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Volumn 98, Issue 10, 2006, Pages 1290-1298

Activation of myocardial contraction by the N-terminal domains of myosin binding protein-C

Author keywords

Ca 2+sensitization; Cardiac myocytes; Frank Starling mechanism; Myosin binding protein C; Sarcomere length

Indexed keywords

ACTIN; ALANINE; CALCIUM; MYOSIN; MYOSIN BINDING PROTEIN C; PROLINE; CARRIER PROTEIN; MYOSIN-BINDING PROTEIN C; PEPTIDE FRAGMENT;

EID: 33744993933     PISSN: 00097330     EISSN: None     Source Type: Journal    
DOI: 10.1161/01.RES.0000222059.54917.ef     Document Type: Article
Times cited : (80)

References (31)
  • 2
    • 2642572455 scopus 로고    scopus 로고
    • Cardiac myosin binding protein C: Its role in physiology and disease
    • Flashman E, Redwood C, Moolman-Smook J, Watkins H. Cardiac myosin binding protein C: its role in physiology and disease. Circ Res. 2004;94:1279-1289.
    • (2004) Circ Res , vol.94 , pp. 1279-1289
    • Flashman, E.1    Redwood, C.2    Moolman-Smook, J.3    Watkins, H.4
  • 3
    • 0142024741 scopus 로고    scopus 로고
    • Loaded shortening, power output, and rate of force redevelopment are increased with knockout of cardiac myosin binding protein-C
    • Korte FS, McDonald KS, Harris SP, Moss RL. Loaded shortening, power output, and rate of force redevelopment are increased with knockout of cardiac myosin binding protein-C. Circ Res. 2003;93:752-758.
    • (2003) Circ Res , vol.93 , pp. 752-758
    • Korte, F.S.1    McDonald, K.S.2    Harris, S.P.3    Moss, R.L.4
  • 5
    • 0032772719 scopus 로고    scopus 로고
    • cAPK-phosphorylation controls the interaction of the regulatory domain of cardiac myosin binding protein C with myosin-S2 in an on-off fashion
    • Gruen M, Prinz H, Gautel M. cAPK-phosphorylation controls the interaction of the regulatory domain of cardiac myosin binding protein C with myosin-S2 in an on-off fashion. FEBS Lett. 1999;453:254-259.
    • (1999) FEBS Lett , vol.453 , pp. 254-259
    • Gruen, M.1    Prinz, H.2    Gautel, M.3
  • 6
    • 0029812703 scopus 로고    scopus 로고
    • Alteration of myosin cross bridges by phosphorylation of myosin-binding protein C in cardiac muscle
    • Weisberg A, Winegrad S. Alteration of myosin cross bridges by phosphorylation of myosin-binding protein C in cardiac muscle. Proc Natl Acad Sci U S A. 1996;93:8999-9003.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 8999-9003
    • Weisberg, A.1    Winegrad, S.2
  • 7
    • 0035947749 scopus 로고    scopus 로고
    • Phosphorylation of troponin-I by protein kinase A accelerates relaxation and cross-bridge cycle kinetics in mouse ventricular muscle
    • Kentish JC, McCloskey DT, Layland J, Palmer S, Leiden JM, Martin AF, Solaro RJ. Phosphorylation of troponin-I by protein kinase A accelerates relaxation and cross-bridge cycle kinetics in mouse ventricular muscle. Circ Res. 2001;88:1059-1065.
    • (2001) Circ Res , vol.88 , pp. 1059-1065
    • Kentish, J.C.1    McCloskey, D.T.2    Layland, J.3    Palmer, S.4    Leiden, J.M.5    Martin, A.F.6    Solaro, R.J.7
  • 8
    • 0042093724 scopus 로고    scopus 로고
    • Structural evidence for the interaction of C-protein (MyBP-C) with actin and sequence identification of a possible actin-binding domain
    • Squire JM, Luther PK, Knupp C. Structural evidence for the interaction of C-protein (MyBP-C) with actin and sequence identification of a possible actin-binding domain. J Mol Biol. 2003;331:713-724.
    • (2003) J Mol Biol , vol.331 , pp. 713-724
    • Squire, J.M.1    Luther, P.K.2    Knupp, C.3
  • 10
    • 0036454919 scopus 로고    scopus 로고
    • Frank-Starling law of the heart and the cellular mechanisms of length-dependent activation
    • Konhilas JP, Irving TC, de Tombe PP. Frank-Starling law of the heart and the cellular mechanisms of length-dependent activation. Pflugers Arch. 2002;445:305-310.
    • (2002) Pflugers Arch , vol.445 , pp. 305-310
    • Konhilas, J.P.1    Irving, T.C.2    De Tombe, P.P.3
  • 11
    • 0022393490 scopus 로고
    • The cellular basis of the length-tension relation in cardiac muscle
    • Allen DG, Kentish JC. The cellular basis of the length-tension relation in cardiac muscle. J Mol Cell Cardiol. 1985;17:821-840.
    • (1985) J Mol Cell Cardiol , vol.17 , pp. 821-840
    • Allen, D.G.1    Kentish, J.C.2
  • 12
    • 0029029477 scopus 로고
    • 2+ sensitivity of tension at short sarcomere length
    • 2+ sensitivity of tension at short sarcomere length. Circ Res. 1995;77:199-205.
    • (1995) Circ Res , vol.77 , pp. 199-205
    • McDonald, K.S.1    Moss, R.L.2
  • 13
    • 28444479858 scopus 로고    scopus 로고
    • 2+ activation in cardiac muscle: Some remaining questions
    • 2+ activation in cardiac muscle: some remaining questions. J Muscle Res Cell Motility. 2005;26:199-212.
    • (2005) J Muscle Res Cell Motility , vol.26 , pp. 199-212
    • Fuchs, F.1    Martyn, D.A.2
  • 14
    • 33745458278 scopus 로고    scopus 로고
    • Regulation of skinned cardiac myocyte contractility by the N-terminal region of myosin-binding protein C
    • Abstract
    • Herron TJ, Kunst G, Gautel M, Kentish JC. Regulation of skinned cardiac myocyte contractility by the N-terminal region of myosin-binding protein C. J Muscle Res Cell Motility. 2003;24:328 Abstract.
    • (2003) J Muscle Res Cell Motility , vol.24 , pp. 328
    • Herron, T.J.1    Kunst, G.2    Gautel, M.3    Kentish, J.C.4
  • 15
    • 0033605334 scopus 로고    scopus 로고
    • Mutations in β-myosin S2 that cause familial hypertrophic cardiomyopathy (FHC) abolish the interaction with the regulatory domain of myosin-binding protein-C
    • Gruen M, Gautel M. Mutations in β-myosin S2 that cause familial hypertrophic cardiomyopathy (FHC) abolish the interaction with the regulatory domain of myosin-binding protein-C. J Mol Biol. 1999;286:933-949.
    • (1999) J Mol Biol , vol.286 , pp. 933-949
    • Gruen, M.1    Gautel, M.2
  • 16
    • 0033972217 scopus 로고    scopus 로고
    • Myosin binding protein C, a phosphorylation-dependent force regulator in muscle that controls the attachment of myosin heads by its interaction with myosin S2
    • Kunst G, Kress KR, Gruen M, Uttenweiler D, Gautel M, Fink RHA. Myosin binding protein C, a phosphorylation-dependent force regulator in muscle that controls the attachment of myosin heads by its interaction with myosin S2. Circ Res. 2000;86:51-58.
    • (2000) Circ Res , vol.86 , pp. 51-58
    • Kunst, G.1    Kress, K.R.2    Gruen, M.3    Uttenweiler, D.4    Gautel, M.5    Fink, R.H.A.6
  • 17
    • 0032572414 scopus 로고    scopus 로고
    • 2+ activation and relaxation in rat and guinea-pig skinned trabeculae
    • 2+ activation and relaxation in rat and guinea-pig skinned trabeculae. Circ Res. 1998;83:179-186.
    • (1998) Circ Res , vol.83 , pp. 179-186
    • Palmer, S.1    Kentish, J.C.2
  • 18
    • 0035824911 scopus 로고    scopus 로고
    • Power output is increased after phosphorylation of myofibrillar proteins in rat skinned cardiac myocytes
    • Herron TJ, Korte FS, McDonald KS. Power output is increased after phosphorylation of myofibrillar proteins in rat skinned cardiac myocytes. Circ Res. 2001;89:1184-1190.
    • (2001) Circ Res , vol.89 , pp. 1184-1190
    • Herron, T.J.1    Korte, F.S.2    McDonald, K.S.3
  • 19
    • 2042451727 scopus 로고
    • Rate of force generation in muscle: Correlation with actomyosin ATPase activity in solution
    • Brenner B, Eisenberg E. Rate of force generation in muscle: correlation with actomyosin ATPase activity in solution. Proc Natl Acad Scu U S A. 1986;83:3542-3546.
    • (1986) Proc Natl Acad Scu U S A , vol.83 , pp. 3542-3546
    • Brenner, B.1    Eisenberg, E.2
  • 20
    • 0030052266 scopus 로고    scopus 로고
    • A molecular map of the interactions between titin and myosin-binding protein C: Implications for sarcomeric assembly in familial hypertrophic cardiomyopathy
    • Freiburg A, Gautel M. A molecular map of the interactions between titin and myosin-binding protein C: implications for sarcomeric assembly in familial hypertrophic cardiomyopathy. Eur J Biochem. 1996;235:317-323.
    • (1996) Eur J Biochem , vol.235 , pp. 317-323
    • Freiburg, A.1    Gautel, M.2
  • 23
    • 0033575919 scopus 로고    scopus 로고
    • An improved method for exchanging troponin subunits in detergent skinned rat cardiac fiber bundles
    • Chandra M, Kim JJ, Solaro RJ. An improved method for exchanging troponin subunits in detergent skinned rat cardiac fiber bundles. Biochem Biophys Res Commun. 1999;263:219-223.
    • (1999) Biochem Biophys Res Commun , vol.263 , pp. 219-223
    • Chandra, M.1    Kim, J.J.2    Solaro, R.J.3
  • 24
    • 0028919177 scopus 로고
    • Rate of tension development in cardiac muscle varies with level of activator calcium
    • Wolff MR, Mcdonald KS, Moss RL. Rate of tension development in cardiac muscle varies with level of activator calcium. Circ Res. 1995;76:154-160.
    • (1995) Circ Res , vol.76 , pp. 154-160
    • Wolff, M.R.1    Mcdonald, K.S.2    Moss, R.L.3
  • 25
    • 7244245537 scopus 로고    scopus 로고
    • Binding of myosin binding protein-C to myosin subfragment S2 affects contractility independent of a tether mechanism
    • Harris SP, Rostkova E, Gautel M, Moss RL. Binding of myosin binding protein-C to myosin subfragment S2 affects contractility independent of a tether mechanism. Circ Res. 2004;95:930-936.
    • (2004) Circ Res , vol.95 , pp. 930-936
    • Harris, S.P.1    Rostkova, E.2    Gautel, M.3    Moss, R.L.4
  • 26
    • 0034027364 scopus 로고    scopus 로고
    • Effect of protein kinase A on calcium sensitivity of force and its sarcomere length dependence in human cardiomyocytes
    • van der Velden J, de Jong JW, Owen VJ, Burton PBJ, Stienen GJ. Effect of protein kinase A on calcium sensitivity of force and its sarcomere length dependence in human cardiomyocytes. Cardiovasc Res. 2000;46:487-495.
    • (2000) Cardiovasc Res , vol.46 , pp. 487-495
    • Van Der Velden, J.1    De Jong, J.W.2    Owen, V.J.3    Burton, P.B.J.4    Stienen, G.J.5
  • 27
    • 0033607481 scopus 로고    scopus 로고
    • COOH-terminal truncated cardiac myosin-binding protein C mutants resulting from familial hypertrophie cardiomyopathy mutations exhibit altered expression and/or incorporation in fetal rat cardiomyocytes
    • Flavigny J, Souchet M, Sebillon P, Berrebi-Bertrand I, Hainque B, Mallet A, Bril A, Schwartz K, Carrier L. COOH-terminal truncated cardiac myosin-binding protein C mutants resulting from familial hypertrophie cardiomyopathy mutations exhibit altered expression and/or incorporation in fetal rat cardiomyocytes. J Mol Biol. 1999;294:443-456.
    • (1999) J Mol Biol , vol.294 , pp. 443-456
    • Flavigny, J.1    Souchet, M.2    Sebillon, P.3    Berrebi-Bertrand, I.4    Hainque, B.5    Mallet, A.6    Bril, A.7    Schwartz, K.8    Carrier, L.9
  • 29
    • 0000266364 scopus 로고    scopus 로고
    • Modulation of contractility in human cardiac hypertrophy by myosin essential light chain isoforms
    • Schaub MC, Hefti MA, Zuellig RA, Morano I. Modulation of contractility in human cardiac hypertrophy by myosin essential light chain isoforms. Cardiovascular Res. 1998;37:381-404.
    • (1998) Cardiovascular Res , vol.37 , pp. 381-404
    • Schaub, M.C.1    Hefti, M.A.2    Zuellig, R.A.3    Morano, I.4
  • 30
    • 0033391877 scopus 로고    scopus 로고
    • 2+ activation in skinned cardiac muscle
    • 2+ activation in skinned cardiac muscle. J Mol Cell Cardiol. 1999;31:2115-2125.
    • (1999) J Mol Cell Cardiol , vol.31 , pp. 2115-2125
    • Smith, S.H.1    Fuchs, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.