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Volumn 288, Issue 40, 2013, Pages 28925-28935

Decreasing tropomyosin phosphorylation rescues tropomyosin-induced familial hypertrophic cardiomyopathy

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CALCIUM;

EID: 84885107602     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.466466     Document Type: Article
Times cited : (20)

References (57)
  • 1
    • 0027285642 scopus 로고
    • Developmental analysis of tropomyosin gene expression in embryonic stem cells and mouse embryos
    • Muthuchamy, M., Pajak, L., Howles, P., Doetschman, T., and Wieczorek, D. F. (1993) Developmental analysis of tropomyosin gene expression in embryonic stem cells and mouse embryos. Mol. Cell. Biol. 13, 3311-3323
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 3311-3323
    • Muthuchamy, M.1    Pajak, L.2    Howles, P.3    Doetschman, T.4    Wieczorek, D.F.5
  • 2
    • 0017864059 scopus 로고
    • Specific phosphorylation at serine-283 of tropomyosin from frog skeletal and rabbit skeletal and cardiac muscle
    • Mak, A., Smillie, L. B., and Bárány, M. (1978) Specific phosphorylation at serine-283 of tropomyosin from frog skeletal and rabbit skeletal and cardiac muscle. Proc. Natl. Acad. Sci. U.S.A. 75, 3588-3592
    • (1978) Proc. Natl. Acad. Sci. U.S.A. , vol.75 , pp. 3588-3592
    • Mak, A.1    Smillie, L.B.2    Bárány, M.3
  • 3
    • 0021337345 scopus 로고
    • In vitro phosphorylation of tropomyosin by a kinase from chicken embryo
    • Montgomery, K., and Mak, A. S. (1984) In vitro phosphorylation of tropomyosin by a kinase from chicken embryo. J. Biol. Chem. 259, 5555-5560
    • (1984) J. Biol. Chem. , vol.259 , pp. 5555-5560
    • Montgomery, K.1    Mak, A.S.2
  • 5
    • 46749104084 scopus 로고    scopus 로고
    • Myofilament proteins: From cardiac disorders to proteomic changes
    • Yuan, C., and Solaro, R. J. (2008) Myofilament proteins: from cardiac disorders to proteomic changes. Proteomics Clin. Appl. 2, 788-799
    • (2008) Proteomics Clin. Appl. , vol.2 , pp. 788-799
    • Yuan, C.1    Solaro, R.J.2
  • 6
    • 0015858368 scopus 로고
    • Phosphorylation of cardiac native tropomyosin and troponin: Inhibitory effect of actomyosin and possible presence of endogenous myofibrillar-located cyclic-AMP-dependent protein kinase
    • Reddy, Y. S., Ballard, D., Giri, N. Y., and Schwartz, A. (1973) Phosphorylation of cardiac native tropomyosin and troponin: inhibitory effect of actomyosin and possible presence of endogenous myofibrillar-located cyclic-AMP-dependent protein kinase. J. Mol. Cell. Cardiol. 5, 461-471
    • (1973) J. Mol. Cell. Cardiol. , vol.5 , pp. 461-471
    • Reddy, Y.S.1    Ballard, D.2    Giri, N.Y.3    Schwartz, A.4
  • 7
    • 0023657783 scopus 로고
    • Isolation and characterization of tropomyosin kinase from chicken embryo
    • deBelle, I., and Mak, A. S. (1987) Isolation and characterization of tropomyosin kinase from chicken embryo. Biochim. Biophys. Acta 925, 17-26
    • (1987) Biochim. Biophys. Acta , vol.925 , pp. 17-26
    • Debelle, I.1    Mak, A.S.2
  • 9
    • 38149014016 scopus 로고    scopus 로고
    • Use of 2-D DIGE analysis reveals altered phosphorylation in a tropomyosin mutant (Glu54Lys) linked to dilated cardiomyopathy
    • Warren, C. M., Arteaga, G. M., Rajan, S., Ahmed, R. P., Wieczorek, D. F., and Solaro, R. J. (2008) Use of 2-D DIGE analysis reveals altered phosphorylation in a tropomyosin mutant (Glu54Lys) linked to dilated cardiomyopathy. Proteomics 8, 100-105
    • (2008) Proteomics , vol.8 , pp. 100-105
    • Warren, C.M.1    Arteaga, G.M.2    Rajan, S.3    Ahmed, R.P.4    Wieczorek, D.F.5    Solaro, R.J.6
  • 12
    • 0034623718 scopus 로고    scopus 로고
    • A single site (Ser16) phosphorylation in phospholamban is sufficient in mediating its maximal cardiac responses to-agonists
    • Chu, G., Lester, J. W., Young, K. B., Luo, W., Zhai, J., and Kranias, E. G. (2000) A single site (Ser16) phosphorylation in phospholamban is sufficient in mediating its maximal cardiac responses to-agonists. J. Biol. Chem. 275, 38938-38943
    • (2000) J. Biol. Chem. , vol.275 , pp. 38938-38943
    • Chu, G.1    Lester, J.W.2    Young, K.B.3    Luo, W.4    Zhai, J.5    Kranias, E.G.6
  • 14
    • 0038464639 scopus 로고    scopus 로고
    • Phospholamban: A crucial regulator of cardiac contractility
    • MacLennan, D. H., and Kranias, E. G. (2003) Phospholamban: a crucial regulator of cardiac contractility. Nat. Rev. Mol. Cell Biol. 4, 566-577
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 566-577
    • Maclennan, D.H.1    Kranias, E.G.2
  • 15
    • 0034697029 scopus 로고    scopus 로고
    • Maximal inhibition of SERCA2 Ca2+ affinity by phospholamban in transgenic hearts overexpressing a non-phosphorylatable form of phospholamban
    • Brittsan, A. G., Carr, A. N., Schmidt, A. G., and Kranias, E. G. (2000) Maximal inhibition of SERCA2 Ca2+ affinity by phospholamban in transgenic hearts overexpressing a non-phosphorylatable form of phospholamban. J. Biol. Chem. 275, 12129-12135
    • (2000) J. Biol. Chem. , vol.275 , pp. 12129-12135
    • Brittsan, A.G.1    Carr, A.N.2    Schmidt, A.G.3    Kranias, E.G.4
  • 18
    • 0035827593 scopus 로고    scopus 로고
    • Overwhelming evidence of the beneficial effects of SERCA gene transfer in heart failure
    • del Monte, F., Hajjar, R. J., and Harding, S. E. (2001) Overwhelming evidence of the beneficial effects of SERCA gene transfer in heart failure. Circ. Res. 88, E66-E67
    • (2001) Circ. Res. , vol.88
    • Del Monte, F.1    Hajjar, R.J.2    Harding, S.E.3
  • 22
    • 0034781383 scopus 로고    scopus 로고
    • A familial hypertrophic cardiomyopathy alpha-tropomyosin mutation causes severe cardiac hypertrophy and death in mice
    • Prabhakar, R., Boivin, G. P., Grupp, I. L., Hoit, B., Arteaga, G., Solaro, R. J., and Wieczorek, D. F. (2001) A familial hypertrophic cardiomyopathy alpha-tropomyosin mutation causes severe cardiac hypertrophy and death in mice. J. Mol. Cell. Cardiol. 33, 1815-1828
    • (2001) J. Mol. Cell. Cardiol. , vol.33 , pp. 1815-1828
    • Prabhakar, R.1    Boivin, G.P.2    Grupp, I.L.3    Hoit, B.4    Arteaga, G.5    Solaro, R.J.6    Wieczorek, D.F.7
  • 24
    • 0026342911 scopus 로고
    • Tissue-specific regulation of the-myosin heavy chain gene promoter in transgenic mice
    • Subramaniam, A., Jones, W. K., Gulick, J., Wert, S., Neumann, J., and Robbins, J. (1991) Tissue-specific regulation of the-myosin heavy chain gene promoter in transgenic mice. J. Biol. Chem. 266, 24613-24620
    • (1991) J. Biol. Chem. , vol.266 , pp. 24613-24620
    • Subramaniam, A.1    Jones, W.K.2    Gulick, J.3    Wert, S.4    Neumann, J.5    Robbins, J.6
  • 26
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl, M. W. (2001) A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res. 29, e45
    • (2001) Nucleic Acids Res. , vol.29
    • Pfaffl, M.W.1
  • 28
    • 29244432482 scopus 로고    scopus 로고
    • Recommendations for chamber quantification: A report from the American Society of Echocardiography's Guidelines and Standards Committee and the Chamber Quantification Writing Group, developed in conjunction with the European Association of Echocardiography, a branch of the European Society of Cardiology
    • Lang, R. M., Bierig, M., Devereux, R. B., Flachskampf, F. A., Foster, E., Pellikka, P. A., Picard, M. H., Roman, M. J., Seward, J., Shanewise, J. S., Solomon, S. D., Spencer, K. T., Sutton, M. S., and Stewart, W. J. (2005) Recommendations for chamber quantification: a report from the American Society of Echocardiography's Guidelines and Standards Committee and the Chamber Quantification Writing Group, developed in conjunction with the European Association of Echocardiography, a branch of the European Society of Cardiology. J. Am. Soc. Echocardiogr. 18, 1440-1463
    • (2005) J. Am. Soc. Echocardiogr. , vol.18 , pp. 1440-1463
    • Lang, R.M.1    Bierig, M.2    Devereux, R.B.3    Flachskampf, F.A.4    Foster, E.5    Pellikka, P.A.6    Picard, M.H.7    Roman, M.J.8    Seward, J.9    Shanewise, J.S.10    Solomon, S.D.11    Spencer, K.T.12    Sutton, M.S.13    Stewart, W.J.14
  • 33
    • 10644275373 scopus 로고    scopus 로고
    • Impact of-myosin heavy chain expression on cardiac function during stress
    • Krenz, M., and Robbins, J. (2004) Impact of-myosin heavy chain expression on cardiac function during stress. J. Am. Coll. Cardiol. 44, 2390-2397
    • (2004) J. Am. Coll. Cardiol. , vol.44 , pp. 2390-2397
    • Krenz, M.1    Robbins, J.2
  • 35
    • 0036702666 scopus 로고    scopus 로고
    • Calcium cycling in congestive heart failure
    • Hasenfuss, G., and Pieske, B. (2002) Calcium cycling in congestive heart failure. J. Mol. Cell. Cardiol. 34, 951-969
    • (2002) J. Mol. Cell. Cardiol. , vol.34 , pp. 951-969
    • Hasenfuss, G.1    Pieske, B.2
  • 40
    • 77954623302 scopus 로고    scopus 로고
    • Localization of the two tropomyosinbinding sites of troponin T
    • Jin, J. P., and Chong, S. M. (2010) Localization of the two tropomyosinbinding sites of troponin T. Arch. Biochem. Biophys. 500, 144-150
    • (2010) Arch. Biochem. Biophys. , vol.500 , pp. 144-150
    • Jin, J.P.1    Chong, S.M.2
  • 41
    • 84883346948 scopus 로고    scopus 로고
    • Interplay between the overlapping ends of tropomyosin and the N terminus of cardiac troponin T affects tropomyosin states on actin
    • 10.1096/fj.13-232363
    • Mamidi, R., Michael, J. J., Muthuchamy, M., and Chandra, M. (2013) Interplay between the overlapping ends of tropomyosin and the N terminus of cardiac troponin T affects tropomyosin states on actin. FASEB J. 10.1096/fj.13-232363
    • (2013) FASEB J.
    • Mamidi, R.1    Michael, J.J.2    Muthuchamy, M.3    Chandra, M.4
  • 42
    • 84876415331 scopus 로고    scopus 로고
    • The tropomyosin binding region of cardiac troponin T modulates crossbridge recruitment dynamics in rat cardiac muscle fibers
    • Gollapudi, S. K., Gallon, C. E., and Chandra, M. (2013) The tropomyosin binding region of cardiac troponin T modulates crossbridge recruitment dynamics in rat cardiac muscle fibers. J. Mol. Biol. 425, 1565-1581
    • (2013) J. Mol. Biol. , vol.425 , pp. 1565-1581
    • Gollapudi, S.K.1    Gallon, C.E.2    Chandra, M.3
  • 43
    • 84866607365 scopus 로고    scopus 로고
    • Familial hypertrophic cardiomyopathy related E180G mutation increases flexibility of human cardiac-tropomyosin
    • Loong, C. K., Zhou, H. X., and Chase, P. B. (2012) Familial hypertrophic cardiomyopathy related E180G mutation increases flexibility of human cardiac-tropomyosin. FEBS Lett. 586, 3503-3507
    • (2012) FEBS Lett. , vol.586 , pp. 3503-3507
    • Loong, C.K.1    Zhou, H.X.2    Chase, P.B.3
  • 44
    • 84865119925 scopus 로고    scopus 로고
    • Long-range effects of familial hypertrophic cardiomyopathy mutations E180G and D175N on the properties of tropomyosin
    • Ly, S., and Lehrer, S. S. (2012) Long-range effects of familial hypertrophic cardiomyopathy mutations E180G and D175N on the properties of tropomyosin. Biochemistry 51, 6413-6420
    • (2012) Biochemistry , vol.51 , pp. 6413-6420
    • Ly, S.1    Lehrer, S.S.2
  • 46
    • 84862687135 scopus 로고    scopus 로고
    • Persistence length of human cardiac-tropomyosin measured by single molecule direct probe microscopy
    • Loong, C. K., Zhou, H. X., and Chase, P. B. (2012) Persistence length of human cardiac-tropomyosin measured by single molecule direct probe microscopy. PLoS One 7, e39676
    • (2012) PLoS One , vol.7
    • Loong, C.K.1    Zhou, H.X.2    Chase, P.B.3
  • 47
    • 79953055654 scopus 로고    scopus 로고
    • Thin filament mutations: Developing an integrative approach to a complex disorder
    • Tardiff, J. C. (2011) Thin filament mutations: developing an integrative approach to a complex disorder. Circ. Res. 108, 765-782
    • (2011) Circ. Res. , vol.108 , pp. 765-782
    • Tardiff, J.C.1
  • 48
    • 2442710177 scopus 로고    scopus 로고
    • Parvalbumin corrects slowed relaxation in adult cardiac myocytes expressing hypertrophic cardiomyopathy-linked-tropomyosin mutations
    • Coutu, P., Bennett, C. N., Favre, E. G., Day, S. M., and Metzger, J. M. (2004) Parvalbumin corrects slowed relaxation in adult cardiac myocytes expressing hypertrophic cardiomyopathy-linked-tropomyosin mutations. Circ. Res. 94, 1235-1241
    • (2004) Circ. Res. , vol.94 , pp. 1235-1241
    • Coutu, P.1    Bennett, C.N.2    Favre, E.G.3    Day, S.M.4    Metzger, J.M.5
  • 50
    • 77953526511 scopus 로고    scopus 로고
    • Removal of the cardiac troponin i N-terminal extension improves cardiac function in aged mice
    • Biesiadecki, B. J., Tachampa, K., Yuan, C., Jin, J. P., de Tombe, P. P., and Solaro, R. J. (2010) Removal of the cardiac troponin I N-terminal extension improves cardiac function in aged mice. J. Biol. Chem. 285, 19688-19698
    • (2010) J. Biol. Chem. , vol.285 , pp. 19688-19698
    • Biesiadecki, B.J.1    Tachampa, K.2    Yuan, C.3    Jin, J.P.4    De Tombe, P.P.5    Solaro, R.J.6
  • 51
    • 84863058123 scopus 로고    scopus 로고
    • The effect of myosin RLC phosphorylation in normal and cardiomyopathic mouse hearts
    • Muthu, P., Kazmierczak, K., Jones, M., and Szczesna-Cordary, D. (2012) The effect of myosin RLC phosphorylation in normal and cardiomyopathic mouse hearts. J. Cell. Mol. Med. 16, 911-919
    • (2012) J. Cell. Mol. Med. , vol.16 , pp. 911-919
    • Muthu, P.1    Kazmierczak, K.2    Jones, M.3    Szczesna-Cordary, D.4
  • 53
    • 0032500583 scopus 로고    scopus 로고
    • Molecular analysis of the interactions between protein kinase C- and filamentous actin
    • Prekeris, R., Hernandez, R. M., Mayhew, M. W., White, M. K., and Terrian, D. M. (1998) Molecular analysis of the interactions between protein kinase C- and filamentous actin. J. Biol. Chem. 273, 26790-26798
    • (1998) J. Biol. Chem. , vol.273 , pp. 26790-26798
    • Prekeris, R.1    Hernandez, R.M.2    Mayhew, M.W.3    White, M.K.4    Terrian, D.M.5
  • 54
    • 0035800770 scopus 로고    scopus 로고
    • Constitutive association of c-N-Ras with c-Raf-1 and protein kinase Cδ in latent signaling modules
    • Hamilton, M., Liao, J., Cathcart, M. K., and Wolfman, A. (2001) Constitutive association of c-N-Ras with c-Raf-1 and protein kinase Cδ in latent signaling modules. J. Biol. Chem. 276, 29079-29090
    • (2001) J. Biol. Chem. , vol.276 , pp. 29079-29090
    • Hamilton, M.1    Liao, J.2    Cathcart, M.K.3    Wolfman, A.4
  • 55
    • 0035042676 scopus 로고    scopus 로고
    • Localization and kinetics of protein kinase C- anchoring in cardiac myocytes
    • Robia, S. L., Ghanta, J., Robu, V. G., and Walker, J. W. (2001) Localization and kinetics of protein kinase C- anchoring in cardiac myocytes. Biophys. J. 80, 2140-2151
    • (2001) Biophys. J. , vol.80 , pp. 2140-2151
    • Robia, S.L.1    Ghanta, J.2    Robu, V.G.3    Walker, J.W.4


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