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Volumn 246, Issue 2, 1999, Pages 433-442

Potential m-calpain substrates during myoblast fusion

Author keywords

Antisense oligodeoxyribonucleotides; Calpain inhibitors; Desmin; Fibronectin; Fusion; M calpain; Myoblast culture; Talin; Vimentin

Indexed keywords

ANTISENSE OLIGONUCLEOTIDE; CALPAIN; CALPASTATIN; DESMIN; MEMBRANE PROTEIN; TALIN; TYLOXAPOL; VIMENTIN;

EID: 0033080465     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.1998.4325     Document Type: Article
Times cited : (56)

References (36)
  • 2
    • 0025831476 scopus 로고
    • Calcium-activated neutral proteases (calpain) system: Structure, function and regulation
    • Croall D. E., Demartino G. N. Calcium-activated neutral proteases (calpain) system: Structure, function and regulation. Physiol. Rev. 71:1991;813-847.
    • (1991) Physiol. Rev. , vol.71 , pp. 813-847
    • Croall, D.E.1    Demartino, G.N.2
  • 4
    • 0022885854 scopus 로고
    • Possible role of calpain I and calpain II in differentiating muscle
    • Schollmeyer J. E. Possible role of calpain I and calpain II in differentiating muscle. Exp. Cell Res. 163:1986;413-422.
    • (1986) Exp. Cell Res. , vol.163 , pp. 413-422
    • Schollmeyer, J.E.1
  • 5
    • 0027728978 scopus 로고
    • Quantitative measurement of calpain I and II mRNAs in differentiating rat muscle cells using a competitive polymerase chain reaction method
    • Poussard S., Cottin P., Brustis J. J., Talmat S., Elamrani N., Ducastaing A. Quantitative measurement of calpain I and II mRNAs in differentiating rat muscle cells using a competitive polymerase chain reaction method. Biochimie. 75:1993;885-890.
    • (1993) Biochimie , vol.75 , pp. 885-890
    • Poussard, S.1    Cottin, P.2    Brustis, J.J.3    Talmat, S.4    Elamrani, N.5    Ducastaing, A.6
  • 11
    • 0027535597 scopus 로고
    • Increase in the level of m-calpain correlates with the elevated cleavage of filamin during myogenic differentiation of embryonic muscle cells
    • Kwak K. B., Chung S. S., Kim O. M., Kang M. S., Ha D. B., Chung C. H. Increase in the level of m-calpain correlates with the elevated cleavage of filamin during myogenic differentiation of embryonic muscle cells. Biochim. Biophys. Acta. 1175:1993;243-249.
    • (1993) Biochim. Biophys. Acta , vol.1175 , pp. 243-249
    • Kwak, K.B.1    Chung, S.S.2    Kim, O.M.3    Kang, M.S.4    Ha, D.B.5    Chung, C.H.6
  • 13
    • 0023661249 scopus 로고
    • Colocalization of calcium-dependent protease II and one of its substrates at sites of cell adhesion
    • Beckerle M. C., Burridge K., De Martino G. N., Croall D. E. Colocalization of calcium-dependent protease II and one of its substrates at sites of cell adhesion. Cell. 51:1987;569-577.
    • (1987) Cell , vol.51 , pp. 569-577
    • Beckerle, M.C.1    Burridge, K.2    De Martino, G.N.3    Croall, D.E.4
  • 15
    • 0026674188 scopus 로고
    • Transmembrane signaling by integrins
    • Schwartz M. A. Transmembrane signaling by integrins. Trends Cell Biol. 2:1992;304-308.
    • (1992) Trends Cell Biol. , vol.2 , pp. 304-308
    • Schwartz, M.A.1
  • 16
    • 0020490735 scopus 로고
    • Purification and properties of human platelet P235. A high molecular weight protein substrate of endogenous calcium-activated protease(s)
    • Collier N. C., Wang K. Purification and properties of human platelet P235. A high molecular weight protein substrate of endogenous calcium-activated protease(s). J. Biol. Chem. 257:1982;6937-6943.
    • (1982) J. Biol. Chem. , vol.257 , pp. 6937-6943
    • Collier, N.C.1    Wang, K.2
  • 18
    • 0344147309 scopus 로고
    • Identification of talin as a major cytoplasmic protein implicated in platelet activation
    • O'Halloran T., Beckerle M. C., Burridge K. Identification of talin as a major cytoplasmic protein implicated in platelet activation. Nature. 312:1985;566-570.
    • (1985) Nature , vol.312 , pp. 566-570
    • O'Halloran, T.1    Beckerle, M.C.2    Burridge, K.3
  • 21
    • 0027988820 scopus 로고
    • Calpain inhibition: An overview of its therapeutic potential
    • Wang K. K. W., Yuen P. W. Calpain inhibition: An overview of its therapeutic potential. Trends Pharmacol. Sci. 15:1994;412-419.
    • (1994) Trends Pharmacol. Sci. , vol.15 , pp. 412-419
    • Wang, K.K.W.1    Yuen, P.W.2
  • 22
    • 0024990759 scopus 로고
    • Sequence and domain structure of talin
    • Rees D. J., Ades S. E., Singer S. J., Hynes R. O. Sequence and domain structure of talin. Nature. 347:1990;685-689.
    • (1990) Nature , vol.347 , pp. 685-689
    • Rees, D.J.1    Ades, S.E.2    Singer, S.J.3    Hynes, R.O.4
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0027665765 scopus 로고
    • Assembly of intermediate filaments
    • Shoeman R. L., Traub P. Assembly of intermediate filaments. BioAssays. 15:1993;605-611.
    • (1993) BioAssays , vol.15 , pp. 605-611
    • Shoeman, R.L.1    Traub, P.2
  • 27
    • 0019842813 scopus 로고
    • All classes of intermediate filaments share a common antigenic determinant defined by a monoclonal antibody
    • Pruss R. M., Mirsky R., Raff M. C., Thorpe R., Dowding A. J., Anderton B. H. All classes of intermediate filaments share a common antigenic determinant defined by a monoclonal antibody. Cell. 27:1981;419-428.
    • (1981) Cell , vol.27 , pp. 419-428
    • Pruss, R.M.1    Mirsky, R.2    Raff, M.C.3    Thorpe, R.4    Dowding, A.J.5    Anderton, B.H.6
  • 28
    • 0019588235 scopus 로고
    • Comparison of the proteins of two immunologically distinct intermediate filaments by amino acid sequence analysis: Desmin and vimentin
    • Geisler N., Weber K. Comparison of the proteins of two immunologically distinct intermediate filaments by amino acid sequence analysis: Desmin and vimentin. Proc. Natl. Acad. Sci. USA. 78:1981;4120-4123.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 4120-4123
    • Geisler, N.1    Weber, K.2
  • 30
    • 0025865925 scopus 로고
    • High level desmin expression depends on a muscle-specific enhancer
    • Li Z., Paulin D. High level desmin expression depends on a muscle-specific enhancer. J. Biol. Chem. 266:1991;6562-6570.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6562-6570
    • Li, Z.1    Paulin, D.2
  • 31
  • 32
    • 0027453032 scopus 로고
    • Desmin sequence elements regulating skeletal muscle-specific expression in transgenic mice
    • Li Z., Marchand P., Humbert J., Babinet C., Paulin D. Desmin sequence elements regulating skeletal muscle-specific expression in transgenic mice. Development. 117:1993;947-959.
    • (1993) Development , vol.117 , pp. 947-959
    • Li, Z.1    Marchand, P.2    Humbert, J.3    Babinet, C.4    Paulin, D.5
  • 33
    • 0030718545 scopus 로고    scopus 로고
    • Interaction of cytoskeletal proteins with membrane lipids
    • Isenberg G., Niggli V. Interaction of cytoskeletal proteins with membrane lipids. Int. Rev. Cytol. 178:1998;73-124.
    • (1998) Int. Rev. Cytol. , vol.178 , pp. 73-124
    • Isenberg, G.1    Niggli, V.2
  • 34
    • 0017687232 scopus 로고
    • Increased membrane fluidity precedes fusion of muscle cells
    • Prives J., Stinitsky M. Increased membrane fluidity precedes fusion of muscle cells. Nature. 268:1977;761-763.
    • (1977) Nature , vol.268 , pp. 761-763
    • Prives, J.1    Stinitsky, M.2
  • 35
    • 0018356877 scopus 로고
    • Membrane events in myoblasts fusion
    • Kalderon N., Gilula N. B. Membrane events in myoblasts fusion. J. Cell Biol. 81:1979;411-425.
    • (1979) J. Cell Biol. , vol.81 , pp. 411-425
    • Kalderon, N.1    Gilula, N.B.2
  • 36
    • 0022426155 scopus 로고
    • The fusion of myoblasts
    • Wakelam M. J. O. The fusion of myoblasts. Biochem. J. 228:1985;1-12.
    • (1985) Biochem. J. , vol.228 , pp. 1-12
    • Wakelam, M.J.O.1


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