메뉴 건너뛰기




Volumn 95, Issue 4, 2005, Pages 1035-1046

Muscular dystrophy by merosin deficiency decreases acetylcholinesterase activity in thymus of Lama2dy mice

Author keywords

Acetylcholinesterase mRNAs; Glycosylphosphatidylinositol anchored proteins; Laminin; Peripheral blood lymphocytes

Indexed keywords

2 CYANO N (4 CYANOPHENYL) 3 CYCLOPROPYL 3 OXOPROPIONAMIDE; ACETYLCHOLINESTERASE; ACETYLTHIOCHOLINE; AMPHOPHILE; ANTIBODY; CHOLINESTERASE; DIMER; GLYCOSYLPHOSPHATIDYLINOSITOL; LAMININ ALPHA2; LECTIN; MEROSIN; MONOMER; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE PHOSPHODIESTERASE;

EID: 28244492010     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2005.03433.x     Document Type: Article
Times cited : (14)

References (62)
  • 1
    • 0006152802 scopus 로고    scopus 로고
    • Expression of three acetylcholinesterase mRNAs in human lymphocytes
    • Ando T., Fujii T. and Kawashima K. (1999) Expression of three acetylcholinesterase mRNAs in human lymphocytes. Jpn. J. Pharmacol. 79, 289P.
    • (1999) Jpn. J. Pharmacol. , vol.79
    • Ando, T.1    Fujii, T.2    Kawashima, K.3
  • 2
    • 0023483234 scopus 로고
    • Molecular forms of human lymphocyte membrane-bound acetylcholinesterase
    • Bartha E., Rakonczay Z., Kasa P., Hollan S. and Gyevai A. (1987) Molecular forms of human lymphocyte membrane-bound acetylcholinesterase. Life Sci. 41, 1853-1860.
    • (1987) Life Sci , vol.41 , pp. 1853-1860
    • Bartha, E.1    Rakonczay, Z.2    Kasa, P.3    Hollan, S.4    Gyevai, A.5
  • 3
    • 0035091565 scopus 로고    scopus 로고
    • Immuno-characterization of neuroendocrine cells in the rat thymus gland in vitro and vivo
    • Botham C. A., Jones G. V. and Kendall M. D. (2001) Immuno- characterization of neuroendocrine cells in the rat thymus gland in vitro and vivo. Cell Tissue Res. 303, 381-389.
    • (2001) Cell Tissue Res , vol.303 , pp. 381-389
    • Botham, C.A.1    Jones, G.V.2    Kendall, M.D.3
  • 4
    • 0023621364 scopus 로고
    • Nerve-related 3S acetylcholinesterase in murine thymus
    • Bulloch K. and Bossone S. A. (1987) Nerve-related 3S acetylcholinesterase in murine thymus. Ann. N. Y. Acad. Sci. 496, 338-345.
    • (1987) Ann. N. Y. Acad. Sci. , vol.496 , pp. 338-345
    • Bulloch, K.1    Bossone, S.A.2
  • 5
    • 0023694485 scopus 로고
    • The effects of cortisone on acetylcholinesterase (AChE) in the neonatal and aged thymus
    • Bulloch K. and Lucito R. (1988) The effects of cortisone on acetylcholinesterase (AChE) in the neonatal and aged thymus. Ann. N. Y. Acad. Sci. 521, 59-71.
    • (1988) Ann. N. Y. Acad. Sci. , vol.521 , pp. 59-71
    • Bulloch, K.1    Lucito, R.2
  • 6
    • 0028050299 scopus 로고
    • Amphiphilic properties of molecular forms of acetylcholinesterase in normal and dystrophic muscle
    • Cabezas-Herrera J., Campoy F. J. and Vidal C. J. (1994a) Amphiphilic properties of molecular forms of acetylcholinesterase in normal and dystrophic muscle. J. Neurosci. Res. 38, 505-514.
    • (1994) J. Neurosci. Res. , vol.38 , pp. 505-514
    • Cabezas-Herrera, J.1    Campoy, F.J.2    Vidal, C.J.3
  • 7
    • 0028778469 scopus 로고
    • 4 forms of acetylcholinesterase and butyrylcholinesterase in normal and dystrophic mouse muscle differ in their interaction with Ricinus communis agglutinin
    • 4 forms of acetylcholinesterase and butyrylcholinesterase in normal and dystrophic mouse muscle differ in their interaction with Ricinus communis agglutinin. Biochim. Biophys. Acta 1225, 283-288.
    • (1994) Biochim. Biophys. Acta , vol.1225 , pp. 283-288
    • Cabezas-Herrera, J.1    Moral-Naranjo, M.T.2    Campoy, F.J.3    Vidal, C.J.4
  • 8
    • 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. (1997) Glycosylation of acetylcholinesterase forms in microsomal membranes from normal and dystrophic Lama2dy mouse muscle. J. Neurochem. 69, 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
  • 9
    • 0034112933 scopus 로고    scopus 로고
    • Acetylcholinesterase activity in rat thymus after immunostimulation with interleukin β
    • Cavallotti D., Artico M., Cavallotti C., Iannetti G. and Frati A. (2000a) Acetylcholinesterase activity in rat thymus after immunostimulation with interleukin β. Ann. Anat. 182, 243-248.
    • (2000) Ann. Anat. , vol.182 , pp. 243-248
    • Cavallotti, D.1    Artico, M.2    Cavallotti, C.3    Iannetti, G.4    Frati, A.5
  • 10
    • 0033992546 scopus 로고    scopus 로고
    • Quantification of acetylcholinesterase-positive structures in human thymus during development and aging
    • Cavallotti D., Artico M., Iannetti G. and Cavallotti C. (2000b) Quantification of acetylcholinesterase-positive structures in human thymus during development and aging. Neurochem. Int. 36, 75-82.
    • (2000) Neurochem. Int. , vol.36 , pp. 75-82
    • Cavallotti, D.1    Artico, M.2    Iannetti, G.3    Cavallotti, C.4
  • 11
    • 1442323992 scopus 로고    scopus 로고
    • Long-lasting acetylcholinesterase splice variations in anticholinesterase-treated Alzheimer's disease patients
    • Darreh-Shori T., Hellström-Lindahl E., Flores-Flores C., Guan Z. Z., Soreq H. and Nordberg A. (2004) Long-lasting acetylcholinesterase splice variations in anticholinesterase-treated Alzheimer's disease patients. J. Neurochem. 88, 1102-1113.
    • (2004) J. Neurochem. , vol.88 , pp. 1102-1113
    • Darreh-Shori, T.1    Hellström-Lindahl, E.2    Flores-Flores, C.3    Guan, Z.Z.4    Soreq, H.5    Nordberg, A.6
  • 12
    • 18444368408 scopus 로고    scopus 로고
    • Conditional disruption of β1 integrin in Schwann cells impedes interactions with axons
    • Feltri M. L., Porta D. G., Previtali S. C. et al. (2002) Conditional disruption of β1 integrin in Schwann cells impedes interactions with axons. J. Cell Biol. 156, 199-209.
    • (2002) J. Cell Biol. , vol.156 , pp. 199-209
    • Feltri, M.L.1    Porta, D.G.2    Previtali, S.C.3
  • 13
    • 0033594106 scopus 로고    scopus 로고
    • Genetic analysis of collagen Q: Roles in acetylcholinesterase and butyrylcholinesterase assembly and in synaptic structure and function
    • Feng G., Krejci E., Molgo J., Cunningham A., Massoulié J. and Sanes J. R. (1999) Genetic analysis of collagen Q: roles in acetylcholinesterase and butyrylcholinesterase assembly and in synaptic structure and function. J. Cell Biol. 144, 1349-1360.
    • (1999) J. Cell Biol. , vol.144 , pp. 1349-1360
    • Feng, G.1    Krejci, E.2    Molgo, J.3    Cunningham, A.4    Massoulié, J.5    Sanes, J.R.6
  • 15
    • 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. (2000) Muscular dystrophy alters the processing of light acetylcholinesterase but not butyrylcholinesterase forms in liver of Lama2dy mice. J. Neurosci. Res. 62, 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
  • 17
    • 0033568704 scopus 로고    scopus 로고
    • Structural roles of acetylcholinesterase variants in biology and pathology
    • Grisaru D., Sternfeld M., Eldor A., Glick D. and Soreq H. (1999) Structural roles of acetylcholinesterase variants in biology and pathology. Eur. J. Biochem. 264, 672-686.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 672-686
    • Grisaru, D.1    Sternfeld, M.2    Eldor, A.3    Glick, D.4    Soreq, H.5
  • 18
    • 0035376717 scopus 로고    scopus 로고
    • Determination of glycosyl-phosphatidylinositol membrane protein anchorage
    • Hooper N. M. (2001) Determination of glycosyl-phosphatidylinositol membrane protein anchorage. Proteomics 1, 748-755.
    • (2001) Proteomics , vol.1 , pp. 748-755
    • Hooper, N.M.1
  • 19
    • 0034076506 scopus 로고    scopus 로고
    • Interaction of merosin (laminin-2) with very late activation antigen-6 is necessary for the survival of CD4+ CD8+ immature thymocytes
    • Iwao M., Fukada S., Harada T., Tsujikawa K., Yagita H., Hiramine C., Miyagoe Y., Takeda S. and Yamamoto H. (2000) Interaction of merosin (laminin-2) with very late activation antigen-6 is necessary for the survival of CD4+ CD8+ immature thymocytes. Immunology 99, 481-488.
    • (2000) Immunology , vol.99 , pp. 481-488
    • Iwao, M.1    Fukada, S.2    Harada, T.3    Tsujikawa, K.4    Yagita, H.5    Hiramine, C.6    Miyagoe, Y.7    Takeda, S.8    Yamamoto, H.9
  • 20
    • 0034104866 scopus 로고    scopus 로고
    • Extraneuronal cholinergic system in lymphocytes
    • Kawashima K. and Fujii T. (2000) Extraneuronal cholinergic system in lymphocytes. Pharmacol Ther. 86, 29-48.
    • (2000) Pharmacol Ther. , vol.86 , pp. 29-48
    • Kawashima, K.1    Fujii, T.2
  • 21
    • 0029163984 scopus 로고
    • Novel functions of cholinesterases in development, physiology and disease
    • Layer P. G. and Willbold E. (1995) Novel functions of cholinesterases in development, physiology and disease. Prog. Histochem. Cytochem. 29, 1-94.
    • (1995) Prog. Histochem. Cytochem. , vol.29 , pp. 1-94
    • Layer, P.G.1    Willbold, E.2
  • 24
    • 0026335386 scopus 로고
    • Gene structure of mammalian acetylcholinesterase. Alternative exons dictate tissue-specific expression
    • Li Y., Camp S., Rachinsky T. L., German D. and Taylor P. (1991) Gene structure of mammalian acetylcholinesterase. Alternative exons dictate tissue-specific expression. J. Biol. Chem. 266, 23083-23090.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23083-23090
    • Li, Y.1    Camp, S.2    Rachinsky, T.L.3    German, D.4    Taylor, P.5
  • 26
    • 0023179265 scopus 로고
    • Expression of muscarinic cholinergic receptors during T cell maturation in the thymus
    • Maslinski W., Grabczewska E., Laskowska-Bozek H. and Ryzewski J. (1987) Expression of muscarinic cholinergic receptors during T cell maturation in the thymus. Eur. J. Immunol. 17, 1059-1063.
    • (1987) Eur. J. Immunol. , vol.17 , pp. 1059-1063
    • Maslinski, W.1    Grabczewska, E.2    Laskowska-Bozek, H.3    Ryzewski, J.4
  • 27
    • 0033038088 scopus 로고    scopus 로고
    • The polymorphism of acetylcholinesterase: Posttranslational processing, quaternary associations and localization
    • Massoulié J., Anselmet A., Bon S., Krejci E., Legay C., Morel N. and Simon S. (1999) The polymorphism of acetylcholinesterase: posttranslational processing, quaternary associations and localization. Chem. Biol Interact. 119-120, 29-42.
    • (1999) Chem. Biol Interact. , vol.119-120 , pp. 29-42
    • Massoulié, J.1    Anselmet, A.2    Bon, S.3    Krejci, E.4    Legay, C.5    Morel, N.6    Simon, S.7
  • 28
    • 0028344848 scopus 로고
    • Relationships between monoaminergic and cholinergic innervation of the rat thymus during aging
    • Micic M., Leposavic G. and Ugresic N. (1994) Relationships between monoaminergic and cholinergic innervation of the rat thymus during aging. J. Neuroimmunol. 49, 205-212.
    • (1994) J. Neuroimmunol. , vol.49 , pp. 205-212
    • Micic, M.1    Leposavic, G.2    Ugresic, N.3
  • 29
    • 0035796676 scopus 로고    scopus 로고
    • Thymic epithelial cell line expresses transcripts encoding α-3, β-5 and β-4 subunits of acetylcholine receptors, -responds to cholinergic agents and expresses choline acetyl transferase. An in vitro system to investigate thymic cholinergic mechanisms
    • Mihovilovic M. and Butterworth-Robinette J. (2001) Thymic epithelial cell line expresses transcripts encoding α-3, β-5 and β-4 subunits of acetylcholine receptors, -responds to cholinergic agents and expresses choline acetyl transferase. An in vitro system to investigate thymic cholinergic mechanisms. J. Neuroimmunol. 17, 58-67.
    • (2001) J. Neuroimmunol. , vol.17 , pp. 58-67
    • Mihovilovic, M.1    Butterworth-Robinette, J.2
  • 31
    • 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. (1996) Molecular forms of acetyl- and butyrylcholinesterase in normal and dystrophic mouse brain. J. Neurosci. Res. 43, 224-234.
    • (1996) J. Neurosci. Res. , vol.43 , pp. 224-234
    • Moral-Naranjo, M.T.1    Cabezas-Herrera, J.2    Vidal, C.J.3
  • 32
    • 33745173517 scopus 로고    scopus 로고
    • Differential glycosylation of asymmetric acetylcholinesterase forms in external and internal muscle membranes
    • Moral-Naranjo M. T., Cabezas-Herrera J., Campoy F. J. and Vidal C. J. (1997) Differential glycosylation of asymmetric acetylcholinesterase forms in external and internal muscle membranes. Biochem. Soc. Trans. 25, 441S.
    • (1997) Biochem. Soc. Trans. , vol.25
    • Moral-Naranjo, M.T.1    Cabezas-Herrera, J.2    Campoy, F.J.3    Vidal, C.J.4
  • 33
    • 0032838527 scopus 로고    scopus 로고
    • Increased butyrylcholinesterase levels in microsomal membranes of dystrophic Lama2dy mouse muscle
    • Moral-Naranjo M. T., Campoy F. J., Cabezas-Herrera J. and Vidal C. J. (1999) Increased butyrylcholinesterase levels in microsomal membranes of dystrophic Lama2dy mouse muscle. J. Neurochem. 73, 1138-1144.
    • (1999) J. Neurochem. , vol.73 , pp. 1138-1144
    • Moral-Naranjo, M.T.1    Campoy, F.J.2    Cabezas-Herrera, J.3    Vidal, C.J.4
  • 34
    • 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. (2002) Muscular dystrophy with laminin deficiency decreases the content of butyrylcholinesterase tetramers in sciatic nerves of Lama2dy mice. Neurosci. Lett. 331, 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
  • 36
    • 0025175718 scopus 로고
    • Manipulations of cholinesterase gene expression modulate murine megakaryocytopoiesis in vitro
    • Patinkin D., Seidman S., Eckstein F., Benseler F., Zakut H. and Soreq H. (1990) Manipulations of cholinesterase gene expression modulate murine megakaryocytopoiesis in vitro. Mol. Cell. Biol. 10, 6046-6050.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 6046-6050
    • Patinkin, D.1    Seidman, S.2    Eckstein, F.3    Benseler, F.4    Zakut, H.5    Soreq, H.6
  • 37
    • 1542278459 scopus 로고    scopus 로고
    • Lineage choices in the developing thymus: Choosing the T and NKT pathways
    • Pear W. S., Tu L. and Stein P. L. (2004) Lineage choices in the developing thymus: choosing the T and NKT pathways. Curr. Opin. Immunol 16, 167-173.
    • (2004) Curr. Opin. Immunol , vol.16 , pp. 167-173
    • Pear, W.S.1    Tu, L.2    Stein, P.L.3
  • 38
    • 0037122918 scopus 로고    scopus 로고
    • PRiMA: The membrane anchor of acetylcholinesterase in the brain
    • Ferner A. L., Massoulié J. and Krejci E. (2002) PRiMA: the membrane anchor of acetylcholinesterase in the brain. Neuron 33, 275-285.
    • (2002) Neuron , vol.33 , pp. 275-285
    • Ferner, A.L.1    Massoulié, J.2    Krejci, E.3
  • 39
    • 0037028246 scopus 로고    scopus 로고
    • Complex regulation of acetylcholinesterase gene expression in human brain tumors
    • Perry C., Sklan E. H., Birikh K., Shapira M., Trejo L., Eldor A. and Soreq H. (2002) Complex regulation of acetylcholinesterase gene expression in human brain tumors. Oncogene 21, 8428-8441.
    • (2002) Oncogene , vol.21 , pp. 8428-8441
    • Perry, C.1    Sklan, E.H.2    Birikh, K.3    Shapira, M.4    Trejo, L.5    Eldor, A.6    Soreq, H.7
  • 40
    • 0029801456 scopus 로고    scopus 로고
    • Immunoregulatory role of neurotransmiters
    • Qiu Y., Peng Y. and Wang J. (1996) Immunoregulatory role of neurotransmiters. Adv. Neuroimmunol. 6, 223-231.
    • (1996) Adv. Neuroimmunol. , vol.6 , pp. 223-231
    • Qiu, Y.1    Peng, Y.2    Wang, J.3
  • 41
    • 0025161330 scopus 로고
    • Molecular cloning of mouse acetylcholinesterase: Tissue distribution of alternatively spliced mRNA species
    • Rachinsky T. L., Camp S., Li Y., Ekström T. J., Newton M. and Taylor P. (1990) Molecular cloning of mouse acetylcholinesterase: tissue distribution of alternatively spliced mRNA species. Neuron 5, 317-327.
    • (1990) Neuron , vol.5 , pp. 317-327
    • Rachinsky, T.L.1    Camp, S.2    Li, Y.3    Ekström, T.J.4    Newton, M.5    Taylor, P.6
  • 42
    • 0028241566 scopus 로고
    • Cellular expression of a cloned, hydrophilic, murine acetylcholinesterase. Evidence of palmitoylated membrane-bound forms
    • Randall W. R. (1994) Cellular expression of a cloned, hydrophilic, murine acetylcholinesterase. Evidence of palmitoylated membrane-bound forms. J. Biol. Chem. 269, 12 367-12 374.
    • (1994) J. Biol. Chem. , vol.269 , Issue.12 , pp. 367-412
    • Randall, W.R.1
  • 46
    • 77957183589 scopus 로고
    • Modulation of respiratory burst activity and mitogenic response of human peripheral blood mononuclear cells and murine splenocytes and peritoneal cells by malathion
    • Rodgers K. E. and Ellefson D. D. (1990) Modulation of respiratory burst activity and mitogenic response of human peripheral blood mononuclear cells and murine splenocytes and peritoneal cells by malathion. Fundam. Appl. Toxicol. 14, 309-317.
    • (1990) Fundam. Appl. Toxicol. , vol.14 , pp. 309-317
    • Rodgers, K.E.1    Ellefson, D.D.2
  • 47
    • 0024387710 scopus 로고
    • Cholinergic agonists selectively induce proliferative responses in the mature subpopulation of murine thymocytes
    • Rossi A., Tria M. A., Baschieri S., Doria G. and Frasca D. (1989) Cholinergic agonists selectively induce proliferative responses in the mature subpopulation of murine thymocytes. J. Neurosci. Res. 24, 369-373.
    • (1989) J. Neurosci. Res. , vol.24 , pp. 369-373
    • Rossi, A.1    Tria, M.A.2    Baschieri, S.3    Doria, G.4    Frasca, D.5
  • 48
    • 0025768851 scopus 로고
    • Acetylcholinesterase distribution in subpopulations of murine thymocyte
    • Rossi A., Vicini E., Scarsella G. and Biagioni S. (1991) Acetylcholinesterase distribution in subpopulations of murine thymocyte. J. Neurosci. Res. 29, 201-206.
    • (1991) J. Neurosci. Res. , vol.29 , pp. 201-206
    • Rossi, A.1    Vicini, E.2    Scarsella, G.3    Biagioni, S.4
  • 50
    • 0036349637 scopus 로고    scopus 로고
    • Expression and distribution of laminin alpha 1 and alpha 2 chains in embryonic and adult tissues: An immunochemical approach
    • Sasaki T., Giltay R., Talts U., Timpl R. and Talts J. F. (2002) Expression and distribution of laminin alpha 1 and alpha 2 chains in embryonic and adult tissues: an immunochemical approach. Exp. Cell Res. 275, 185-199.
    • (2002) Exp. Cell Res. , vol.275 , pp. 185-199
    • Sasaki, T.1    Giltay, R.2    Talts, U.3    Timpl, R.4    Talts, J.F.5
  • 51
    • 0034883653 scopus 로고    scopus 로고
    • Do immune cells promote the pathology of dystrophin-deficient myopathies?
    • Spencer M. J. and Tidball J. G. (2001) Do immune cells promote the pathology of dystrophin-deficient myopathies? Neuromusc. Disord. 11, 556-564.
    • (2001) Neuromusc. Disord. , vol.11 , pp. 556-564
    • Spencer, M.J.1    Tidball, J.G.2
  • 52
    • 0028174977 scopus 로고
    • The cholinesterases: From genes to proteins
    • Taylor P. and Radic Z. (1994) The cholinesterases: from genes to proteins. Annu. Rev. Pharmacol. Toxicol. 34, 281-320.
    • (1994) Annu. Rev. Pharmacol. Toxicol. , vol.34 , pp. 281-320
    • Taylor, P.1    Radic, Z.2
  • 53
    • 0033112073 scopus 로고    scopus 로고
    • The saga of congenital muscular dystrophy
    • Tomé F. M. S. (1999) The saga of congenital muscular dystrophy. Neuropediatrics 30, 55-65.
    • (1999) Neuropediatrics , vol.30 , pp. 55-65
    • Tomé, F.M.S.1
  • 54
    • 0021927748 scopus 로고
    • Acetylcholinesterase in human thymus cells
    • Topilko A. and Kaillou B. (1985) Acetylcholinesterase in human thymus cells. Blood 66, 891-895.
    • (1985) Blood , vol.66 , pp. 891-895
    • Topilko, A.1    Kaillou, B.2
  • 55
    • 0025058952 scopus 로고
    • Molecular forms of acetylcholinesterase in two sublines of human erythroleukemia K562 cells. Sensitivity or resistance to phosphatidylinositol specific phospholipase C and biosynthesis
    • Toutant J. P., Richards M. K., Krall J. A. and Rosenberry T. L. (1990) Molecular forms of acetylcholinesterase in two sublines of human erythroleukemia K562 cells. Sensitivity or resistance to phosphatidylinositol specific phospholipase C and biosynthesis. Eur. J. Biochem. 187, 31-38.
    • (1990) Eur. J. Biochem. , vol.187 , pp. 31-38
    • Toutant, J.P.1    Richards, M.K.2    Krall, J.A.3    Rosenberry, T.L.4
  • 57
    • 0030610576 scopus 로고    scopus 로고
    • Integrins (alpha7beta1) in muscle function and survival. Disrupted expression in merosin-deficient congenital muscular dystrophy
    • Vachon P. H., Xu H., Liu L., Loechel F., Hayashi Y., Arahata K., Reed J. C., Wewer U. M. and Engvall E. (1997) Integrins (alpha7beta1) in muscle function and survival. Disrupted expression in merosin-deficient congenital muscular dystrophy. J. Clin. Invest. 100, 1870-1881.
    • (1997) J. Clin. Invest. , vol.100 , pp. 1870-1881
    • Vachon, P.H.1    Xu, H.2    Liu, L.3    Loechel, F.4    Hayashi, Y.5    Arahata, K.6    Reed, J.C.7    Wewer, U.M.8    Engvall, E.9
  • 59
    • 0029966435 scopus 로고    scopus 로고
    • Involvement of the NMDA receptor in a non-cholinergic action of acetylcholinesterase in guinea-pig substantia nigra pars compacta neurons
    • Webb C. P., Nedergaard S., Giles K. and Greenfield S. A. (1996) Involvement of the NMDA receptor in a non-cholinergic action of acetylcholinesterase in guinea-pig substantia nigra pars compacta neurons. Eur. J. Neurosci. 8, 837-841.
    • (1996) Eur. J. Neurosci. , vol.8 , pp. 837-841
    • Webb, C.P.1    Nedergaard, S.2    Giles, K.3    Greenfield, S.A.4
  • 60
    • 0037470640 scopus 로고    scopus 로고
    • The non-neuronal cholinergic system in humans: Expression, function and pathophysiology
    • Wessler I., Kilbinger H., Bittinger F., Unger R. and Kirkpatrick C. J. (2003) The non-neuronal cholinergic system in humans: expression, function and pathophysiology. Life Sci. 72, 2055-2061.
    • (2003) Life Sci. , vol.72 , pp. 2055-2061
    • Wessler, I.1    Kilbinger, H.2    Bittinger, F.3    Unger, R.4    Kirkpatrick, C.J.5
  • 61
    • 0028135436 scopus 로고
    • Murine muscular dystrophy caused by a mutation in the laminin alfa2 (Lama2) gene
    • Xu H., Wu X.-R., Wewer U. M. and Engvall E. (1994) Murine muscular dystrophy caused by a mutation in the laminin alfa2 (Lama2) gene. Nat. Genet. 8, 297-302.
    • (1994) Nat. Genet. , vol.8 , pp. 297-302
    • Xu, H.1    Wu, X.-R.2    Wewer, U.M.3    Engvall, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.