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Volumn 379, Issue 2, 2004, Pages 479-488

Drastic reduction of sarcalumenin in Dp427 (dystrophin of 427 kDa)-deficient fibres indicates that abnormal calcium handling plays a key role in muscular dystrophy

Author keywords

Calcium handling; Dp427 (dystrophin of 427 kDa); Dystrophin; Muscular dystrophy; Sarcalumenin

Indexed keywords

CHROMOSOMES; CROSSLINKING; EXPERIMENTS; FIBERS; FLUORESCENCE; MEMBRANES; MICROSCOPIC EXAMINATION; PROTEINS; REDUCTION;

EID: 2342614190     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20031311     Document Type: Article
Times cited : (69)

References (49)
  • 2
    • 0033939421 scopus 로고    scopus 로고
    • Calcium ion in skeletal muscle: Its crucial role for muscle function, plasticity, and disease
    • Berchtold, M. W., Brinkmeier, H. and Muntener, M. (2000) Calcium ion in skeletal muscle: its crucial role for muscle function, plasticity, and disease. Physiol. Rev. 80. 1215-1265
    • (2000) Physiol. Rev. , vol.80 , pp. 1215-1265
    • Berchtold, M.W.1    Brinkmeier, H.2    Muntener, M.3
  • 4
    • 0036087342 scopus 로고    scopus 로고
    • Function and genetics of dystrophin and dystrophin-related proteins in muscle
    • Blake, D. J., Weir, A., Newey, S. E. and Davies, K. E. (2002) Function and genetics of dystrophin and dystrophin-related proteins in muscle. Physiol. Rev. 82, 291-329
    • (2002) Physiol. Rev. , vol.82 , pp. 291-329
    • Blake, D.J.1    Weir, A.2    Newey, S.E.3    Davies, K.E.4
  • 5
    • 0034468908 scopus 로고    scopus 로고
    • How calcium influx through calcium leak channels is responsible for the elevated levels of calcium-dependent proteolysis in dystrophic myotubes
    • Alderton, J. M. and Steinhardt, R. A. (2000) How calcium influx through calcium leak channels is responsible for the elevated levels of calcium-dependent proteolysis in dystrophic myotubes. Trends Cardiovasc. Med. 10, 268-272
    • (2000) Trends Cardiovasc. Med. , vol.10 , pp. 268-272
    • Alderton, J.M.1    Steinhardt, R.A.2
  • 6
    • 0028914964 scopus 로고
    • Three muscular dystrophies: Loss of cytoskeleton-extracellular matrix linkage
    • Cambridge. Mass.
    • Campbell, K. P. (1995) Three muscular dystrophies: loss of cytoskeleton-extracellular matrix linkage. Cell (Cambridge. Mass.) 80, 675-679
    • (1995) Cell , vol.80 , pp. 675-679
    • Campbell, K.P.1
  • 7
    • 0030026119 scopus 로고    scopus 로고
    • Towards an understanding of the dystrophin-glycoprotein complex: Linkage between the extracellular matrix and the subsarcolemmal membrane cytoskeleton
    • Ohlendieck, K. (1996) Towards an understanding of the dystrophin-glycoprotein complex: linkage between the extracellular matrix and the subsarcolemmal membrane cytoskeleton. Eur. J. Cell Biol. 69, 1-10
    • (1996) Eur. J. Cell Biol. , vol.69 , pp. 1-10
    • Ohlendieck, K.1
  • 8
    • 0027430098 scopus 로고
    • Loss of cytoplasmic basic fibroblast growth factor from physiologically wounded myofibers of normal and dystrophic muscle
    • Clarke, M. S., Khakee, R. and McNeil, P. L. (1993) Loss of cytoplasmic basic fibroblast growth factor from physiologically wounded myofibers of normal and dystrophic muscle. J. Cell Sci. 106, 121-133
    • (1993) J. Cell Sci. , vol.106 , pp. 121-133
    • Clarke, M.S.1    Khakee, R.2    McNeil, P.L.3
  • 9
    • 12244272395 scopus 로고    scopus 로고
    • Prevention of pathology in mdx mice by expression of utrophin: Analysis using an inducible transgenic expression system
    • Squire, S., Raymackers, J. M., Vandebrouck, C., Potter, A., Tinsley, J., Fisher, R., Gillis, J. M. and Davies, K. E. (2002) Prevention of pathology in mdx mice by expression of utrophin: analysis using an inducible transgenic expression system. Hum. Mol. Genet. 11, 3333-3344
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 3333-3344
    • Squire, S.1    Raymackers, J.M.2    Vandebrouck, C.3    Potter, A.4    Tinsley, J.5    Fisher, R.6    Gillis, J.M.7    Davies, K.E.8
  • 11
    • 0034737602 scopus 로고    scopus 로고
    • Calcium influx through calcium leak channels is responsible for the elevated levels of calcium-dependent proteolysis in dystrophic myotubes
    • Alderton, J. M. and Steinhardt, R. A. (2000) Calcium influx through calcium leak channels is responsible for the elevated levels of calcium-dependent proteolysis in dystrophic myotubes. J. Biol. Chem. 275, 9452-9460
    • (2000) J. Biol. Chem. , vol.275 , pp. 9452-9460
    • Alderton, J.M.1    Steinhardt, R.A.2
  • 13
    • 0037119993 scopus 로고    scopus 로고
    • Involvement of TRPC in the abnormal calcium influx observed in dystrophic (mdx) mouse skeletal muscle fibers
    • Vandebrouck, C., Martin, D., Colson-Van Schoor, M., Debaix, H. and Gailly, P. (2002) Involvement of TRPC in the abnormal calcium influx observed in dystrophic (mdx) mouse skeletal muscle fibers. J. Cell Biol. 158, 1089-1096
    • (2002) J. Cell Biol. , vol.158 , pp. 1089-1096
    • Vandebrouck, C.1    Martin, D.2    Colson-Van Schoor, M.3    Debaix, H.4    Gailly, P.5
  • 14
    • 12244249139 scopus 로고    scopus 로고
    • Intramembrane charge movement and L-type calcium current in skeletal muscle fibers isolated from control and mdx mice
    • Collet, C., Csernoch, L. and Jacquemond, V. (2003) Intramembrane charge movement and L-type calcium current in skeletal muscle fibers isolated from control and mdx mice. Biophys. J. 84, 251-265
    • (2003) Biophys. J. , vol.84 , pp. 251-265
    • Collet, C.1    Csernoch, L.2    Jacquemond, V.3
  • 15
    • 0037677267 scopus 로고    scopus 로고
    • Use of continuous-elution gel electrophoresis as a preparative tool for blot overlay analysis
    • Mulvey, C. and Ohlendieck, K. (2003) Use of continuous-elution gel electrophoresis as a preparative tool for blot overlay analysis. Anal. Biochem. 319, 122-130
    • (2003) Anal. Biochem. , vol.319 , pp. 122-130
    • Mulvey, C.1    Ohlendieck, K.2
  • 16
    • 0036092560 scopus 로고    scopus 로고
    • Drastic reduction of calsequestrin-like proteins and impaired calcium binding in dystrophic mdx muscle
    • Culligan, K., Banville, N., Dowling, P. and Ohlendieck, K. (2002) Drastic reduction of calsequestrin-like proteins and impaired calcium binding in dystrophic mdx muscle. J. Appl. Physiol. 92, 435-445
    • (2002) J. Appl. Physiol. , vol.92 , pp. 435-445
    • Culligan, K.1    Banville, N.2    Dowling, P.3    Ohlendieck, K.4
  • 17
    • 2342558309 scopus 로고
    • Molecular cloning and expression of cDNA encoding a lumenal calcium binding glycoprotein from sarcoplasmic reticulum
    • Leberer, E., Charuk, J. H., Green, N. M. and MacLennan, D. H. (1989) Molecular cloning and expression of cDNA encoding a lumenal calcium binding glycoprotein from sarcoplasmic reticulum. Proc. Natl. Acad. Sci. U.S.A. 88, 6047-6051
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 6047-6051
    • Leberer, E.1    Charuk, J.H.2    Green, N.M.3    MacLennan, D.H.4
  • 18
    • 0038823857 scopus 로고    scopus 로고
    • Comparative analysis of Dp427-deficient mdx tissues shows that the milder dystrophic phenotype of extraocular and toe muscle fibres is associated with a persistent expression of β-dystroglycan
    • Dowling, P., Lohan, J. and Ohlendleck, K. (2003) Comparative analysis of Dp427-deficient mdx tissues shows that the milder dystrophic phenotype of extraocular and toe muscle fibres is associated with a persistent expression of β-dystroglycan. Eur. J. Cell Biol. 82, 222-230
    • (2003) Eur. J. Cell Biol. , vol.82 , pp. 222-230
    • Dowling, P.1    Lohan, J.2    Ohlendleck, K.3
  • 19
    • 0025280251 scopus 로고
    • Purification, calcium binding properties, and ultrastructural localization of the 53 000- and 160 000 (sarcalumenin)-dalton glycoproteins of the sarcoplasmic reticulum
    • Leberer, E., Timms, B. G., Campbell, K. P. and MacLennan, D. H. (1990) Purification, calcium binding properties, and ultrastructural localization of the 53 000- and 160 000 (sarcalumenin)-dalton glycoproteins of the sarcoplasmic reticulum. J. Biol. Chem. 265, 10118-10124
    • (1990) J. Biol. Chem. , vol.265 , pp. 10118-10124
    • Leberer, E.1    Timms, B.G.2    Campbell, K.P.3    MacLennan, D.H.4
  • 20
    • 0026316261 scopus 로고
    • Analysis of excitation-contraction-coupling components in chronically stimulated canine skeletal muscle
    • Ohlendieck, K., Briggs, F. N., Lee, K. F., Wechsler, A. W. and Campbell, K. P. (1991) Analysis of excitation-contraction-coupling components in chronically stimulated canine skeletal muscle. Eur. J. Biochem. 202, 739-747
    • (1991) Eur. J. Biochem. , vol.202 , pp. 739-747
    • Ohlendieck, K.1    Briggs, F.N.2    Lee, K.F.3    Wechsler, A.W.4    Campbell, K.P.5
  • 22
    • 0024403297 scopus 로고
    • Calcium transport by sarcoplasmic reticulum of skeletal muscle is inhibited by antibodies against the 53-kilodalton glycoprotein of the sarcoplasmic reticulum membrane
    • Kutchai, H. and Campbell, K. P. (1989) Calcium transport by sarcoplasmic reticulum of skeletal muscle is inhibited by antibodies against the 53-kilodalton glycoprotein of the sarcoplasmic reticulum membrane. Biochemistry 28, 4830-4839
    • (1989) Biochemistry , vol.28 , pp. 4830-4839
    • Kutchai, H.1    Campbell, K.P.2
  • 23
    • 0030583220 scopus 로고    scopus 로고
    • The identification of the phosphorylated 150/160-kDa proteins of sarcoplasmic reticulum, their kinase and their association with the ryanodine receptor
    • Shoshan-Barmatz, V., Orr, I., Weil, S., Meyer, H., Varsanyi, M. and Heilmeyer, L. M. (1996) The identification of the phosphorylated 150/160-kDa proteins of sarcoplasmic reticulum, their kinase and their association with the ryanodine receptor. Biochim. Biophys. Acta 1283, 89-100
    • (1996) Biochim. Biophys. Acta , vol.1283 , pp. 89-100
    • Shoshan-Barmatz, V.1    Orr, I.2    Weil, S.3    Meyer, H.4    Varsanyi, M.5    Heilmeyer, L.M.6
  • 26
    • 0033982278 scopus 로고    scopus 로고
    • Delay of muscle degeneration and necrosis in mdx mice by calpain inhibition
    • Badalamente, W. A. and Stracher, A. (2000) Delay of muscle degeneration and necrosis in mdx mice by calpain inhibition. Muscle Nerve 23, 106-111
    • (2000) Muscle Nerve , vol.23 , pp. 106-111
    • Badalamente, W.A.1    Stracher, A.2
  • 27
    • 0036798005 scopus 로고    scopus 로고
    • Overexpression of a calpastatin transgene in mdx muscle reduces dystrophic pathology
    • Spencer, M. J. and Mellgren, R. L. (2002) Overexpression of a calpastatin transgene in mdx muscle reduces dystrophic pathology. Hum. Mol. Genet 11, 2645-2655
    • (2002) Hum. Mol. Genet , vol.11 , pp. 2645-2655
    • Spencer, M.J.1    Mellgren, R.L.2
  • 31
    • 0032934834 scopus 로고    scopus 로고
    • Self-aggregation of triadin in the sarcoplasmic reticulum of rabbit skeletal muscle
    • Froemming, G. R., Murray, B. E. and Ohlendieck, K. (1999) Self-aggregation of triadin in the sarcoplasmic reticulum of rabbit skeletal muscle. Biochim. Biophys. Acta 1418, 197-205
    • (1999) Biochim. Biophys. Acta , vol.1418 , pp. 197-205
    • Froemming, G.R.1    Murray, B.E.2    Ohlendieck, K.3
  • 32
    • 0035106676 scopus 로고    scopus 로고
    • The native dihydropyridine receptor exists as a supramolecular complex in skeletal muscle
    • Froemming, G. R. and Ohlendieck, K. (2001) The native dihydropyridine receptor exists as a supramolecular complex in skeletal muscle. Cell. Mol. Life Sci. 58, 312-320
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 312-320
    • Froemming, G.R.1    Ohlendieck, K.2
  • 33
    • 0027350105 scopus 로고
    • Separation and analysis of membrane proteins by SDS-polyacrylamide gel electrophoresis
    • Bradd, S. J. and Ounn, M. J. (1993) Separation and analysis of membrane proteins by SDS-polyacrylamide gel electrophoresis. Methods Mol. Biol. 19, 203-210
    • (1993) Methods Mol. Biol. , vol.19 , pp. 203-210
    • Bradd, S.J.1    Ounn, M.J.2
  • 34
    • 0020643575 scopus 로고
    • 2+-binding proteins, calsequestrin, calmodulin, troponin C, and S-100, with the cationic carbocyanine dye 'Stains-all'
    • 2+-binding proteins, calsequestrin, calmodulin, troponin C, and S-100, with the cationic carbocyanine dye 'Stains-all'. J. Biol. Chem. 258, 11267-11273
    • (1983) J. Biol. Chem. , vol.258 , pp. 11267-11273
    • Campbell, K.P.1    MacLennan, D.H.2    Jorgensen, A.O.3
  • 35
    • 0030968771 scopus 로고    scopus 로고
    • Cross-linking analysis of the ryanodine receptor and α1- dihydropyridine receptor in rabbit skeletal muscle
    • Murray, B. E. and Ohlendieck, K. (1997) Cross-linking analysis of the ryanodine receptor and α1-dihydropyridine receptor in rabbit skeletal muscle. Biochem. J. 324, 689-696
    • (1997) Biochem. J. , vol.324 , pp. 689-696
    • Murray, B.E.1    Ohlendieck, K.2
  • 36
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 39
    • 0036188005 scopus 로고    scopus 로고
    • Distal mdx muscle groups exhibiting up-regulation of utrophin and rescue of dystrophin-associated glycoproteins exemplify a protected phenotype in muscular dystrophy
    • Dowling, P., Culligan, K. and Ohlendieck, K. (2002) Distal mdx muscle groups exhibiting up-regulation of utrophin and rescue of dystrophin-associated glycoproteins exemplify a protected phenotype in muscular dystrophy. Naturwissenschaften 89, 75-88
    • (2002) Naturwissenschaften , vol.89 , pp. 75-88
    • Dowling, P.1    Culligan, K.2    Ohlendieck, K.3
  • 40
    • 0033527403 scopus 로고    scopus 로고
    • 2+ binding protein) resides in the lumen of the sarcoplasmic reticulum as a multimer
    • 2+ binding protein) resides in the lumen of the sarcoplasmic reticulum as a multimer. Biochem. Biophys. Res. Commun. 263, 667-671
    • (1999) Biochem. Biophys. Res. Commun. , vol.263 , pp. 667-671
    • Suk, J.Y.1    Kim, Y.S.2    Park, W.J.3
  • 41
    • 0037160782 scopus 로고    scopus 로고
    • The muscular dystrophies
    • Emery, A. E. (2002) The muscular dystrophies. Lancet 359, 687-695
    • (2002) Lancet , vol.359 , pp. 687-695
    • Emery, A.E.1
  • 43
    • 0032698773 scopus 로고    scopus 로고
    • Muscular dystrophy. Identification and use of genes for diagnostics and therapeutics
    • Hoffman, E. P. (1999) Muscular dystrophy. Identification and use of genes for diagnostics and therapeutics. Arch. Pathol. Lab. Med. 123, 1050-1052
    • (1999) Arch. Pathol. Lab. Med. , vol.123 , pp. 1050-1052
    • Hoffman, E.P.1
  • 44
    • 0036021778 scopus 로고    scopus 로고
    • Functional characteristics of dystrophic skeletal muscle: Insights from animal models
    • Watchko, J. F., O'Day, T. L. and Hoffman, E. P. (2002) Functional characteristics of dystrophic skeletal muscle: insights from animal models. J. Appl. Physiol. 93, 407-417
    • (2002) J. Appl. Physiol. , vol.93 , pp. 407-417
    • Watchko, J.F.1    O'Day, T.L.2    Hoffman, E.P.3
  • 45
    • 0027281140 scopus 로고
    • Proteotysis results in altered leak channel kinetics and elevated free calcium in mdx muscle
    • Turner, P. R., Schutz, R., Ganguly, B. and Steinhardt, R. A. (1993) Proteotysis results in altered leak channel kinetics and elevated free calcium in mdx muscle. J. Membr. Biol. 133, 243-251
    • (1993) J. Membr. Biol. , vol.133 , pp. 243-251
    • Turner, P.R.1    Schutz, R.2    Ganguly, B.3    Steinhardt, R.A.4
  • 47
    • 0034659815 scopus 로고    scopus 로고
    • Proteomics to study genes and genomes
    • Pandey, A. and Mann, M. (2000) Proteomics to study genes and genomes. Nature (London) 405, 837-846
    • (2000) Nature (London) , vol.405 , pp. 837-846
    • Pandey, A.1    Mann, M.2
  • 48
    • 0037023852 scopus 로고    scopus 로고
    • Proteomic analysis of striated muscle
    • Isfort, R. J. (2002) Proteomic analysis of striated muscle. J. Chromatogr. B 771, 155-165
    • (2002) J. Chromatogr. B , vol.771 , pp. 155-165
    • Isfort, R.J.1
  • 49
    • 0025881734 scopus 로고
    • Dystrophin constitutes 5 % of membrane cytoskeleton in skeletal muscle
    • Ohlendieck, K. and Campbell, K. P. (1991) Dystrophin constitutes 5 % of membrane cytoskeleton in skeletal muscle. FEBS Lett. 283, 230-234
    • (1991) FEBS Lett. , vol.283 , pp. 230-234
    • Ohlendieck, K.1    Campbell, K.P.2


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