메뉴 건너뛰기




Volumn 52, Issue 5, 2012, Pages 1145-1154

The dynamic role of cardiac myosin binding protein-C during ischemia

Author keywords

Cardiac contractility; Cardiac ischemia; Myosin binding protein C; Phosphorylation; Thick filament

Indexed keywords

MYOSIN BINDING PROTEIN C; PROTEIN ANTIBODY;

EID: 84859643919     PISSN: 00222828     EISSN: 10958584     Source Type: Journal    
DOI: 10.1016/j.yjmcc.2012.01.006     Document Type: Article
Times cited : (14)

References (44)
  • 1
    • 0015924821 scopus 로고
    • A new protein of the thick filaments of vertebrate skeletal myofibrils. Extraction. purification and characterization
    • Offer G., Moos C., Starr R. A new protein of the thick filaments of vertebrate skeletal myofibrils. Extraction. purification and characterization. J Mol Biol 1973, 74:653-676.
    • (1973) J Mol Biol , vol.74 , pp. 653-676
    • Offer, G.1    Moos, C.2    Starr, R.3
  • 2
    • 0018126953 scopus 로고
    • The binding of skeletal muscle C-protein to F-actin, and its relation to the interaction of actin with myosin subfragment-1
    • Moos C., Mason C.M., Besterman J.M., Feng M., Dubin J.H. The binding of skeletal muscle C-protein to F-actin, and its relation to the interaction of actin with myosin subfragment-1. J Mol Biol 1978, 124:571-586.
    • (1978) J Mol Biol , vol.124 , pp. 571-586
    • Moos, C.1    Mason, C.M.2    Besterman, J.M.3    Feng, M.4    Dubin, J.H.5
  • 4
    • 41249089916 scopus 로고    scopus 로고
    • Crystal structure of the C1 domain of cardiac myosin binding protein-C: implications for hypertrophic cardiomyopathy
    • Govada L., Carpenter L., da Fonseca P.C., Helliwell J.R., Rizkallah P., Flashman E., et al. Crystal structure of the C1 domain of cardiac myosin binding protein-C: implications for hypertrophic cardiomyopathy. J Mol Biol 2008, 378:387-397.
    • (2008) J Mol Biol , vol.378 , pp. 387-397
    • Govada, L.1    Carpenter, L.2    da Fonseca, P.C.3    Helliwell, J.R.4    Rizkallah, P.5    Flashman, E.6
  • 5
    • 0029029027 scopus 로고
    • Phosphorylation switches specific for the cardiac isoform of myosin binding protein-C: a modulator of cardiac contraction?
    • Gautel M., Zuffardi O., Freiburg A., Labeit S. Phosphorylation switches specific for the cardiac isoform of myosin binding protein-C: a modulator of cardiac contraction?. EMBO J 1995, 14:1952-1960.
    • (1995) EMBO J , vol.14 , pp. 1952-1960
    • Gautel, M.1    Zuffardi, O.2    Freiburg, A.3    Labeit, S.4
  • 6
    • 59149087665 scopus 로고    scopus 로고
    • Common MYBPC3 (cardiac myosin binding protein C) variant associated with cardiomyopathies in South Asia
    • Dhandapany P.S., Sadayappan S., Xue Y., Powell G.T., Rani D.S., Nallari P., et al. Common MYBPC3 (cardiac myosin binding protein C) variant associated with cardiomyopathies in South Asia. Nat Genet 2009, 41:187-191.
    • (2009) Nat Genet , vol.41 , pp. 187-191
    • Dhandapany, P.S.1    Sadayappan, S.2    Xue, Y.3    Powell, G.T.4    Rani, D.S.5    Nallari, P.6
  • 7
    • 0036623918 scopus 로고    scopus 로고
    • Cardiac titin: an adjustable multifunctional spring
    • Granzier H., Labeit S. Cardiac titin: an adjustable multifunctional spring. J Physiol 2002, 541:335-342.
    • (2002) J Physiol , vol.541 , pp. 335-342
    • Granzier, H.1    Labeit, S.2
  • 8
    • 77952481131 scopus 로고    scopus 로고
    • Cardiac titin: a multifunctional giant
    • LeWinter M.M., Granzier H. Cardiac titin: a multifunctional giant. Circulation 2010, 121:2137-2145.
    • (2010) Circulation , vol.121 , pp. 2137-2145
    • LeWinter, M.M.1    Granzier, H.2
  • 9
    • 33750061609 scopus 로고    scopus 로고
    • Cardiac titin: structure, functions and role in disease
    • LeWinter M.M., Wu Y., Labeit S., Granzier H. Cardiac titin: structure, functions and role in disease. Clin Chim Acta 2007, 375:1-9.
    • (2007) Clin Chim Acta , vol.375 , pp. 1-9
    • LeWinter, M.M.1    Wu, Y.2    Labeit, S.3    Granzier, H.4
  • 10
    • 78349268749 scopus 로고    scopus 로고
    • Role of titin in skeletal muscle function and disease
    • Ottenheij C.A., Granzier H. Role of titin in skeletal muscle function and disease. Adv Exp Med Biol 2010, 682:105-122.
    • (2010) Adv Exp Med Biol , vol.682 , pp. 105-122
    • Ottenheij, C.A.1    Granzier, H.2
  • 11
    • 0028886136 scopus 로고
    • Cardiac myosin binding protein-C gene splice acceptor site mutation is associated with familial hypertrophic cardiomyopathy
    • Bonne G., Carrier L., Bercovici J., Cruaud C., Richard P., Hainque B., et al. Cardiac myosin binding protein-C gene splice acceptor site mutation is associated with familial hypertrophic cardiomyopathy. Nat Genet 1995, 11:438-440.
    • (1995) Nat Genet , vol.11 , pp. 438-440
    • Bonne, G.1    Carrier, L.2    Bercovici, J.3    Cruaud, C.4    Richard, P.5    Hainque, B.6
  • 12
    • 0028844204 scopus 로고
    • Mutations in the cardiac myosin binding protein-C gene on chromosome 11 cause familial hypertrophic cardiomyopathy
    • Watkins H., Conner D., Thierfelder L., Jarcho J.A., MacRae C., McKenna W.J., et al. Mutations in the cardiac myosin binding protein-C gene on chromosome 11 cause familial hypertrophic cardiomyopathy. Nat Genet 1995, 11:434-437.
    • (1995) Nat Genet , vol.11 , pp. 434-437
    • Watkins, H.1    Conner, D.2    Thierfelder, L.3    Jarcho, J.A.4    MacRae, C.5    McKenna, W.J.6
  • 13
    • 33744944759 scopus 로고    scopus 로고
    • Ablation of cardiac myosin-binding protein-C accelerates force development in mouse myocardium
    • Stelzer J.E., Fitzsimons D.P., Moss R.L. Ablation of cardiac myosin-binding protein-C accelerates force development in mouse myocardium. Biophys J 2006, 90:4119-4127.
    • (2006) Biophys J , vol.90 , pp. 4119-4127
    • Stelzer, J.E.1    Fitzsimons, D.P.2    Moss, R.L.3
  • 14
    • 0034900675 scopus 로고    scopus 로고
    • Multiple structures of thick filaments in resting cardiac muscle and their influence on cross-bridge interactions
    • Levine R., Weisberg A., Kulikovskaya I., McClellen G., Winegrad S. Multiple structures of thick filaments in resting cardiac muscle and their influence on cross-bridge interactions. Biophys J 2001, 81:1070-1082.
    • (2001) Biophys J , vol.81 , pp. 1070-1082
    • Levine, R.1    Weisberg, A.2    Kulikovskaya, I.3    McClellen, G.4    Winegrad, S.5
  • 15
    • 34247571338 scopus 로고    scopus 로고
    • Multiple forms of cardiac myosin binding protein-C exist and can regulate thick filament stability
    • Kulikovskaya I., McClellan G.B., Levine R., Winegrad S. Multiple forms of cardiac myosin binding protein-C exist and can regulate thick filament stability. J Gen Physiol 2007, 129:419-428.
    • (2007) J Gen Physiol , vol.129 , pp. 419-428
    • Kulikovskaya, I.1    McClellan, G.B.2    Levine, R.3    Winegrad, S.4
  • 16
    • 14044262241 scopus 로고    scopus 로고
    • Myosin binding protein C phosphorylation, myofibril structure, and contractile function during low flow ischemia
    • Decker R.S., Decker M.L., Kulikovskaya I., Nakamura S., Lee D.C., Harris K., et al. Myosin binding protein C phosphorylation, myofibril structure, and contractile function during low flow ischemia. Circulation 2005, 111:906-912.
    • (2005) Circulation , vol.111 , pp. 906-912
    • Decker, R.S.1    Decker, M.L.2    Kulikovskaya, I.3    Nakamura, S.4    Lee, D.C.5    Harris, K.6
  • 18
    • 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 F.S., McDonald K.S., Harris S.P., Moss R.L. 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
  • 20
    • 0037155775 scopus 로고    scopus 로고
    • Hypertrophic cardiomyopathy in cardiac myosin binding protein-C knockout mice
    • Harris S., Bartley T., Hacker K., McDonald P., Douglas M., Greaser M., et al. Hypertrophic cardiomyopathy in cardiac myosin binding protein-C knockout mice. Circ Res 2002, 90:594-601.
    • (2002) Circ Res , vol.90 , pp. 594-601
    • Harris, S.1    Bartley, T.2    Hacker, K.3    McDonald, P.4    Douglas, M.5    Greaser, M.6
  • 22
    • 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
  • 23
    • 2442698889 scopus 로고    scopus 로고
    • Role of cardiac myosin binding protein C in sustaining left ventricular systolic stiffening
    • Palmer B.M., Georgakopoulos D., Janssen P.M., Wang Y., Alpert N.R., Belardi D.F., et al. Role of cardiac myosin binding protein C in sustaining left ventricular systolic stiffening. Circ Res 2004, 94:1249-1255.
    • (2004) Circ Res , vol.94 , pp. 1249-1255
    • Palmer, B.M.1    Georgakopoulos, D.2    Janssen, P.M.3    Wang, Y.4    Alpert, N.R.5    Belardi, D.F.6
  • 24
    • 0034907680 scopus 로고    scopus 로고
    • Changes in cardiac contractility related to calcium-mediated changes in phosphorylation of myosin binding protein C
    • McClellan G., Kulikovskaya I., Winegrad S. Changes in cardiac contractility related to calcium-mediated changes in phosphorylation of myosin binding protein C. Biophys J 2001, 81:1083-1092.
    • (2001) Biophys J , vol.81 , pp. 1083-1092
    • McClellan, G.1    Kulikovskaya, I.2    Winegrad, S.3
  • 25
    • 0037131207 scopus 로고    scopus 로고
    • Identification of novel interactions between domains of myosin binding protein-C that are modulated by hypertrophic cardiomyopathy missense mutations
    • Moolman-Smook J., Flashman W., de Lange Z., Corfield V., Redwood C., Watkins H. Identification of novel interactions between domains of myosin binding protein-C that are modulated by hypertrophic cardiomyopathy missense mutations. Circ Res 2002, 91:704-711.
    • (2002) Circ Res , vol.91 , pp. 704-711
    • Moolman-Smook, J.1    Flashman, W.2    de Lange, Z.3    Corfield, V.4    Redwood, C.5    Watkins, H.6
  • 27
    • 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 K.R., Gruen M., Uttenweiller D., Gautel M., Fink H.A.R. 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    Uttenweiller, D.4    Gautel, M.5    Fink, H.A.R.6
  • 28
    • 33644674009 scopus 로고    scopus 로고
    • Cardiac myosin binding protein-C phosphorylation and cardiac function
    • Sadayappan S., Gulick J., Osinska H., Martin Lisa A., Harvey S., et al. Cardiac myosin binding protein-C phosphorylation and cardiac function. Circ Res 2005, 97:1156-1163.
    • (2005) Circ Res , vol.97 , pp. 1156-1163
    • Sadayappan, S.1    Gulick, J.2    Osinska, H.3    Martin, L.A.4    Harvey, S.5
  • 29
    • 33644874505 scopus 로고    scopus 로고
    • Resting blood flow in hypocontractile myocardium: resolving thecontroversy
    • Klocke F.J. Resting blood flow in hypocontractile myocardium: resolving thecontroversy. Circulation 2005, 112:3222-3224.
    • (2005) Circulation , vol.112 , pp. 3222-3224
    • Klocke, F.J.1
  • 30
    • 0025727168 scopus 로고
    • Phosphorylation of chicken cardiac C protein by calcium-dependent protein kinase II
    • Schlender K., Bean L. Phosphorylation of chicken cardiac C protein by calcium-dependent protein kinase II. J Biol Chem 1991, 266:2811-2817.
    • (1991) J Biol Chem , vol.266 , pp. 2811-2817
    • Schlender, K.1    Bean, L.2
  • 31
    • 0021713707 scopus 로고
    • Phosphorylation of purified cardiac muscle kinase protein by purified cAMP-dependent and endogenous Ca-calmodulin-dependent protein
    • Hartzell H.C., Glass D.D. Phosphorylation of purified cardiac muscle kinase protein by purified cAMP-dependent and endogenous Ca-calmodulin-dependent protein. J Biol Chem 1984, 259:15587-15596.
    • (1984) J Biol Chem , vol.259 , pp. 15587-15596
    • Hartzell, H.C.1    Glass, D.D.2
  • 32
    • 40649098633 scopus 로고    scopus 로고
    • Three-dimensional structure of vertebrate cardiac muscle myosin filaments
    • Zoghbi M.E., Woodhead J.L., Moss R.L., Craig R. Three-dimensional structure of vertebrate cardiac muscle myosin filaments. Proc Natl Acad Sci U S A 2008, 105:2386-2390.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 2386-2390
    • Zoghbi, M.E.1    Woodhead, J.L.2    Moss, R.L.3    Craig, R.4
  • 34
    • 66449110385 scopus 로고    scopus 로고
    • The myosin-binding protein C motif binds to F-actin in a phosphorylation-sensitive manner
    • Shaffer J.F., Kensler R.W., Harris S.P. The myosin-binding protein C motif binds to F-actin in a phosphorylation-sensitive manner. J Biol Chem 2009, 284:12318-12327.
    • (2009) J Biol Chem , vol.284 , pp. 12318-12327
    • Shaffer, J.F.1    Kensler, R.W.2    Harris, S.P.3
  • 35
    • 71049170111 scopus 로고    scopus 로고
    • Phosphorylation of contractile proteins in response to alpha and beta adrenergic stimulation in neonatal cardiomyocytes
    • Decker R.S., Rines A.K., Nakamura S., Naik T.J., Wassertsrom J.A., Ardehali H. Phosphorylation of contractile proteins in response to alpha and beta adrenergic stimulation in neonatal cardiomyocytes. Transl Res 2010, 155:27-34.
    • (2010) Transl Res , vol.155 , pp. 27-34
    • Decker, R.S.1    Rines, A.K.2    Nakamura, S.3    Naik, T.J.4    Wassertsrom, J.A.5    Ardehali, H.6
  • 36
    • 84859650518 scopus 로고    scopus 로고
    • Altered MyBP-C phosphorylation pattern and loss of myosin content in congestive heart failure
    • [Abstracts of Annual Meeting]
    • Paolucci N., Toniolo L., Kulikovskaya I., Katori T., Kass D.A., Reggiani C., et al. Altered MyBP-C phosphorylation pattern and loss of myosin content in congestive heart failure. Biophys J 2006, [Abstracts of Annual Meeting].
    • (2006) Biophys J
    • Paolucci, N.1    Toniolo, L.2    Kulikovskaya, I.3    Katori, T.4    Kass, D.A.5    Reggiani, C.6
  • 37
    • 0033570292 scopus 로고    scopus 로고
    • Self-protection by cardiac myocytes against hypoxia and hyperoxia
    • Winegrad S., Henrion D., Rappaport L., Samuel J.-L. Self-protection by cardiac myocytes against hypoxia and hyperoxia. Circ Res 1999, 85:690-698.
    • (1999) Circ Res , vol.85 , pp. 690-698
    • Winegrad, S.1    Henrion, D.2    Rappaport, L.3    Samuel, J.-L.4
  • 38
    • 0027490199 scopus 로고
    • Evidence for the existence of endothelial factors regulating contractility in rat heart
    • Winegrad S. Evidence for the existence of endothelial factors regulating contractility in rat heart. Adv Exp Med Biol 1993, 332:155-163.
    • (1993) Adv Exp Med Biol , vol.332 , pp. 155-163
    • Winegrad, S.1
  • 39
    • 0027461422 scopus 로고
    • Cardiac endothelial cells modulate contractility of rat heart in response to oxygen tension and coronary flow
    • Ramaciotti C., McClellan G., Sharkey A., Rose D., Weisberg A., Winegrad S. Cardiac endothelial cells modulate contractility of rat heart in response to oxygen tension and coronary flow. Circ Res 1993, 72:1044-1064.
    • (1993) Circ Res , vol.72 , pp. 1044-1064
    • Ramaciotti, C.1    McClellan, G.2    Sharkey, A.3    Rose, D.4    Weisberg, A.5    Winegrad, S.6
  • 40
    • 0026569131 scopus 로고
    • Contractile proteins in myocardial cells are regulated by factor(s) released by blood vessels
    • McClellan G., Weisberg A., Kato N., Ramaciotti C., Sharkey A., Winegrad S. Contractile proteins in myocardial cells are regulated by factor(s) released by blood vessels. Circ Res 1992, 70:787-803.
    • (1992) Circ Res , vol.70 , pp. 787-803
    • McClellan, G.1    Weisberg, A.2    Kato, N.3    Ramaciotti, C.4    Sharkey, A.5    Winegrad, S.6
  • 41
    • 0025743813 scopus 로고
    • A physiological basis for variation in the contractile properties of isolated rat heart
    • Lin L.-E., McClellan G., Weisberg A., Winegrad S. A physiological basis for variation in the contractile properties of isolated rat heart. J Physiol (Lond) 1991, 73-94.
    • (1991) J Physiol (Lond) , pp. 73-94
    • Lin, L.-E.1    McClellan, G.2    Weisberg, A.3    Winegrad, S.4
  • 42
    • 0028341236 scopus 로고
    • Endothelial cell storage and release of endothelin as a cardioregulatory mechanism
    • McClellan G., Weisberg A., Rose D., Winegrad S. Endothelial cell storage and release of endothelin as a cardioregulatory mechanism. Circ Res 1994, 75:85-96.
    • (1994) Circ Res , vol.75 , pp. 85-96
    • McClellan, G.1    Weisberg, A.2    Rose, D.3    Winegrad, S.4
  • 43
    • 0025320651 scopus 로고
    • Effect of thyroid hormone on the accumulation of mRNA for skeletal and cardiac alpha-actin in hearts from normal and hypophysectomized rats
    • Winegrad S., Wisnewsky, Schwartz K. Effect of thyroid hormone on the accumulation of mRNA for skeletal and cardiac alpha-actin in hearts from normal and hypophysectomized rats. Proc Natl Acad Sci U S A 1990, 87:2456-2460.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 2456-2460
    • Winegrad, S.1    Wisnewsky2    Schwartz, K.3
  • 44
    • 0023277546 scopus 로고
    • Isozyme specific modification of myosin ATPase by cAMP in rat heart
    • Winegrad S., Weisberg A. Isozyme specific modification of myosin ATPase by cAMP in rat heart. Circ Res 1987, 60:384-392.
    • (1987) Circ Res , vol.60 , pp. 384-392
    • Winegrad, S.1    Weisberg, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.