC1 genes. Hum. Mutat., 30, 715-723.
    • (2009) Hum. Mutat. , vol.30 , pp. 715-723
    • Singh, S.1    Ganesh, S.2
  • 22
    • 34948889895 scopus 로고    scopus 로고
    • A role for AGL ubiquitination in the glycogen storage disorders of Lafora and Corís disease
    • Cheng, A., Zhang, M., Gentry, M.S., Worby, C.A., Dixon, J.E. and Saltiel, A.R. (2007) A role for AGL ubiquitination in the glycogen storage disorders of Lafora and Corís disease. Genes Dev., 21, 2399-2409.
    • (2007) Genes Dev. , vol.21 , pp. 2399-2409
    • Cheng, A.1    Zhang, M.2    Gentry, M.S.3    Worby, C.A.4    Dixon, J.E.5    Saltiel, A.R.6
  • 23
    • 42949086604 scopus 로고    scopus 로고
    • Malin decreases glycogen accumulation by promoting the degradation of protein targeting to glycogen (PTG)
    • Worby, C.A., Gentry, M.S. and Dixon, J.E. (2008) Malin decreases glycogen accumulation by promoting the degradation of protein targeting to glycogen (PTG). J. Biol. Chem., 283, 4069-4076.
    • (2008) J. Biol. Chem. , vol.283 , pp. 4069-4076
    • Worby, C.A.1    Gentry, M.S.2    Dixon, J.E.3
  • 25
    • 33749620777 scopus 로고    scopus 로고
    • Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates
    • Worby, C.A., Gentry, M. and Dixon, J.E. (2006) Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates. J. Biol. Chem., 281, 30412-30418.
    • (2006) J. Biol. Chem. , vol.281 , pp. 30412-30418
    • Worby, C.A.1    Gentry, M.2    Dixon, J.E.3
  • 28
    • 34547559799 scopus 로고    scopus 로고
    • The phosphatase laforin crosses evolutionary boundaries and links carbohydrate metabolism to neuronal disease
    • Gentry, M.S., Dowen, R.H., Worby, C.A., Mattoo, S., Ecker, J.R. and Dixon, J.E. (2007) The phosphatase laforin crosses evolutionary boundaries and links carbohydrate metabolism to neuronal disease. J. Cell Biol., 178, 477-488.
    • (2007) J. Cell Biol. , vol.178 , pp. 477-488
    • Gentry, M.S.1    Dowen, R.H.2    Worby, C.A.3    Mattoo, S.4    Ecker, J.R.5    Dixon, J.E.6
  • 29
    • 18444405220 scopus 로고    scopus 로고
    • Targeted disruption of the Epm2a gene causes formation of Lafora inclusion bodies, neurodegeneration, ataxia, myoclonus epilepsy and impaired behavioral response in mice
    • Ganesh, S., Delgado-Escueta, A.V., Sakamoto, T., Avila, M.R., Machado-Salas, J., Hoshii, Y., Akagi, T., Gomi, H., Suzuki, T., Amano, K. et al. (2002) Targeted disruption of the Epm2a gene causes formation of Lafora inclusion bodies, neurodegeneration, ataxia, myoclonus epilepsy and impaired behavioral response in mice. Hum. Mol. Genet., 11, 1251-1262.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1251-1262
    • Ganesh, S.1    Delgado-Escueta, A.V.2    Sakamoto, T.3    Avila, M.R.4    Machado-Salas, J.5    Hoshii, Y.6    Akagi, T.7    Gomi, H.8    Suzuki, T.9    Amano, K.10
  • 31
    • 78649240333 scopus 로고    scopus 로고
    • Laforin in autophagy: a possible link between carbohydrate and protein in Lafora disease?
    • Puri, R. and Ganesh, S. (2010) Laforin in autophagy: a possible link between carbohydrate and protein in Lafora disease? Autophagy, 6, 1229-1231.
    • (2010) Autophagy , vol.6 , pp. 1229-1231
    • Puri, R.1    Ganesh, S.2
  • 32
    • 84858171357 scopus 로고    scopus 로고
    • Dysfunctions in endosomal-lysosomal and autophagy pathways underlie neuropathology in a mouse model for Lafora disease
    • Epub ahead of print
    • Puri, R., Suzuki, T., Yamakawa, K. and Ganesh, S. (2011) Dysfunctions in endosomal-lysosomal and autophagy pathways underlie neuropathology in a mouse model for Lafora disease. Hum. Mol. Genet., Epub ahead of print.
    • (2011) Hum. Mol. Genet.
    • Puri, R.1    Suzuki, T.2    Yamakawa, K.3    Ganesh, S.4
  • 34
    • 67650110001 scopus 로고    scopus 로고
    • Increased endoplasmic reticulum stress and decreased proteasomal function in Lafora disease models lacking the phosphatase laforin
    • Vernia, S., Rubio, T., Heredia, M., Rodríguez de Córdoba, S. and Sanz, P. (2009) Increased endoplasmic reticulum stress and decreased proteasomal function in Lafora disease models lacking the phosphatase laforin. PLoS ONE, 4, e5907.
    • (2009) PLoS ONE , vol.4
    • Vernia, S.1    Rubio, T.2    Heredia, M.3    Rodríguez de Córdoba, S.4    Sanz, P.5
  • 36
    • 77955486949 scopus 로고    scopus 로고
    • Genetic depletion of the malin E3 ubiquitin ligase in mice leads to Lafora bodies and the accumulation of insoluble laforin
    • DePaoli-Roach, A.A., Tagliabracci, V.S., Segvich, D.M., Meyer, C.M., Irimia, J.M. and Roach, P.J. (2010) Genetic depletion of the malin E3 ubiquitin ligase in mice leads to Lafora bodies and the accumulation of insoluble laforin. J. Biol. Chem., 285, 25372-25381.
    • (2010) J. Biol. Chem. , vol.285 , pp. 25372-25381
    • DePaoli-Roach, A.A.1    Tagliabracci, V.S.2    Segvich, D.M.3    Meyer, C.M.4    Irimia, J.M.5    Roach, P.J.6
  • 38
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito, R.R. (2000) Aggresomes, inclusion bodies and protein aggregation. Trends Cell. Biol., 10, 524-530.
    • (2000) Trends Cell. Biol. , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 41
    • 68149112275 scopus 로고    scopus 로고
    • Insulin and the brain
    • Laron, Z. (2009) Insulin and the brain. Arch. Physiol. Biochem., 115, 112-116.
    • (2009) Arch. Physiol. Biochem. , vol.115 , pp. 112-116
    • Laron, Z.1
  • 42
    • 68949120737 scopus 로고    scopus 로고
    • Control of energy homeostasis by insulin and leptin: targeting the arcuate nucleus and beyond
    • Könner, A.C., Klöckener, T. and Brüning, J.C. (2009) Control of energy homeostasis by insulin and leptin: targeting the arcuate nucleus and beyond. Physiol. Behav., 97, 632-638.
    • (2009) Physiol. Behav. , vol.97 , pp. 632-638
    • Könner, A.C.1    Klöckener, T.2    Brüning, J.C.3
  • 43
    • 78149272475 scopus 로고    scopus 로고
    • Sequestration of chaperones and proteasome into Lafora bodies and proteasomal dysfunction induced by Lafora disease-associated mutations of malin
    • Rao, S.N.R., Maity, R., Sharma, J., Dey, P., Shankar, S.K., Satishchandra, P. and Jana, N.R. (2010) Sequestration of chaperones and proteasome into Lafora bodies and proteasomal dysfunction induced by Lafora disease-associated mutations of malin. Hum. Mol. Genet., 19, 4726-4734.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 4726-4734
    • Rao, S.N.R.1    Maity, R.2    Sharma, J.3    Dey, P.4    Shankar, S.K.5    Satishchandra, P.6    Jana, N.R.7
  • 44
    • 21644475161 scopus 로고    scopus 로고
    • Glycogen autophagy in the liver and heart of newborn rats. The effects of glucagon, adrenalin or rapamycin
    • Kondomerkos, D.J., Kalamidas, S.A., Kotoulas, O.B. and Hann, A.C. (2005) Glycogen autophagy in the liver and heart of newborn rats. The effects of glucagon, adrenalin or rapamycin. Histol. Histopathol., 20, 689-696.
    • (2005) Histol. Histopathol. , vol.20 , pp. 689-696
    • Kondomerkos, D.J.1    Kalamidas, S.A.2    Kotoulas, O.B.3    Hann, A.C.4
  • 45
    • 77649200841 scopus 로고    scopus 로고
    • Autophagy in skeletal muscle: implications for Pompe disease
    • Shea, L. and Raben, N. (2009) Autophagy in skeletal muscle: implications for Pompe disease. Int. J. Clin. Pharmacol. Ther., 47, S42-S47.
    • (2009) Int. J. Clin. Pharmacol. Ther. , vol.47
    • Shea, L.1    Raben, N.2
  • 46
    • 78649338141 scopus 로고    scopus 로고
    • Autophagy and the integrated stress response
    • Kroemer, G., Mariño, G. and Levine, B. (2010) Autophagy and the integrated stress response. Mol. Cell, 40, 280-293.
    • (2010) Mol. Cell , vol.40 , pp. 280-293
    • Kroemer, G.1    Mariño, G.2    Levine, B.3
  • 47
    • 75149191469 scopus 로고    scopus 로고
    • Nibbling away at synaptic development
    • Shen, W. and Ganetzky, B. (2010) Nibbling away at synaptic development. Autophagy, 6, 168-169.
    • (2010) Autophagy , vol.6 , pp. 168-169
    • Shen, W.1    Ganetzky, B.2
  • 48
    • 33745866244 scopus 로고    scopus 로고
    • Shaping cellular form and function by autophagy
    • Bamber, B.A. and Rowland, A.M. (2006) Shaping cellular form and function by autophagy. Autophagy, 2, 247-249.
    • (2006) Autophagy , vol.2 , pp. 247-249
    • Bamber, B.A.1    Rowland, A.M.2
  • 49
    • 0037401773 scopus 로고    scopus 로고
    • Role of proteasomes in the degradation of short-lived proteins in human fibroblasts under various growth conditions
    • Fuertes, G., Villarroya, A. and Knecht, E. (2003) Role of proteasomes in the degradation of short-lived proteins in human fibroblasts under various growth conditions. Int. J. Biochem. Cell Biol., 35, 651-664.
    • (2003) Int. J. Biochem. Cell Biol. , vol.35 , pp. 651-664
    • Fuertes, G.1    Villarroya, A.2    Knecht, E.3
  • 50
    • 53549084325 scopus 로고    scopus 로고
    • Does bafilomycin A1 block the fusion of autophagosomes with lysosomes?
    • Klionsky, D.J., Elazar, Z., Seglen, P.O. and Rubinsztein, D.C. (2008) Does bafilomycin A1 block the fusion of autophagosomes with lysosomes? Autophagy, 4, 849-950.
    • (2008) Autophagy , vol.4 , pp. 849-950
    • Klionsky, D.J.1    Elazar, Z.2    Seglen, P.O.3    Rubinsztein, D.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.