메뉴 건너뛰기




Volumn 123, Issue 3, 2006, Pages 228-240

A genetic model for muscle-eye-brain disease in mice lacking protein O-mannose 1,2-N-acetylglucosaminyltransferase (POMGnT1)

Author keywords

dystroglycan; Electroretinogram; Mouse model; Muscle eye brain disease; Neuronal migration; OmniBank; POMGnT1

Indexed keywords

ALPHA DYSTROGLYCAN; ISOENZYME; MESSENGER RNA; O MANNOSE 1,2 N ACETYLGLUCOSAMINYLTRANSFERASE; RETROVIRUS VECTOR; UNCLASSIFIED DRUG;

EID: 33645971589     PISSN: 09254773     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mod.2005.12.003     Document Type: Article
Times cited : (111)

References (43)
  • 1
    • 3142731311 scopus 로고    scopus 로고
    • LARGE can functionally bypass alpha-dystroglycan glycosylation defects in distinct congenital muscular dystrophies
    • Barresi R., Michele D.E., Kanagawa M., Harper H.A., Dovico S.A., Satz J.S., et al. LARGE can functionally bypass alpha-dystroglycan glycosylation defects in distinct congenital muscular dystrophies. Nat. Med. 10 (2004) 696-703
    • (2004) Nat. Med. , vol.10 , pp. 696-703
    • Barresi, R.1    Michele, D.E.2    Kanagawa, M.3    Harper, H.A.4    Dovico, S.A.5    Satz, J.S.6
  • 4
    • 0042734819 scopus 로고    scopus 로고
    • An adhesion molecule involved in muscular dystrophies: structural and functional analysis of dystroglycan domains
    • Brancaccio A. An adhesion molecule involved in muscular dystrophies: structural and functional analysis of dystroglycan domains. Ital. J. Biochem. 52 (2003) 51-54
    • (2003) Ital. J. Biochem. , vol.52 , pp. 51-54
    • Brancaccio, A.1
  • 5
    • 0033032081 scopus 로고    scopus 로고
    • Dystrophic phenotype induced in vitro by antibody blockade of muscle alpha-dystroglycan-laminin interaction
    • Brown S.C., Fassati A., Popplewell L., Page A.M., Henry M.D., Campbell K.P., et al. Dystrophic phenotype induced in vitro by antibody blockade of muscle alpha-dystroglycan-laminin interaction. J. Cell Sci. 112 (1999) 209-216
    • (1999) J. Cell Sci. , vol.112 , pp. 209-216
    • Brown, S.C.1    Fassati, A.2    Popplewell, L.3    Page, A.M.4    Henry, M.D.5    Campbell, K.P.6
  • 6
    • 0028914964 scopus 로고
    • Three muscular dystrophies: loss of cytoskeleton-extracellular matrix linkage
    • Campell K.P. Three muscular dystrophies: loss of cytoskeleton-extracellular matrix linkage. Cell 80 (1995) 675-679
    • (1995) Cell , vol.80 , pp. 675-679
    • Campell, K.P.1
  • 7
    • 0031026624 scopus 로고    scopus 로고
    • Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve alpha-dystroglycan. The role of a novel O-mannosyl-type oligosaccharide in the binding of alpha-dystroglycan with laminin
    • Chiba A., Matsumura K., Yamada H., Inazu T., Shimizu T., Kusunoki S., et al. Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve alpha-dystroglycan. The role of a novel O-mannosyl-type oligosaccharide in the binding of alpha-dystroglycan with laminin. J. Biol. Chem. 272 (1997) 2156-2162
    • (1997) J. Biol. Chem. , vol.272 , pp. 2156-2162
    • Chiba, A.1    Matsumura, K.2    Yamada, H.3    Inazu, T.4    Shimizu, T.5    Kusunoki, S.6
  • 8
    • 0033360965 scopus 로고    scopus 로고
    • Assignment of the muscle-eye-brain disease gene to 1p32-p34 by linkage analysis and homozygosity mapping
    • Cormand B., Avela K., Pihko H., Santavuori P., Talim B., Topaloglu H., et al. Assignment of the muscle-eye-brain disease gene to 1p32-p34 by linkage analysis and homozygosity mapping. Am. J. Hum. Genet. 64 (1999) 126-135
    • (1999) Am. J. Hum. Genet. , vol.64 , pp. 126-135
    • Cormand, B.1    Avela, K.2    Pihko, H.3    Santavuori, P.4    Talim, B.5    Topaloglu, H.6
  • 9
    • 0031048434 scopus 로고    scopus 로고
    • The muscular dystrophies-clarity or chaos?
    • Dubowitz V. The muscular dystrophies-clarity or chaos?. N. Engl. J. Med. 336 (1997) 650-651
    • (1997) N. Engl. J. Med. , vol.336 , pp. 650-651
    • Dubowitz, V.1
  • 11
    • 0032712593 scopus 로고    scopus 로고
    • O-Mannosyl glycans in mammals
    • Endo T. O-Mannosyl glycans in mammals. Biochim. Biophys. Acta 1473 (1999) 237-246
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 237-246
    • Endo, T.1
  • 12
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • Ervasti J.M., and Campbell K.P. A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J. Cell Biol. 122 (1993) 809-823
    • (1993) J. Cell Biol. , vol.122 , pp. 809-823
    • Ervasti, J.M.1    Campbell, K.P.2
  • 13
    • 0019471880 scopus 로고
    • Congenital progressive muscular dystrophy of the Fukuyama type-clinical, genetic and pathological considerations
    • Fukuyama Y., Osawa M., and Suzuki H. Congenital progressive muscular dystrophy of the Fukuyama type-clinical, genetic and pathological considerations. Brain Dev. 3 (1981) 1-29
    • (1981) Brain Dev. , vol.3 , pp. 1-29
    • Fukuyama, Y.1    Osawa, M.2    Suzuki, H.3
  • 14
    • 0034975777 scopus 로고    scopus 로고
    • Mutant glycosyltransferase and altered glycosylation of alpha-dystroglycan in the myodystrophy mouse
    • Grewal P.K., Holzfeind P.J., Bittner R.E., and Hewitt J.E. Mutant glycosyltransferase and altered glycosylation of alpha-dystroglycan in the myodystrophy mouse. Nat. Genet. 28 2 (2001) 151-154
    • (2001) Nat. Genet. , vol.28 , Issue.2 , pp. 151-154
    • Grewal, P.K.1    Holzfeind, P.J.2    Bittner, R.E.3    Hewitt, J.E.4
  • 15
    • 0035838362 scopus 로고    scopus 로고
    • Selective deficiency of alpha-dystroglycan in Fukuyama-type congenital muscular dystrophy
    • Hayashi Y.K., Ogawa M., Tagawa K., Noguchi S., Ishihara T., Nonaka I., et al. Selective deficiency of alpha-dystroglycan in Fukuyama-type congenital muscular dystrophy. Neurology 57 (2001) 115-121
    • (2001) Neurology , vol.57 , pp. 115-121
    • Hayashi, Y.K.1    Ogawa, M.2    Tagawa, K.3    Noguchi, S.4    Ishihara, T.5    Nonaka, I.6
  • 16
    • 0036799939 scopus 로고    scopus 로고
    • Skeletal, cardiac and tongue muscle pathology, defective retinal transmission, and neuronal migration defects in the Large(myd) mouse defines a natural model for glycosylation-deficient muscle-eye-brain disorders
    • Holzfeind P.J., Grewal P.K., Reitsamer H.A., Kechvar J., Lassmann H., Hoeger H., et al. Skeletal, cardiac and tongue muscle pathology, defective retinal transmission, and neuronal migration defects in the Large(myd) mouse defines a natural model for glycosylation-deficient muscle-eye-brain disorders. Hum. Mol. Genet. 11 (2002) 2673-2687
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2673-2687
    • Holzfeind, P.J.1    Grewal, P.K.2    Reitsamer, H.A.3    Kechvar, J.4    Lassmann, H.5    Hoeger, H.6
  • 17
    • 0033180233 scopus 로고    scopus 로고
    • Chemorepulsion of neuronal migration by Slit2 in the developing mammalian forebrain
    • Hu H. Chemorepulsion of neuronal migration by Slit2 in the developing mammalian forebrain. Neuron 23 (1999) 703-711
    • (1999) Neuron , vol.23 , pp. 703-711
    • Hu, H.1
  • 18
    • 0034283812 scopus 로고    scopus 로고
    • Polysialic acid regulates chain formation by migrating olfactory interneuron precursors
    • Hu H. Polysialic acid regulates chain formation by migrating olfactory interneuron precursors. J. Neurosci. Res. 61 (2000) 480-492
    • (2000) J. Neurosci. Res. , vol.61 , pp. 480-492
    • Hu, H.1
  • 20
    • 2942733346 scopus 로고    scopus 로고
    • Molecular recognition by LARGE is essential for expression of functional dystroglycan
    • Kanagawa M., Saito F., Kunz S., Yoshida-Moriguchi T., Barresi R., Kobayashi Y.M., et al. Molecular recognition by LARGE is essential for expression of functional dystroglycan. Cell 117 (2004) 953-964
    • (2004) Cell , vol.117 , pp. 953-964
    • Kanagawa, M.1    Saito, F.2    Kunz, S.3    Yoshida-Moriguchi, T.4    Barresi, R.5    Kobayashi, Y.M.6
  • 21
    • 17044453813 scopus 로고    scopus 로고
    • Founder-haplotype analysis in Fukuyama-type congenital muscular dystrophy (FCMD)
    • Kobayashi K., Nakahori Y., Mizuno K., Miyake M., Kumagai T., Honma A., et al. Founder-haplotype analysis in Fukuyama-type congenital muscular dystrophy (FCMD). Hum. Genet. 103 (1998) 323-327
    • (1998) Hum. Genet. , vol.103 , pp. 323-327
    • Kobayashi, K.1    Nakahori, Y.2    Mizuno, K.3    Miyake, M.4    Kumagai, T.5    Honma, A.6
  • 22
    • 24944532170 scopus 로고    scopus 로고
    • Ocular abnormalities in Large(myd) and Large(vls) mice, spontaneous models for muscle, eye, and brain diseases
    • Lee Y., Kameya S., Cox G.A., Hsu J., Hicks W., Maddatu T.P., et al. Ocular abnormalities in Large(myd) and Large(vls) mice, spontaneous models for muscle, eye, and brain diseases. Mol. Cell. Neurosci. 30 (2005) 160-172
    • (2005) Mol. Cell. Neurosci. , vol.30 , pp. 160-172
    • Lee, Y.1    Kameya, S.2    Cox, G.A.3    Hsu, J.4    Hicks, W.5    Maddatu, T.P.6
  • 23
    • 0141783992 scopus 로고    scopus 로고
    • Congenital diaphragmatic hernia, kidney agenesis and cardiac defects associated with Slit3-deficiency in mice
    • Liu J., Zhang L., Wang D., Shen H., Jiang M., Mei P., et al. Congenital diaphragmatic hernia, kidney agenesis and cardiac defects associated with Slit3-deficiency in mice. Mech. Dev. 120 (2003) 1059-1070
    • (2003) Mech. Dev. , vol.120 , pp. 1059-1070
    • Liu, J.1    Zhang, L.2    Wang, D.3    Shen, H.4    Jiang, M.5    Mei, P.6
  • 24
    • 0025836594 scopus 로고
    • J1/tenascin in substrate-bound and soluble form displays contrary effects on neurite outgrowth
    • Lochter A., Vaughan L., Kaplony A., Prochiantz A., Schachner M., and Faissner A. J1/tenascin in substrate-bound and soluble form displays contrary effects on neurite outgrowth. J. Cell Biol. 113 (1991) 1159-1171
    • (1991) J. Cell Biol. , vol.113 , pp. 1159-1171
    • Lochter, A.1    Vaughan, L.2    Kaplony, A.3    Prochiantz, A.4    Schachner, M.5    Faissner, A.6
  • 25
    • 10744226857 scopus 로고    scopus 로고
    • Mutations in the human LARGE gene cause MDC1D, a novel form of congenital muscular dystrophy with severe mental retardation and abnormal glycosylation of alpha-dystroglycan
    • Longman C., Brockington M., Torelli S., Jimenez-Mallebrera C., Kennedy C., Khalil N., et al. Mutations in the human LARGE gene cause MDC1D, a novel form of congenital muscular dystrophy with severe mental retardation and abnormal glycosylation of alpha-dystroglycan. Hum. Mol. Genet. 12 (2003) 2853-2861
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 2853-2861
    • Longman, C.1    Brockington, M.2    Torelli, S.3    Jimenez-Mallebrera, C.4    Kennedy, C.5    Khalil, N.6
  • 26
    • 0347635516 scopus 로고    scopus 로고
    • Demonstration of mammalian protein O-mannosyltransferase activity: coexpression of POMT1 and POMT2 required for enzymatic activity
    • Manya H., Chiba A., Yoshida A., Wang X., Chiba Y., Jigami Y., et al. Demonstration of mammalian protein O-mannosyltransferase activity: coexpression of POMT1 and POMT2 required for enzymatic activity. Proc. Natl Acad. Sci. USA 101 (2004) 500-505
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 500-505
    • Manya, H.1    Chiba, A.2    Yoshida, A.3    Wang, X.4    Chiba, Y.5    Jigami, Y.6
  • 27
    • 0038182574 scopus 로고    scopus 로고
    • Dystrophin-glycoprotein complex: post-translational processing and dystroglycan function
    • Michele D.E., and Campbell K.P. Dystrophin-glycoprotein complex: post-translational processing and dystroglycan function. J. Biol. Chem. 278 (2003) 15457-15460
    • (2003) J. Biol. Chem. , vol.278 , pp. 15457-15460
    • Michele, D.E.1    Campbell, K.P.2
  • 28
    • 0037173670 scopus 로고    scopus 로고
    • Post-translational disruption of dystroglycan-ligand interactions in congenital muscular dystrophies
    • Michele D.E., Barresi R., Kanagawa M., Saito F., Cohn R.D., Satz J.S., et al. Post-translational disruption of dystroglycan-ligand interactions in congenital muscular dystrophies. Nature 418 (2002) 417-422
    • (2002) Nature , vol.418 , pp. 417-422
    • Michele, D.E.1    Barresi, R.2    Kanagawa, M.3    Saito, F.4    Cohn, R.D.5    Satz, J.S.6
  • 29
    • 0037461754 scopus 로고    scopus 로고
    • Targeting dystroglycan in the brain
    • Montanaro F., and Carbonetto S. Targeting dystroglycan in the brain. Neuron 37 (2003) 193-196
    • (2003) Neuron , vol.37 , pp. 193-196
    • Montanaro, F.1    Carbonetto, S.2
  • 30
    • 0037173629 scopus 로고    scopus 로고
    • Deletion of brain dystroglycan recapitulates aspects of congenital muscular dystrophy
    • Moore S.A., Saito F., Chen J., Michele D.E., Henry M.D., Messing A., et al. Deletion of brain dystroglycan recapitulates aspects of congenital muscular dystrophy. Nature 418 (2002) 422-425
    • (2002) Nature , vol.418 , pp. 422-425
    • Moore, S.A.1    Saito, F.2    Chen, J.3    Michele, D.E.4    Henry, M.D.5    Messing, A.6
  • 31
    • 0027172743 scopus 로고
    • Dystrophin expression in the human retina is required for normal function as defined by electroretinography
    • Pillers D.A., Bulman D.E., Weleber R.G., Sigesmund D.A., Musarella M.A., Powell B.R., et al. Dystrophin expression in the human retina is required for normal function as defined by electroretinography. Nat Genet 4 (1993) 82-86
    • (1993) Nat Genet , vol.4 , pp. 82-86
    • Pillers, D.A.1    Bulman, D.E.2    Weleber, R.G.3    Sigesmund, D.A.4    Musarella, M.A.5    Powell, B.R.6
  • 33
    • 0029072703 scopus 로고
    • Purification of cranin, a laminin binding membrane protein. Identity with dystroglycan and reassessment of its carbohydrate moieties
    • Smalheiser N.R., and Kim E. Purification of cranin, a laminin binding membrane protein. Identity with dystroglycan and reassessment of its carbohydrate moieties. J. Biol. Chem. 270 (1995) 15425-15433
    • (1995) J. Biol. Chem. , vol.270 , pp. 15425-15433
    • Smalheiser, N.R.1    Kim, E.2
  • 34
    • 0032508544 scopus 로고    scopus 로고
    • Structural analysis of sequences O-linked to mannose reveals a novel Lewis X structure in cranin (dystroglycan) purified from sheep brain
    • Smalheiser N.R., Haslam S.M., Sutton-Smith M., Morris H.R., and Dell A. Structural analysis of sequences O-linked to mannose reveals a novel Lewis X structure in cranin (dystroglycan) purified from sheep brain. J. Biol. Chem. 273 (1998) 23698-23703
    • (1998) J. Biol. Chem. , vol.273 , pp. 23698-23703
    • Smalheiser, N.R.1    Haslam, S.M.2    Sutton-Smith, M.3    Morris, H.R.4    Dell, A.5
  • 36
    • 0035095886 scopus 로고    scopus 로고
    • A new beta-1,2-N-acetylglucosaminyltransferase that may play a role in the biosynthesis of mammalian O-mannosyl glycans
    • Takahashi S., Sasaki T., Manya H., Chiba Y., Yoshida A., Mizuno M., et al. A new beta-1,2-N-acetylglucosaminyltransferase that may play a role in the biosynthesis of mammalian O-mannosyl glycans. Glycobiology 11 (2001) 37-45
    • (2001) Glycobiology , vol.11 , pp. 37-45
    • Takahashi, S.1    Sasaki, T.2    Manya, H.3    Chiba, Y.4    Yoshida, A.5    Mizuno, M.6
  • 37
    • 10744230411 scopus 로고    scopus 로고
    • Fukutin is required for maintenance of muscle integrity, cortical histiogenesis and normal eye development
    • Takeda S., Kondo M., Sasaki J., Kurahashi H., Kano H., Arai K., et al. Fukutin is required for maintenance of muscle integrity, cortical histiogenesis and normal eye development. Hum. Mol. Genet. 12 (2003) 1449-1459
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 1449-1459
    • Takeda, S.1    Kondo, M.2    Sasaki, J.3    Kurahashi, H.4    Kano, H.5    Arai, K.6
  • 42
    • 18044400450 scopus 로고    scopus 로고
    • Muscular dystrophy and neuronal migration disorder caused by mutations in a glycosyltransferase, POMGnT1
    • Yoshida A., Kobayashi K., Manya H., Taniguchi K., Kano H., Mizuno M., et al. Muscular dystrophy and neuronal migration disorder caused by mutations in a glycosyltransferase, POMGnT1. Dev. Cell 1 (2001) 717-724
    • (2001) Dev. Cell , vol.1 , pp. 717-724
    • Yoshida, A.1    Kobayashi, K.2    Manya, H.3    Taniguchi, K.4    Kano, H.5    Mizuno, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.