메뉴 건너뛰기




Volumn 404, Issue 2, 2010, Pages 197-203

Mass spectrometric identification of dystrophin isoform Dp427 by on-membrane digestion of sarcolemma from skeletal muscle

Author keywords

Dystrophin; Muscle proteomics; On membrane digestion; Sarcoglycan; Sarcolemma; Syntrophin

Indexed keywords

ELECTROPHORESIS; GLYCOPROTEINS; MASS SPECTROMETERS; MASS SPECTROMETRY; MEMBRANES; MUSCLE; PROTEOMICS;

EID: 77954457960     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2010.05.017     Document Type: Article
Times cited : (36)

References (28)
  • 1
    • 0028914964 scopus 로고
    • Three muscular dystrophies: loss of cytoskeleton-extracellular matrix linkage
    • Campbell K.P. Three muscular dystrophies: loss of cytoskeleton-extracellular matrix linkage. Cell 1995, 80:675-679.
    • (1995) Cell , vol.80 , pp. 675-679
    • Campbell, K.P.1
  • 2
    • 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. Towards an understanding of the dystrophin-glycoprotein complex: linkage between the extracellular matrix and the subsarcolemmal membrane cytoskeleton. Eur. J. Cell Biol. 1996, 69:1-10.
    • (1996) Eur. J. Cell Biol. , vol.69 , pp. 1-10
    • Ohlendieck, K.1
  • 3
    • 38949130017 scopus 로고    scopus 로고
    • Biology of the striated muscle dystrophin-glycoprotein complex
    • Ervasti J.M., Sonnemann K.J. Biology of the striated muscle dystrophin-glycoprotein complex. Int. Rev. Cytol. 2008, 265:191-225.
    • (2008) Int. Rev. Cytol. , vol.265 , pp. 191-225
    • Ervasti, J.M.1    Sonnemann, K.J.2
  • 4
    • 0025217703 scopus 로고
    • Detailed analysis of the repeat domain of dystrophin reveals four potential hinge segments that may confer flexibility
    • Koenig M., Kunkel L.M. Detailed analysis of the repeat domain of dystrophin reveals four potential hinge segments that may confer flexibility. J. Biol. Chem. 1990, 265:4560-4566.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4560-4566
    • Koenig, M.1    Kunkel, L.M.2
  • 6
    • 0142182391 scopus 로고    scopus 로고
    • Proteomic analysis of mdx skeletal muscle: great reduction of adenylate kinase 1 expression and enzymatic activity
    • Ge Y., Molloy M.P., Chamberlain J.S., Andrews P.C. Proteomic analysis of mdx skeletal muscle: great reduction of adenylate kinase 1 expression and enzymatic activity. Proteomics 2003, 3:1895-1903.
    • (2003) Proteomics , vol.3 , pp. 1895-1903
    • Ge, Y.1    Molloy, M.P.2    Chamberlain, J.S.3    Andrews, P.C.4
  • 8
    • 33646102225 scopus 로고    scopus 로고
    • Reduced expression of regucalcin in young and aged mdx diaphragm indicates abnormal cytosolic calcium handling in dystrophin-deficient muscle
    • Doran P., Dowling P., Donoghue P., Buffini M., Ohlendieck K. Reduced expression of regucalcin in young and aged mdx diaphragm indicates abnormal cytosolic calcium handling in dystrophin-deficient muscle. Biochim. Biophys. Acta 2006, 1764:773-785.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 773-785
    • Doran, P.1    Dowling, P.2    Donoghue, P.3    Buffini, M.4    Ohlendieck, K.5
  • 9
    • 33748339008 scopus 로고    scopus 로고
    • Proteome analysis of the dystrophin-deficient MDX diaphragm reveals a drastic increase in the heat shock protein cvHSP
    • Doran P., Martin G., Dowling P., Jockusch H., Ohlendieck K. Proteome analysis of the dystrophin-deficient MDX diaphragm reveals a drastic increase in the heat shock protein cvHSP. Proteomics 2006, 6:4610-4621.
    • (2006) Proteomics , vol.6 , pp. 4610-4621
    • Doran, P.1    Martin, G.2    Dowling, P.3    Jockusch, H.4    Ohlendieck, K.5
  • 11
    • 10644230916 scopus 로고    scopus 로고
    • Current two-dimensional electrophoresis technology for proteomics
    • Goerg A., Weiss W., Dunn M.J. Current two-dimensional electrophoresis technology for proteomics. Proteomics 2004, 4:3665-3685.
    • (2004) Proteomics , vol.4 , pp. 3665-3685
    • Goerg, A.1    Weiss, W.2    Dunn, M.J.3
  • 12
    • 33748571491 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis as tool for proteomics studies in combination with protein identification by mass spectrometry
    • Wittmann-Liebold B., Graack H.R., Pohl T. Two-dimensional gel electrophoresis as tool for proteomics studies in combination with protein identification by mass spectrometry. Proteomics 2006, 6:4688-4703.
    • (2006) Proteomics , vol.6 , pp. 4688-4703
    • Wittmann-Liebold, B.1    Graack, H.R.2    Pohl, T.3
  • 14
    • 33746263851 scopus 로고    scopus 로고
    • Use of nitrocellulose membranes for protein characterization by matrix-assisted laser desorption/ionization mass spectrometry
    • Luque-Garcia J.L., Zhou G., Sun T.T., Neubert T.A. Use of nitrocellulose membranes for protein characterization by matrix-assisted laser desorption/ionization mass spectrometry. Anal. Chem. 2006, 78:5102-5108.
    • (2006) Anal. Chem. , vol.78 , pp. 5102-5108
    • Luque-Garcia, J.L.1    Zhou, G.2    Sun, T.T.3    Neubert, T.A.4
  • 15
    • 39749084477 scopus 로고    scopus 로고
    • Analysis of electroblotted proteins by mass spectrometry: protein identification after Western blotting
    • Luque-Garcia J.L., Zhou G., Spellman D.S., Tung-Tien S., Neubert T.A. Analysis of electroblotted proteins by mass spectrometry: protein identification after Western blotting. Mol. Cell. Proteomics 2008, 7:308-314.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 308-314
    • Luque-Garcia, J.L.1    Zhou, G.2    Spellman, D.S.3    Tung-Tien, S.4    Neubert, T.A.5
  • 16
    • 0023430927 scopus 로고
    • Internal amino acid sequence analysis of proteins separated by one- or two-dimensional gel electrophoresis after in situ protease digestion on nitrocellulose
    • Aebersold R.H., Leavitt J., Saavedra R.A., Hood L.E., Kent S.B. Internal amino acid sequence analysis of proteins separated by one- or two-dimensional gel electrophoresis after in situ protease digestion on nitrocellulose. Proc. Natl. Acad. Sci. USA 1987, 84:6970-6974.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6970-6974
    • Aebersold, R.H.1    Leavitt, J.2    Saavedra, R.A.3    Hood, L.E.4    Kent, S.B.5
  • 17
    • 67649171407 scopus 로고    scopus 로고
    • On-membrane tryptic digestion of proteins for mass spectrometry analysis
    • Luque-Garcia J.L., Neubert T.A. On-membrane tryptic digestion of proteins for mass spectrometry analysis. Methods Mol. Biol. 2009, 536:331-341.
    • (2009) Methods Mol. Biol. , vol.536 , pp. 331-341
    • Luque-Garcia, J.L.1    Neubert, T.A.2
  • 18
    • 0026067790 scopus 로고
    • Dystrophin glycoprotein complex is highly enriched in skeletal muscle sarcolemma
    • Ohlendieck K., Ervasti J.M., Snook J.B., Campbell K.P. Dystrophin glycoprotein complex is highly enriched in skeletal muscle sarcolemma. J. Cell Biol. 1991, 112:135-148.
    • (1991) J. Cell Biol. , vol.112 , pp. 135-148
    • Ohlendieck, K.1    Ervasti, J.M.2    Snook, J.B.3    Campbell, K.P.4
  • 19
    • 0025881734 scopus 로고
    • Dystrophin constitutes 5% of membrane cytoskeleton in skeletal muscle
    • Ohlendieck K., Campbell K.P. Dystrophin constitutes 5% of membrane cytoskeleton in skeletal muscle. FEBS Lett. 1991, 283:230-234.
    • (1991) FEBS Lett. , vol.283 , pp. 230-234
    • Ohlendieck, K.1    Campbell, K.P.2
  • 20
    • 0030568868 scopus 로고    scopus 로고
    • Membrane cytoskeletal characterisation of utrophin in highly purified sarcolemma vesicles
    • Ohlendieck K. Membrane cytoskeletal characterisation of utrophin in highly purified sarcolemma vesicles. Biochim. Biophys. Acta 1996, 1283:215-222.
    • (1996) Biochim. Biophys. Acta , vol.1283 , pp. 215-222
    • Ohlendieck, K.1
  • 21
    • 0025272250 scopus 로고
    • Deficiency of a glycoprotein component of the dystrophin complex in dystrophic muscle
    • Ervasti J.M., Ohlendieck K., Kahl S.D., Gaver M.G., Campbell K.P. Deficiency of a glycoprotein component of the dystrophin complex in dystrophic muscle. Nature 1990, 345:315-319.
    • (1990) Nature , vol.345 , pp. 315-319
    • Ervasti, J.M.1    Ohlendieck, K.2    Kahl, S.D.3    Gaver, M.G.4    Campbell, K.P.5
  • 22
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko A., Tomas H., Havlis J., Olsen J.V., Mann M. In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat. Protoc. 2006, 1:2856-2860.
    • (2006) Nat. Protoc. , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 23
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins D.N., Pappin D.J., Creasy D.M., Cottrell J.S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999, 20:3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 26
    • 0037023852 scopus 로고    scopus 로고
    • Proteomic analysis of striated muscle
    • Isfort R.J. Proteomic analysis of striated muscle. J. Chromatogr. B 2002, 771:155-165.
    • (2002) J. Chromatogr. B , vol.771 , pp. 155-165
    • Isfort, R.J.1
  • 27
    • 77950795909 scopus 로고    scopus 로고
    • Proteomics of skeletal muscle differentiation, neuromuscular disorders, and aging
    • Ohlendieck K. Proteomics of skeletal muscle differentiation, neuromuscular disorders, and aging. Expert Rev. Proteomics 2010, 7:283-296.
    • (2010) Expert Rev. Proteomics , vol.7 , pp. 283-296
    • Ohlendieck, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.