메뉴 건너뛰기




Volumn 48, Issue 5, 2010, Pages 893-898

Investigations into tropomyosin function using mouse models

Author keywords

Calcium sensitivity; Cardiac function; Sarcometic thin filament; Tropomyosin

Indexed keywords

ACTIN; ALPHA TROPOMYOSIN; BETA TROPOMYOSIN; GAMMA TROPOMYOSIN; TROPOMYOSIN; TROPONIN; TROPONIN T; UNCLASSIFIED DRUG;

EID: 77951623501     PISSN: 00222828     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yjmcc.2009.10.003     Document Type: Review
Times cited : (40)

References (44)
  • 1
    • 60849116181 scopus 로고    scopus 로고
    • Tropomyosin and the steric mechanism of muscle regulation. In: Tropomyosin (ed: P. Gunning)
    • Lehman W., Craig R. Tropomyosin and the steric mechanism of muscle regulation. In: Tropomyosin (ed: P. Gunning). Adv Exp Med Biol 2008, 644:95-109.
    • (2008) Adv Exp Med Biol , vol.644 , pp. 95-109
    • Lehman, W.1    Craig, R.2
  • 2
    • 67349282758 scopus 로고    scopus 로고
    • Structural basis for the activation of muscle contraction by troponin and tropomyosin
    • Lehman W., Galinska-Rakocsy A., Hatch V., Tobacman L., Craig R. Structural basis for the activation of muscle contraction by troponin and tropomyosin. J Mol Biol 2009, 388:673-681.
    • (2009) J Mol Biol , vol.388 , pp. 673-681
    • Lehman, W.1    Galinska-Rakocsy, A.2    Hatch, V.3    Tobacman, L.4    Craig, R.5
  • 3
    • 65649150702 scopus 로고    scopus 로고
    • 2+-dependent photocrosslinking of tropomyosin residue 146 to residues 157-163 in the c-terminal domain of troponin I in reconstituted skeletal muscle thin filaments
    • 2+-dependent photocrosslinking of tropomyosin residue 146 to residues 157-163 in the c-terminal domain of troponin I in reconstituted skeletal muscle thin filaments. J Mol Biol 2009, 389:575-583.
    • (2009) J Mol Biol , vol.389 , pp. 575-583
    • Mudalige, A.1    Tao, T.2    Lehrer, S.3
  • 4
    • 3142772675 scopus 로고    scopus 로고
    • Expression of a novel cardiac-specific tropomyosin isoform in humans
    • Denz C.R., Narshi A., Zajdel R.W., Dube D.K. Expression of a novel cardiac-specific tropomyosin isoform in humans. Biochem Biophy Res Commun 2004, 320:1291-1297.
    • (2004) Biochem Biophy Res Commun , vol.320 , pp. 1291-1297
    • Denz, C.R.1    Narshi, A.2    Zajdel, R.W.3    Dube, D.K.4
  • 5
    • 76649084202 scopus 로고    scopus 로고
    • Molecular and functional characterization of a novel cardiac specific human tropomyosin isoform
    • Rajan S., Jagatheesan G., Karam C.N., Alves M.L., Bodi I., Schwartz A., et al. Molecular and functional characterization of a novel cardiac specific human tropomyosin isoform. Circulation 2010, 121:410-418.
    • (2010) Circulation , vol.121 , pp. 410-418
    • Rajan, S.1    Jagatheesan, G.2    Karam, C.N.3    Alves, M.L.4    Bodi, I.5    Schwartz, A.6
  • 6
    • 0027285642 scopus 로고
    • Developmental analysis of tropomyosin gene expression in embryonic stem cells and mouse embryos
    • Muthuchamy M., Pajak L., Howles P., Doetschman T., Wieczorek D.F. Developmental analysis of tropomyosin gene expression in embryonic stem cells and mouse embryos. Mol Cell Biol 1993, 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
  • 9
    • 1542374026 scopus 로고    scopus 로고
    • Gamma tropomyosin gene products are required for embryonic development
    • Hook J., Lemckert F., Qin H., Schevzov G., Gunning P. Gamma tropomyosin gene products are required for embryonic development. Mol Cell Biol 2004, 24:2318-2323.
    • (2004) Mol Cell Biol , vol.24 , pp. 2318-2323
    • Hook, J.1    Lemckert, F.2    Qin, H.3    Schevzov, G.4    Gunning, P.5
  • 10
    • 0034703378 scopus 로고    scopus 로고
    • Tropomyosin and actin isoforms modulate the localization of tropomyosin strands on actin filaments
    • Lehman W., Hatch V., Korman V., Rosol M., Thomas L., Maytum R., et al. Tropomyosin and actin isoforms modulate the localization of tropomyosin strands on actin filaments. J Mol Biol 2000, 302:593-606.
    • (2000) J Mol Biol , vol.302 , pp. 593-606
    • Lehman, W.1    Hatch, V.2    Korman, V.3    Rosol, M.4    Thomas, L.5    Maytum, R.6
  • 11
    • 0029559447 scopus 로고
    • Molecular and physiological effects of overexpressing striated muscle b-tropomyosin in the adult murine heart
    • Muthuchamy M., Grupp I.L., Grupp G., O'Toole B.A., Kier A.B., Boivin G.P., et al. Molecular and physiological effects of overexpressing striated muscle b-tropomyosin in the adult murine heart. J Biol Chem 1995, 270:30593-30603.
    • (1995) J Biol Chem , vol.270 , pp. 30593-30603
    • Muthuchamy, M.1    Grupp, I.L.2    Grupp, G.3    O'Toole, B.A.4    Kier, A.B.5    Boivin, G.P.6
  • 13
    • 0034781383 scopus 로고    scopus 로고
    • A familial hypertrophic cardiomyopathy α-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., Wieczorek D.F. A familial hypertrophic cardiomyopathy α-tropomyosin mutation causes severe cardiac hypertrophy and death in mice. J Mol Cell Cardiol 2001, 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
  • 15
    • 23744475805 scopus 로고    scopus 로고
    • Different effects of cardiac versus skeletal muscle regulatory proteins on in vitro measures of actin filament speed and force
    • Clemmens E., Entezari M., Martyn D., Regnier M. Different effects of cardiac versus skeletal muscle regulatory proteins on in vitro measures of actin filament speed and force. J Physiol 2005, 566:737-746.
    • (2005) J Physiol , vol.566 , pp. 737-746
    • Clemmens, E.1    Entezari, M.2    Martyn, D.3    Regnier, M.4
  • 16
    • 0034682640 scopus 로고    scopus 로고
    • Tropomyosin 3 increases striated muscle isoform diversity
    • Pieples K., Wieczorek D.F. Tropomyosin 3 increases striated muscle isoform diversity. Biochem 2000, 39:8291-8297.
    • (2000) Biochem , vol.39 , pp. 8291-8297
    • Pieples, K.1    Wieczorek, D.F.2
  • 18
    • 67749145755 scopus 로고    scopus 로고
    • A peek into tropomyosin binding and unfolding on the actin filament
    • Singh A., Hitchcock-DeGregori S. A peek into tropomyosin binding and unfolding on the actin filament. PLoS ONE 2009, 4:e6336.
    • (2009) PLoS ONE , vol.4
    • Singh, A.1    Hitchcock-DeGregori, S.2
  • 19
    • 43749096824 scopus 로고    scopus 로고
    • Conserved Asp-137 imparts flexibility to tropomyosin and affects function
    • Sumida J., Wu E., Lehrer S. Conserved Asp-137 imparts flexibility to tropomyosin and affects function. J Biol Chem 2008, 283:6728-6734.
    • (2008) J Biol Chem , vol.283 , pp. 6728-6734
    • Sumida, J.1    Wu, E.2    Lehrer, S.3
  • 21
    • 0023071735 scopus 로고
    • Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction
    • Zot A.S., Potter J.D. Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction. Annu Rev Biophy Biophy Chem 1987, 16:535-559.
    • (1987) Annu Rev Biophy Biophy Chem , vol.16 , pp. 535-559
    • Zot, A.S.1    Potter, J.D.2
  • 22
    • 0036842026 scopus 로고    scopus 로고
    • Structure and interactions of the carboxyl terminus of striated muscle alpha-tropomyosin: it is important to be flexible
    • Greenfield N.J., Palm T., Hitchcock-DeGregori S.E. Structure and interactions of the carboxyl terminus of striated muscle alpha-tropomyosin: it is important to be flexible. Biophys J 2002, 83:2754-2766.
    • (2002) Biophys J , vol.83 , pp. 2754-2766
    • Greenfield, N.J.1    Palm, T.2    Hitchcock-DeGregori, S.E.3
  • 23
    • 33750306274 scopus 로고    scopus 로고
    • Solution NMR structure of the junction between tropomyosin molecules: implications for actin binding and regulation
    • Greenfield N.J., Huang Y.J., Swapna G.V., Bhattacharya A., Rapp B., Singh A., et al. Solution NMR structure of the junction between tropomyosin molecules: implications for actin binding and regulation. J Mol Biol 2006, 364:80-96.
    • (2006) J Mol Biol , vol.364 , pp. 80-96
    • Greenfield, N.J.1    Huang, Y.J.2    Swapna, G.V.3    Bhattacharya, A.4    Rapp, B.5    Singh, A.6
  • 24
    • 0038001087 scopus 로고    scopus 로고
    • Functional importance of the carboxyl-terminal region of striated muscle tropomyosin
    • Jagatheesan G., Rajan S., Petrashevskaya N., Schwartz, Boivin G., Vahebi S., et al. Functional importance of the carboxyl-terminal region of striated muscle tropomyosin. J Biol Chem 2003, 278:23204-23211.
    • (2003) J Biol Chem , vol.278 , pp. 23204-23211
    • Jagatheesan, G.1    Rajan, S.2    Petrashevskaya, N.3    Schwartz4    Boivin, G.5    Vahebi, S.6
  • 27
    • 23344452467 scopus 로고    scopus 로고
    • Dilated cardiomyopathy mutations in three thin filament regulatory proteins results in a common functional phenotype
    • Mirza M., Marston S., Willott R., Ashley C., Mogensen J., McKenna W., et al. Dilated cardiomyopathy mutations in three thin filament regulatory proteins results in a common functional phenotype. J Biol Chem 2005, 280:28498-28506.
    • (2005) J Biol Chem , vol.280 , pp. 28498-28506
    • Mirza, M.1    Marston, S.2    Willott, R.3    Ashley, C.4    Mogensen, J.5    McKenna, W.6
  • 28
    • 34547605959 scopus 로고    scopus 로고
    • Dilated cardiomyopathy mutant tropomyosin mice develop cardiac dysfunction with significantly decreased fractional shortening and myofilament calcium sensitivity
    • Rajan S., Ahmed R., Jagatheesan G., Petrashevskaya N., Boivin G., Urboniene D., et al. Dilated cardiomyopathy mutant tropomyosin mice develop cardiac dysfunction with significantly decreased fractional shortening and myofilament calcium sensitivity. Circ Res 2007, 101:205-214.
    • (2007) Circ Res , vol.101 , pp. 205-214
    • Rajan, S.1    Ahmed, R.2    Jagatheesan, G.3    Petrashevskaya, N.4    Boivin, G.5    Urboniene, D.6
  • 29
    • 0142149180 scopus 로고    scopus 로고
    • Cardiomyopathic tropomyosin mutations that increase thin filament Ca2+ sensitivity and tropomyosin N-domain flexibility
    • Heller M., Nili M., Homsher E., Tobacman L. Cardiomyopathic tropomyosin mutations that increase thin filament Ca2+ sensitivity and tropomyosin N-domain flexibility. J Biol Chem 2003, 278:41742-41748.
    • (2003) J Biol Chem , vol.278 , pp. 41742-41748
    • Heller, M.1    Nili, M.2    Homsher, E.3    Tobacman, L.4
  • 30
    • 60849113734 scopus 로고    scopus 로고
    • Tropomyosins in skeletal muscle diseases. In: Tropomyosin (ed: P. Gunning)
    • Kee A.J., Hardeman E.C. Tropomyosins in skeletal muscle diseases. In: Tropomyosin (ed: P. Gunning). Adv Exp Med Biol 2008, 644:143-157.
    • (2008) Adv Exp Med Biol , vol.644 , pp. 143-157
    • Kee, A.J.1    Hardeman, E.C.2
  • 31
    • 60849112865 scopus 로고    scopus 로고
    • The role of tropomyosin in heart disease. In: Tropomyosin (ed: P. Gunning)
    • Wieczorek D.F., Jagatheesan G., Rajan S. The role of tropomyosin in heart disease. In: Tropomyosin (ed: P. Gunning). Adv Exp Med Biol 2008, 644:132-142.
    • (2008) Adv Exp Med Biol , vol.644 , pp. 132-142
    • Wieczorek, D.F.1    Jagatheesan, G.2    Rajan, S.3
  • 32
    • 30944444021 scopus 로고    scopus 로고
    • Sarcomeric proteins and familial hypertrophic cardiomyopathy: linking mutations in structural proteins to complex cardiovascular phenotypes
    • Tardiff J. Sarcomeric proteins and familial hypertrophic cardiomyopathy: linking mutations in structural proteins to complex cardiovascular phenotypes. Heart Fail Rev 2005, 10:237-248.
    • (2005) Heart Fail Rev , vol.10 , pp. 237-248
    • Tardiff, J.1
  • 34
    • 0033538612 scopus 로고    scopus 로고
    • Mouse model of a familial hypertrophic cardiomyopathy mutation in α-tropomyosin manifests cardiac dysfunction
    • Muthuchamy M., Pieples K., Rethinasamy P., Hoit B., Grupp I.L., Boivin G.P., et al. Mouse model of a familial hypertrophic cardiomyopathy mutation in α-tropomyosin manifests cardiac dysfunction. Circ Res 1999, 85:47-56.
    • (1999) Circ Res , vol.85 , pp. 47-56
    • Muthuchamy, M.1    Pieples, K.2    Rethinasamy, P.3    Hoit, B.4    Grupp, I.L.5    Boivin, G.P.6
  • 37
    • 0037047648 scopus 로고    scopus 로고
    • Cardiac dysfunction in hypertrophic cardiomyopathy mutant tropomyosin mice is transgene-dependent, hypertrophy-independent, and improved by β-blockade
    • Michele D.E., Gomez C.A., Hong K.E., Westfall M.V., Metzger J.M. Cardiac dysfunction in hypertrophic cardiomyopathy mutant tropomyosin mice is transgene-dependent, hypertrophy-independent, and improved by β-blockade. Circ Res 2002, 91:255-262.
    • (2002) Circ Res , vol.91 , pp. 255-262
    • Michele, D.E.1    Gomez, C.A.2    Hong, K.E.3    Westfall, M.V.4    Metzger, J.M.5
  • 39
    • 0037236421 scopus 로고    scopus 로고
    • Targeting calcium cycling proteins in heart failure through gene transfer
    • del Monte F., Hajjar R.J. Targeting calcium cycling proteins in heart failure through gene transfer. J Physiol 2003, 546:49-61.
    • (2003) J Physiol , vol.546 , pp. 49-61
    • del Monte, F.1    Hajjar, R.J.2
  • 40
    • 77951622102 scopus 로고    scopus 로고
    • Neonatal gene transfer of SERCA2a improves the response to beta-adrenergic stimulation in a FHC alpha-tropomyosin (Glu180Gly) mouse model
    • Pena JR, Goldspink PH, Prabhakar R, del Monte F, Hajjar RJ, Wieczorek DF, et al. Neonatal gene transfer of SERCA2a improves the response to beta-adrenergic stimulation in a FHC alpha-tropomyosin (Glu180Gly) mouse model. Faseb J. 2004;18:A1216-A1217.
    • (2004) Faseb J. , vol.18
    • Pena, J.R.1    Goldspink, P.H.2    Prabhakar, R.3    del Monte, F.4    Hajjar, R.J.5    Wieczorek, D.F.6
  • 41
    • 77951620586 scopus 로고    scopus 로고
    • Phospholamban Knockout Alters Hypertrophic Gene Expression and Improves Cardiac Function in a HCM alpha-Tropomyosin (Glu180Gly) Mouse
    • Pena JR, Goldspink PH, Heinrich LS, Kranias EG, Wieczorek DF, Wolska BM. Phospholamban Knockout Alters Hypertrophic Gene Expression and Improves Cardiac Function in a HCM alpha-Tropomyosin (Glu180Gly) Mouse. Circ Res 2008;103:E40.
    • (2008) Circ Res , vol.103
    • Pena, J.R.1    Goldspink, P.H.2    Heinrich, L.S.3    Kranias, E.G.4    Wieczorek, D.F.5    Wolska, B.M.6
  • 42
    • 2442710177 scopus 로고    scopus 로고
    • Parvalbumin corrects slowed relaxation in adult cardiac myocytes expressing hypertrophic cardiomyopathy-linked alpha-tropomyosin mutations
    • Coutu P., Bennett C.N., Favre E.G., Day S.M., Metzger J.M. Parvalbumin corrects slowed relaxation in adult cardiac myocytes expressing hypertrophic cardiomyopathy-linked alpha-tropomyosin mutations. Circ Res 2004, 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
  • 43
    • 0032508640 scopus 로고    scopus 로고
    • Prevention of cardiac hypertrophy in mice by calcineurin inhibition
    • Sussman M.A., Lim H.W., Gude N., Taigen T., Olson E.N., Robbins J., et al. Prevention of cardiac hypertrophy in mice by calcineurin inhibition. Science 1998, 281:1690-1693.
    • (1998) Science , vol.281 , pp. 1690-1693
    • Sussman, M.A.1    Lim, H.W.2    Gude, N.3    Taigen, T.4    Olson, E.N.5    Robbins, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.