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Volumn 15, Issue 5, 2005, Pages 336-341

Proteolysis of β-dystroglycan in muscular diseases

Author keywords

Duchenne muscular dystrophy; Dystroglycan; Dystrophin; Extracellular matrix; Laminin; Matrix metalloproteinase; Sarcoglyan; Sarcoglycanopathy

Indexed keywords

BETA DYSTROGLYCAN; BIOLOGICAL MARKER; DYSTROGLYCAN; MATRIX METALLOPROTEINASE; MEMBRANE PROTEIN; MONOCLONAL ANTIBODY; UNCLASSIFIED DRUG;

EID: 17044425028     PISSN: 09608966     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.nmd.2005.01.007     Document Type: Article
Times cited : (43)

References (22)
  • 2
    • 0030272647 scopus 로고    scopus 로고
    • Dystroglycan: An extracellular matrix receptor linked to the cytoskeleton
    • M.D. Henry, and K.P. Campbell Dystroglycan: an extracellular matrix receptor linked to the cytoskeleton Curr Opin Cell Biol 8 1996 625 631
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 625-631
    • Henry, M.D.1    Campbell, K.P.2
  • 3
    • 0035252649 scopus 로고    scopus 로고
    • The complexities of dystroglycan
    • S.J. Winder The complexities of dystroglycan Trends Biochem Sci 26 2001 118 124
    • (2001) Trends Biochem Sci , vol.26 , pp. 118-124
    • Winder, S.J.1
  • 4
    • 0033539929 scopus 로고    scopus 로고
    • Structural and functional analysis of the N-terminal extracellular region of β-dystroglycan
    • E.D. Stasio, F. Sciandra, and B. Maras Structural and functional analysis of the N-terminal extracellular region of β-dystroglycan Biochem Biophys Res Comm 206 1999 274 278
    • (1999) Biochem Biophys Res Comm , vol.206 , pp. 274-278
    • Stasio, E.D.1    Sciandra, F.2    Maras, B.3
  • 5
    • 1842429177 scopus 로고    scopus 로고
    • ZZ domain is essentially required for the physiological binding of dystrophin and utrophin to β-dystroglycan
    • M. Ishikawa-Sakurai, M. Yoshida, M. Imamura, K.E. Davies, and E. Ozawa ZZ domain is essentially required for the physiological binding of dystrophin and utrophin to β-dystroglycan Hum Molec Genet 13 2004 693 702
    • (2004) Hum Molec Genet , vol.13 , pp. 693-702
    • Ishikawa-Sakurai, M.1    Yoshida, M.2    Imamura, M.3    Davies, K.E.4    Ozawa, E.5
  • 6
    • 0035878554 scopus 로고    scopus 로고
    • Processing of β-dystroglycan by matrix metalloproteinase disrupts the link between the extracellular matrix and cell membrane via the dystroglycan complex
    • H. Yamada, F. Saito, and H. Fukuta-Ohi Processing of β-dystroglycan by matrix metalloproteinase disrupts the link between the extracellular matrix and cell membrane via the dystroglycan complex Hum Molec Genet 10 2001 1563 1569
    • (2001) Hum Molec Genet , vol.10 , pp. 1563-1569
    • Yamada, H.1    Saito, F.2    Fukuta-Ohi, H.3
  • 7
    • 0346849958 scopus 로고    scopus 로고
    • Disruption of dystroglycan axis by β-dystroglycan processing in cardiomyopathic hamster muscle
    • K. Matsumura, K. Arai, and D. Zhong Disruption of dystroglycan axis by β-dystroglycan processing in cardiomyopathic hamster muscle Neuromusc Disord 13 2003 796 803
    • (2003) Neuromusc Disord , vol.13 , pp. 796-803
    • Matsumura, K.1    Arai, K.2    Zhong, D.3
  • 8
    • 8244259185 scopus 로고    scopus 로고
    • Identification of the Syrian hamster cardiomyopathy gene
    • V. Nigro, Y. Okazaki, and A. Belsito Identification of the Syrian hamster cardiomyopathy gene Hum Molec Genet 6 1997 601 607
    • (1997) Hum Molec Genet , vol.6 , pp. 601-607
    • Nigro, V.1    Okazaki, Y.2    Belsito, A.3
  • 9
    • 0031471956 scopus 로고    scopus 로고
    • Both hypertrophic and dilated cardiomyopathies are caused by mutation of the same gene, δ-sarcoglycan, in hamster: An animal model of disrupted dystrophin-associated glycoprotein complex
    • A. Sakamoto, K. Ono, and M. Abe Both hypertrophic and dilated cardiomyopathies are caused by mutation of the same gene, δ-sarcoglycan, in hamster: an animal model of disrupted dystrophin-associated glycoprotein complex Proc Natl Acad Sci USA 94 1997 13873 13878
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 13873-13878
    • Sakamoto, A.1    Ono, K.2    Abe, M.3
  • 10
    • 0026757138 scopus 로고
    • Deficiency of the 50K dystrophin-associated glycoprotein in severe childhood autosomal recessive muscular dystrophy
    • K. Matsumura, F.M.S. Tome, and H. Collin Deficiency of the 50K dystrophin-associated glycoprotein in severe childhood autosomal recessive muscular dystrophy Nature 359 1992 320 322
    • (1992) Nature , vol.359 , pp. 320-322
    • Matsumura, K.1    Tome, F.M.S.2    Collin, H.3
  • 11
    • 0032929386 scopus 로고    scopus 로고
    • Multiplex western blotting system for the analysis of muscular dystrophy patients
    • L.V.B. Anderson, and K. Davison Multiplex western blotting system for the analysis of muscular dystrophy patients Am J Pathol 154 1999 1017 1022
    • (1999) Am J Pathol , vol.154 , pp. 1017-1022
    • Anderson, L.V.B.1    Davison, K.2
  • 12
    • 0037388120 scopus 로고    scopus 로고
    • Protein glycosylation in disease: New insights into the congenital muscular dystrophies
    • E. Martin-Rendon, and D.J. Blake Protein glycosylation in disease: new insights into the congenital muscular dystrophies Trends Pharmacol Sci 24 2003 178 183
    • (2003) Trends Pharmacol Sci , vol.24 , pp. 178-183
    • Martin-Rendon, E.1    Blake, D.J.2
  • 13
    • 0141925704 scopus 로고    scopus 로고
    • Glycosylation defects: A new mechanism for muscular dystrophy?
    • P.K. Grewal, and J.E. Hewitt Glycosylation defects: a new mechanism for muscular dystrophy? Hum Molec Genet 12 2003 259 264
    • (2003) Hum Molec Genet , vol.12 , pp. 259-264
    • Grewal, P.K.1    Hewitt, J.E.2
  • 14
    • 1842467267 scopus 로고    scopus 로고
    • Glycosylation in congenital muscular dystrophies
    • T. Endo, and T. Toda Glycosylation in congenital muscular dystrophies Biol Pharm Bull 26 2003 1641 1647
    • (2003) Biol Pharm Bull , vol.26 , pp. 1641-1647
    • Endo, T.1    Toda, T.2
  • 16
    • 0031026624 scopus 로고    scopus 로고
    • Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve α-dystroglycan: The role of a novel mannosyl type oligosaccharide in the binding with laminin
    • A. Chiba, K. Matsumura, and H. Yamada Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve α-dystroglycan: the role of a novel mannosyl type oligosaccharide in the binding 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
  • 17
    • 2942733346 scopus 로고    scopus 로고
    • Molecular recognition by LARGE is essential for expression of functional dystroglycan
    • M. Kanagawa, F. Saito, and S. Kunz 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
  • 18
    • 0027481238 scopus 로고
    • Duchenne muscular dystrophy: Deficiency of dystrophin-associated proteins in the sarcolemma
    • K. Ohlendieck, K. Matsumura, and V.V. Ionasescu Duchenne muscular dystrophy: deficiency of dystrophin-associated proteins in the sarcolemma Neurology 43 1993 795 800
    • (1993) Neurology , vol.43 , pp. 795-800
    • Ohlendieck, K.1    Matsumura, K.2    Ionasescu, V.V.3
  • 19
    • 0037173670 scopus 로고    scopus 로고
    • Post-translational disruption of dystroglycan-ligand interactions in congenital muscular dystrophies
    • D.E. Michele, R. Barresi, and M. Kanagawa 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
  • 20
    • 0033981058 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinases in the muscle of patients with inflammatory myopathies
    • Y.C. Choi, and M.C. Dalakas Expression of matrix metalloproteinases in the muscle of patients with inflammatory myopathies Neurology 54 2000 65 71
    • (2000) Neurology , vol.54 , pp. 65-71
    • Choi, Y.C.1    Dalakas, M.C.2
  • 21
    • 0035122693 scopus 로고    scopus 로고
    • Expression of specific matrix metalloproteinases in inflammatory myopathies
    • B.C. Kieseier, C. Schneider, and J.M. Clements Expression of specific matrix metalloproteinases in inflammatory myopathies Brain 124 2001 341 351
    • (2001) Brain , vol.124 , pp. 341-351
    • Kieseier, B.C.1    Schneider, C.2    Clements, J.M.3
  • 22
    • 0036116405 scopus 로고    scopus 로고
    • Matrix metalloproteinases in inflammatory myopathies: Enhanced immunoreactivity near atrophic myofibers
    • B.G. Schoser, D. Blottner, and H.J. Stuerenburg Matrix metalloproteinases in inflammatory myopathies: enhanced immunoreactivity near atrophic myofibers Acta Neurol Scand 105 2002 309 313
    • (2002) Acta Neurol Scand , vol.105 , pp. 309-313
    • Schoser, B.G.1    Blottner, D.2    Stuerenburg, H.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.