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Volumn 175, Issue 1-3, 2008, Pages 312-317

Targeting of acetylcholinesterase to lipid rafts of muscle

Author keywords

Congenital muscular dystrophy; DIGs; GPI anchored proteins; Laminin 2

Indexed keywords

ACETYLCHOLINESTERASE; CAVEOLIN 3; CHOLINERGIC RECEPTOR; DIMER; DYSTROPHIN; ECTO 5' NUCLEOTIDASE; GLYCOSYLPHOSPHATIDYLINOSITOL; MEROSIN; MUSCARINIC RECEPTOR; NICOTINIC RECEPTOR; PHOSPHOLIPASE C; TRITON X 100;

EID: 50649125121     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2008.04.018     Document Type: Article
Times cited : (2)

References (30)
  • 2
    • 33846265912 scopus 로고    scopus 로고
    • Congenital muscular dystrophies: new aspects of an expanding group of disorders
    • Lisi M.T., and Cohn R.D. Congenital muscular dystrophies: new aspects of an expanding group of disorders. Biochim. Biophys. Acta 1772 (2007) 159-172
    • (2007) Biochim. Biophys. Acta , vol.1772 , pp. 159-172
    • Lisi, M.T.1    Cohn, R.D.2
  • 3
    • 0037131559 scopus 로고    scopus 로고
    • Muscular dystrophy with laminin deficiency decreases the content of butyrylcholinesterase tetramers in sciatic nerves of Lama2dy mice
    • Moral-Naranjo M.T., Cabezas-Herrera J., Vidal C.J., and Campoy F.J. Muscular dystrophy with laminin deficiency decreases the content of butyrylcholinesterase tetramers in sciatic nerves of Lama2dy mice. Neurosci. Lett. 331 (2002) 155-158
    • (2002) Neurosci. Lett. , vol.331 , pp. 155-158
    • Moral-Naranjo, M.T.1    Cabezas-Herrera, J.2    Vidal, C.J.3    Campoy, F.J.4
  • 4
    • 34249087192 scopus 로고    scopus 로고
    • Sphingomyelin chain length influences the distribution of GPI-anchored proteins in rafts in supported lipid bilayers
    • Garner A.E., Smith D.A., and Hooper N.M. Sphingomyelin chain length influences the distribution of GPI-anchored proteins in rafts in supported lipid bilayers. Mol. Membr. Biol. 24 (2007) 233-242
    • (2007) Mol. Membr. Biol. , vol.24 , pp. 233-242
    • Garner, A.E.1    Smith, D.A.2    Hooper, N.M.3
  • 5
    • 34248195469 scopus 로고    scopus 로고
    • Lipid rafts and membrane traffic
    • Hanzal-Bayer M.F., and Hancock J.F. Lipid rafts and membrane traffic. FEBS Lett. 581 (2007) 2098-2104
    • (2007) FEBS Lett. , vol.581 , pp. 2098-2104
    • Hanzal-Bayer, M.F.1    Hancock, J.F.2
  • 6
    • 2142647335 scopus 로고    scopus 로고
    • The biology of caveolae: lessons from caveolin knockout mice and implications for human disease
    • Hnasko R., and Lisanti M.P. The biology of caveolae: lessons from caveolin knockout mice and implications for human disease. Mol. Intervent. 3 (2003) 445-463
    • (2003) Mol. Intervent. , vol.3 , pp. 445-463
    • Hnasko, R.1    Lisanti, M.P.2
  • 8
    • 33845563646 scopus 로고    scopus 로고
    • Agrin elicits membrane lipid condensation at sites of acetylcholine receptor clusters in C2C12 myotubes
    • Stetzkowski-Marden F., Gaus C., Recouvreur M., Cartaud A., and Cartaud J. Agrin elicits membrane lipid condensation at sites of acetylcholine receptor clusters in C2C12 myotubes. J. Lipid Res. 47 (2006) 2121-2133
    • (2006) J. Lipid Res. , vol.47 , pp. 2121-2133
    • Stetzkowski-Marden, F.1    Gaus, C.2    Recouvreur, M.3    Cartaud, A.4    Cartaud, J.5
  • 9
    • 28744432658 scopus 로고    scopus 로고
    • The C-terminal peptides of acetylcholinesterase: cellular trafficking, oligomerization and functional anchoring
    • Massoulié J., Bon S., Perrier N., and Falasca C. The C-terminal peptides of acetylcholinesterase: cellular trafficking, oligomerization and functional anchoring. Chem. Biol. Interact. 157/158 (2005) 3-14
    • (2005) Chem. Biol. Interact. , vol.157-158 , pp. 3-14
    • Massoulié, J.1    Bon, S.2    Perrier, N.3    Falasca, C.4
  • 10
    • 33645988822 scopus 로고    scopus 로고
    • Virtues and woes of AChE alternative splicing in stress-related neuropathologies
    • Meshorer E., and Soreq H. Virtues and woes of AChE alternative splicing in stress-related neuropathologies. Trends Neurosci. 29 (2006) 216-224
    • (2006) Trends Neurosci. , vol.29 , pp. 216-224
    • Meshorer, E.1    Soreq, H.2
  • 11
    • 28244492010 scopus 로고    scopus 로고
    • Muscular dystrophy by merosin deficiency decreases acetylcholinesterase activity in thymus of Lama2dy mice
    • Nieto-Cerón S., Sánchez del Campo L.F., Muñoz-Delgado E., Vidal C.J., and Campoy F.J. Muscular dystrophy by merosin deficiency decreases acetylcholinesterase activity in thymus of Lama2dy mice. J. Neurochem. 95 (2005) 1035-1046
    • (2005) J. Neurochem. , vol.95 , pp. 1035-1046
    • Nieto-Cerón, S.1    Sánchez del Campo, L.F.2    Muñoz-Delgado, E.3    Vidal, C.J.4    Campoy, F.J.5
  • 12
    • 0030833450 scopus 로고    scopus 로고
    • Glycosylation of acetylcholinesterase forms in microsomal membranes from normal and dystrophic Lama2dy mouse muscle
    • Cabezas-Herrera J., Moral-Naranjo M.T., Campoy F.J., and Vidal C.J. Glycosylation of acetylcholinesterase forms in microsomal membranes from normal and dystrophic Lama2dy mouse muscle. J. Neurochem. 69 (1997) 1964-1974
    • (1997) J. Neurochem. , vol.69 , pp. 1964-1974
    • Cabezas-Herrera, J.1    Moral-Naranjo, M.T.2    Campoy, F.J.3    Vidal, C.J.4
  • 14
    • 28744433847 scopus 로고    scopus 로고
    • Acetylcholinesterase and molecular interactions at the neuromuscular junction
    • Guerra M., Cartaud A., Cartaud J., and Legay C. Acetylcholinesterase and molecular interactions at the neuromuscular junction. Chem. Biol. Interact. 157/158 (2005) 57-61
    • (2005) Chem. Biol. Interact. , vol.157-158 , pp. 57-61
    • Guerra, M.1    Cartaud, A.2    Cartaud, J.3    Legay, C.4
  • 15
    • 0032504045 scopus 로고    scopus 로고
    • Increased caveolin-3 levels in mdx mouse muscles
    • Vaghy P., Fang J., Wu W., and Vaghy L. Increased caveolin-3 levels in mdx mouse muscles. FEBS Lett. 431 (1998) 125-127
    • (1998) FEBS Lett. , vol.431 , pp. 125-127
    • Vaghy, P.1    Fang, J.2    Wu, W.3    Vaghy, L.4
  • 17
    • 0035877753 scopus 로고    scopus 로고
    • Caveolin-3 null mice show a loss of caveolae, changes in the microdomain distribution of the dystrophin-glycoprotein complex, and T-tubule abnormalities
    • Galbiati F., Engelman J.A., Volonte D., Zhang X.L., Minetti C., Li M., Hou H., Kneitz B., Edelmann W., and Lisanti M.P. Caveolin-3 null mice show a loss of caveolae, changes in the microdomain distribution of the dystrophin-glycoprotein complex, and T-tubule abnormalities. J. Biol. Chem. 276 (2001) 21425-21433
    • (2001) J. Biol. Chem. , vol.276 , pp. 21425-21433
    • Galbiati, F.1    Engelman, J.A.2    Volonte, D.3    Zhang, X.L.4    Minetti, C.5    Li, M.6    Hou, H.7    Kneitz, B.8    Edelmann, W.9    Lisanti, M.P.10
  • 20
    • 0030043539 scopus 로고    scopus 로고
    • Molecular forms of acetyl- and butyrylcholinesterase in normal and dystrophic mouse brain
    • Moral-Naranjo M.T., Cabezas-Herrera J., and Vidal C.J. Molecular forms of acetyl- and butyrylcholinesterase in normal and dystrophic mouse brain. J. Neurosci. Res. 43 (1996) 224-234
    • (1996) J. Neurosci. Res. , vol.43 , pp. 224-234
    • Moral-Naranjo, M.T.1    Cabezas-Herrera, J.2    Vidal, C.J.3
  • 21
    • 1642554298 scopus 로고    scopus 로고
    • Merosin (laminin-2) localization in basal lamina of normal skeletal muscle fibers and changes in plasma membrane of merosin-deficient skeletal muscle fibers
    • Shibuya S., Wakayama Y., Inoue M., Kojima H., and Oniki H. Merosin (laminin-2) localization in basal lamina of normal skeletal muscle fibers and changes in plasma membrane of merosin-deficient skeletal muscle fibers. Med. Electron. Microsc. 36 (2003) 213-220
    • (2003) Med. Electron. Microsc. , vol.36 , pp. 213-220
    • Shibuya, S.1    Wakayama, Y.2    Inoue, M.3    Kojima, H.4    Oniki, H.5
  • 23
    • 33749153609 scopus 로고    scopus 로고
    • Phenotypic conversion leads to structural and functional changes of smooth muscle sarcolemma
    • Matschke K., Babiychuk E.B., Monastyrskaya K., and Draeger A. Phenotypic conversion leads to structural and functional changes of smooth muscle sarcolemma. Exp. Cell Res. 312 (2006) 3495-3503
    • (2006) Exp. Cell Res. , vol.312 , pp. 3495-3503
    • Matschke, K.1    Babiychuk, E.B.2    Monastyrskaya, K.3    Draeger, A.4
  • 24
    • 0029088486 scopus 로고
    • Developmental regulation of acetylcholinesterase transcripts in the mouse diaphragm: alternative splicing and focalization
    • Legay C., Huchet M., Massoulié J., and Changeux J.P. Developmental regulation of acetylcholinesterase transcripts in the mouse diaphragm: alternative splicing and focalization. Eur. J. Neurosci. 7 (1995) 1803-1809
    • (1995) Eur. J. Neurosci. , vol.7 , pp. 1803-1809
    • Legay, C.1    Huchet, M.2    Massoulié, J.3    Changeux, J.P.4
  • 25
    • 34249694687 scopus 로고    scopus 로고
    • Regulation of a transcript encoding the proline-rich membrane anchor of globular muscle acetylcholinesterase. The suppressive roles of myogenesis and innervating nerves
    • Xie H.Q., Choi R.C., Leung K.W., Siow N.L., Kong L.W., Lau F.T., Peng H.B., and Tsim K.W. Regulation of a transcript encoding the proline-rich membrane anchor of globular muscle acetylcholinesterase. The suppressive roles of myogenesis and innervating nerves. J. Biol. Chem. 282 (2007) 11765-11775
    • (2007) J. Biol. Chem. , vol.282 , pp. 11765-11775
    • Xie, H.Q.1    Choi, R.C.2    Leung, K.W.3    Siow, N.L.4    Kong, L.W.5    Lau, F.T.6    Peng, H.B.7    Tsim, K.W.8
  • 26
    • 0344483883 scopus 로고    scopus 로고
    • Characterization of acetylcholinesterase and butyrylcholinesterase forms in normal and dystrophic Lama2dy mouse heart
    • Gómez J.L., Moral-Naranjo M.T., Campoy F.J., and Vidal C.J. Characterization of acetylcholinesterase and butyrylcholinesterase forms in normal and dystrophic Lama2dy mouse heart. J. Neurosci. Res. 56 (1999) 295-306
    • (1999) J. Neurosci. Res. , vol.56 , pp. 295-306
    • Gómez, J.L.1    Moral-Naranjo, M.T.2    Campoy, F.J.3    Vidal, C.J.4
  • 27
    • 0033769980 scopus 로고    scopus 로고
    • Muscular dystrophy alters the processing of light acetylcholinesterase but not butyrylcholinesterase forms in liver of Lama2dy mice
    • Gómez J.L., García-Ayllón M.S., Campoy F.J., and Vidal C.J. Muscular dystrophy alters the processing of light acetylcholinesterase but not butyrylcholinesterase forms in liver of Lama2dy mice. J. Neurosci. Res. 62 (2000) 134-145
    • (2000) J. Neurosci. Res. , vol.62 , pp. 134-145
    • Gómez, J.L.1    García-Ayllón, M.S.2    Campoy, F.J.3    Vidal, C.J.4
  • 29
    • 28744440838 scopus 로고    scopus 로고
    • Expression of cholinesterases in brain and non-brain tumours
    • Vidal C.J. Expression of cholinesterases in brain and non-brain tumours. Chem. Biol. Interact. 157/158 (2005) 227-232
    • (2005) Chem. Biol. Interact. , vol.157-158 , pp. 227-232
    • Vidal, C.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.