메뉴 건너뛰기




Volumn 117, Issue 12, 2014, Pages 1471-1477

Impact of familial hypertrophic cardiomyopathy-linked mutations in the NH2 terminus of the RLC on β-myosin cross-bridge mechanics

Author keywords

Cardiac ventricular myosin; Hypertrophic cardiomyopathy; In vitro motility; Myosin regulatory light chain

Indexed keywords

CARDIAC MYOSIN; MYOSIN HEAVY CHAIN; MYOSIN LIGHT CHAIN; PROTEIN BINDING; RECOMBINANT PROTEIN;

EID: 84979862406     PISSN: 87507587     EISSN: 15221601     Source Type: Journal    
DOI: 10.1152/japplphysiol.00798.2014     Document Type: Article
Times cited : (11)

References (51)
  • 3
    • 84874040668 scopus 로고    scopus 로고
    • Regulatory light chain mutants linked to heart disease modify the cardiac myosin lever arm
    • Burghardt TP, Sikkink LA. Regulatory light chain mutants linked to heart disease modify the cardiac myosin lever arm. Biochemistry 52: 1249-1259, 2013.
    • (2013) Biochemistry , vol.52 , pp. 1249-1259
    • Burghardt, T.P.1    Sikkink, L.A.2
  • 4
    • 0033051742 scopus 로고    scopus 로고
    • Regulatory light chain mutations affect myosin motor function and kinetics
    • Chaudoir BM, Kowalczyk PA, Chisholm RL. Regulatory light chain mutations affect myosin motor function and kinetics. J Cell Sci 112: 1611-1620, 1999.
    • (1999) J Cell Sci , vol.112 , pp. 1611-1620
    • Chaudoir, B.M.1    Kowalczyk, P.A.2    Chisholm, R.L.3
  • 5
    • 0036286168 scopus 로고    scopus 로고
    • Kinetic effects of myosin regulatory light chain phosphorylation on skeletal muscle contraction
    • Davis JS, Satorius CL, Epstein ND. Kinetic effects of myosin regulatory light chain phosphorylation on skeletal muscle contraction. Biophys J 83: 359-370, 2002.
    • (2002) Biophys J , vol.83 , pp. 359-370
    • Davis, J.S.1    Satorius, C.L.2    Epstein, N.D.3
  • 7
    • 33751184622 scopus 로고    scopus 로고
    • E22K mutation of RLC that causes familial hypertrophic cardiomyopathy in heterozygous mouse myocardium: Effect on crossbridge kinetics
    • Dumka D, Talent J, Akopova I, Guzman G, Szczesna-Cordary D, Borejdo J. E22K mutation of RLC that causes familial hypertrophic cardiomyopathy in heterozygous mouse myocardium: effect on crossbridge kinetics. Am J Physiol Heart Circ Physiol 291: H2098-H2106, 2006.
    • (2006) Am J Physiol Heart Circ Physiol , vol.291 , pp. H2098-H2106
    • Dumka, D.1    Talent, J.2    Akopova, I.3    Guzman, G.4    Szczesna-Cordary, D.5    Borejdo, J.6
  • 9
    • 70349466537 scopus 로고    scopus 로고
    • Phosphorylation and the N-terminal extension of the regulatory light chain help orient and align the myosin heads in Drosophila flight muscle
    • Farman GP, Miller MS, Reedy MC, Soto-Adames FN, Vigoreaux JO, Maughan DW, Irving TC. Phosphorylation and the N-terminal extension of the regulatory light chain help orient and align the myosin heads in Drosophila flight muscle. J Struct Biol 168: 240-249, 2009.
    • (2009) J Struct Biol , vol.168 , pp. 240-249
    • Farman, G.P.1    Miller, M.S.2    Reedy, M.C.3    Soto-Adames, F.N.4    Vigoreaux, J.O.5    Maughan, D.W.6    Irving, T.C.7
  • 10
    • 78049252301 scopus 로고    scopus 로고
    • Cardiomyopathy-linked myosin regulatory light chain mutations disrupt myosin strain-dependent biochemistry
    • Greenberg MJ, Kazmierczak K, Szczesna-Cordary D, Moore JR. Cardiomyopathy-linked myosin regulatory light chain mutations disrupt myosin strain-dependent biochemistry. Proc Natl Acad Sci USA 107: 17403-17408, 2010.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 17403-17408
    • Greenberg, M.J.1    Kazmierczak, K.2    Szczesna-Cordary, D.3    Moore, J.R.4
  • 12
    • 0030773824 scopus 로고    scopus 로고
    • Molecular motors: Structural adaptations to cellular functions
    • Howard J. Molecular motors: structural adaptations to cellular functions. Nature 389: 561-567, 1997.
    • (1997) Nature , vol.389 , pp. 561-567
    • Howard, J.1
  • 13
    • 0015236610 scopus 로고
    • Proposed mechanism of force generation in striated muscle
    • Huxley AF, Simmons RM. Proposed mechanism of force generation in striated muscle. Nature 233: 533-538, 1971.
    • (1971) Nature , vol.233 , pp. 533-538
    • Huxley, A.F.1    Simmons, R.M.2
  • 14
    • 0025368569 scopus 로고
    • Sliding filaments and molecular motile systems
    • Huxley HE. Sliding filaments and molecular motile systems. J Biol Chem 265: 8347-8350, 1990.
    • (1990) J Biol Chem , vol.265 , pp. 8347-8350
    • Huxley, H.E.1
  • 17
    • 84863053181 scopus 로고    scopus 로고
    • Myosin regulatory light chain mutation found in hypertrophic cardiomyopathy patients increases isometric force production in transgenic mice
    • Kazmierczak K, Muthu P, Huang W, Jones M, Wang Y, Szczesna-Cordary D. Myosin regulatory light chain mutation found in hypertrophic cardiomyopathy patients increases isometric force production in transgenic mice. Biochem J 442: 95-103, 2012.
    • (2012) Biochem J , vol.442 , pp. 95-103
    • Kazmierczak, K.1    Muthu, P.2    Huang, W.3    Jones, M.4    Wang, Y.5    Szczesna-Cordary, D.6
  • 18
    • 61449250645 scopus 로고    scopus 로고
    • Malignant familial hypertrophic cardiomyopathy D166V mutation in the ventricular myosin regulatory light chain causes profound effects in skinned and intact papillary muscle fibers from transgenic mice
    • Kerrick WG, Kazmierczak K, Xu Y, Wang Y, Szczesna-Cordary D. Malignant familial hypertrophic cardiomyopathy D166V mutation in the ventricular myosin regulatory light chain causes profound effects in skinned and intact papillary muscle fibers from transgenic mice. FASEB J 23: 855-865, 2009.
    • (2009) FASEB J , vol.23 , pp. 855-865
    • Kerrick, W.G.1    Kazmierczak, K.2    Xu, Y.3    Wang, Y.4    Szczesna-Cordary, D.5
  • 19
    • 0032532501 scopus 로고    scopus 로고
    • Thiophosphorylation of myosin light chain increases rigor stiffness of rabbit smooth muscle
    • Khromov AS, Somlyo AV, Somlyo AP. Thiophosphorylation of myosin light chain increases rigor stiffness of rabbit smooth muscle. J Physiol 512: 345-350, 1998.
    • (1998) J Physiol , vol.512 , pp. 345-350
    • Khromov, A.S.1    Somlyo, A.V.2    Somlyo, A.P.3
  • 20
    • 0031663377 scopus 로고    scopus 로고
    • Structural and functional responses of mammalian thick filaments to alterations in myosin regulatory light chains
    • Levine RJ, Yang Z, Epstein ND, Fananapazir L, Stull JT, Sweeney HL. Structural and functional responses of mammalian thick filaments to alterations in myosin regulatory light chains. J Struct Biol 122: 149-161, 1998.
    • (1998) J Struct Biol , vol.122 , pp. 149-161
    • Levine, R.J.1    Yang, Z.2    Epstein, N.D.3    Fananapazir, L.4    Stull, J.T.5    Sweeney, H.L.6
  • 22
    • 0037070514 scopus 로고    scopus 로고
    • Hypertrophic cardiomyopathy: A systematic review
    • Maron BJ. Hypertrophic cardiomyopathy: a systematic review. JAMA 287: 1308-1320, 2002.
    • (2002) JAMA , vol.287 , pp. 1308-1320
    • Maron, B.J.1
  • 23
    • 84865127014 scopus 로고    scopus 로고
    • Genetics of hypertrophic cardiomyopathy after 20 years: Clinical perspectives
    • Maron BJ, Maron MS, Semsarian C. Genetics of hypertrophic cardiomyopathy after 20 years: clinical perspectives. J Am Coll Cardiol 60: 705-715, 2012.
    • (2012) J Am Coll Cardiol , vol.60 , pp. 705-715
    • Maron, B.J.1    Maron, M.S.2    Semsarian, C.3
  • 24
    • 0034008021 scopus 로고    scopus 로고
    • The effect of removing the N-terminal extension of the Drosophila myosin regulatory light chain upon flight ability and the contractile dynamics of indirect flight muscle
    • Moore JR, Dickinson MH, Vigoreaux JO, Maughan DW. The effect of removing the N-terminal extension of the Drosophila myosin regulatory light chain upon flight ability and the contractile dynamics of indirect flight muscle. Biophys J 78: 1431-1440, 2000.
    • (2000) Biophys J , vol.78 , pp. 1431-1440
    • Moore, J.R.1    Dickinson, M.H.2    Vigoreaux, J.O.3    Maughan, D.W.4
  • 26
    • 0035969240 scopus 로고    scopus 로고
    • Myosin v exhibits a high duty cycle and large unitary displacement
    • Moore JR, Krementsova EB, Trybus KM, Warshaw DM. Myosin V exhibits a high duty cycle and large unitary displacement. J Cell Biol 155: 625-635, 2001.
    • (2001) J Cell Biol , vol.155 , pp. 625-635
    • Moore, J.R.1    Krementsova, E.B.2    Trybus, K.M.3    Warshaw, D.M.4
  • 27
    • 84864230812 scopus 로고    scopus 로고
    • Understanding cardiomyopathy phenotypes based on the functional impact of mutations in the myosin motor
    • Moore JR, Leinwand L, Warshaw DM. Understanding cardiomyopathy phenotypes based on the functional impact of mutations in the myosin motor. Circ Res 111: 375-385, 2012.
    • (2012) Circ Res , vol.111 , pp. 375-385
    • Moore, J.R.1    Leinwand, L.2    Warshaw, D.M.3
  • 28
    • 84863058123 scopus 로고    scopus 로고
    • The effect of myosin RLC phosphorylation in normal and cardiomyopathic mouse hearts
    • Muthu P, Kazmierczak K, Jones M, Szczesna-Cordary D. The effect of myosin RLC phosphorylation in normal and cardiomyopathic mouse hearts. J Cell Mol Med 16: 911-919, 2012.
    • (2012) J Cell Mol Med , vol.16 , pp. 911-919
    • Muthu, P.1    Kazmierczak, K.2    Jones, M.3    Szczesna-Cordary, D.4
  • 29
    • 84901843447 scopus 로고    scopus 로고
    • In vitro rescue study of a malignant familial hypertrophic cardiomyopathy phenotype by pseudo-phosphorylation of myosin regulatory light chain
    • Muthu P, Liang J, Schmidt W, Moore JR, Szczesna-Cordary D. In vitro rescue study of a malignant familial hypertrophic cardiomyopathy phenotype by pseudo-phosphorylation of myosin regulatory light chain. Arch Biochem Biophys 552-553: 29-39, 2014.
    • (2014) Arch Biochem Biophys , vol.552-553 , pp. 29-39
    • Muthu, P.1    Liang, J.2    Schmidt, W.3    Moore, J.R.4    Szczesna-Cordary, D.5
  • 31
    • 9344244157 scopus 로고    scopus 로고
    • + sensitivity of force and activation dependence of the kinetics of myocardial force development
    • Olsson MC, Patel JR, Fitzsimons DP, Walker JW, Moss RL. Basal myosin light chain phosphorylation is a determinant of Ca2+ sensitivity of force and activation dependence of the kinetics of myocardial force development. Am J Physiol Heart Circ Physiol 287: H2712-H2718, 2004.
    • (2004) Am J Physiol Heart Circ Physiol , vol.287 , pp. H2712-H2718
    • Olsson, M.C.1    Patel, J.R.2    Fitzsimons, D.P.3    Walker, J.W.4    Moss, R.L.5
  • 32
    • 70349655895 scopus 로고    scopus 로고
    • Removal of the cardiac myosin regulatory light chain increases isometric force production
    • Pant K, Watt J, Greenberg M, Jones M, Szczesna-Cordary D, Moore JR. Removal of the cardiac myosin regulatory light chain increases isometric force production. FASEB J 23: 3571-3580, 2009.
    • (2009) FASEB J , vol.23 , pp. 3571-3580
    • Pant, K.1    Watt, J.2    Greenberg, M.3    Jones, M.4    Szczesna-Cordary, D.5    Moore, J.R.6
  • 33
    • 0033555870 scopus 로고    scopus 로고
    • Changes in conformation of myosin heads during the development of isometric contraction and rapid shortening in single frog muscle fibres
    • Piazzesi G, Reconditi M, Dobbie I, Linari M, Boesecke P, Diat O, Irving M, Lombardi V. Changes in conformation of myosin heads during the development of isometric contraction and rapid shortening in single frog muscle fibres. J Physiol 514: 305-312, 1999.
    • (1999) J Physiol , vol.514 , pp. 305-312
    • Piazzesi, G.1    Reconditi, M.2    Dobbie, I.3    Linari, M.4    Boesecke, P.5    Diat, O.6    Irving, M.7    Lombardi, V.8
  • 39
    • 3343010238 scopus 로고    scopus 로고
    • A point mutation in the regulatory light chain reduces the step size of skeletal muscle myosin
    • Sherwood JJ, Waller GS, Warshaw DM, Lowey S. A point mutation in the regulatory light chain reduces the step size of skeletal muscle myosin. Proc Natl Acad Sci USA 101: 10973-10978, 2004.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 10973-10978
    • Sherwood, J.J.1    Waller, G.S.2    Warshaw, D.M.3    Lowey, S.4
  • 40
    • 33748097336 scopus 로고    scopus 로고
    • Acceleration of stretch activation in murine myocardium due to phosphorylation of myosin regulatory light chain
    • Stelzer JE, Patel JR, Moss RL. Acceleration of stretch activation in murine myocardium due to phosphorylation of myosin regulatory light chain. J Gen Physiol 128: 261-272, 2006.
    • (2006) J Gen Physiol , vol.128 , pp. 261-272
    • Stelzer, J.E.1    Patel, J.R.2    Moss, R.L.3
  • 41
    • 0038103786 scopus 로고    scopus 로고
    • Regulatory light chains of striated muscle myosin. Structure, function and malfunction
    • Szczesna D. Regulatory light chains of striated muscle myosin. Structure, function and malfunction. Curr Drug Targets Cardiovasc Haematol Disord 3: 187-197, 2003.
    • (2003) Curr Drug Targets Cardiovasc Haematol Disord , vol.3 , pp. 187-197
    • Szczesna, D.1
  • 43
    • 0036095636 scopus 로고    scopus 로고
    • + sensitivity of skeletal muscle contraction
    • Szczesna D, Zhao J, Jones M, Zhi G, Stull J, Potter JD. Phosphorylation of the regulatory light chains of myosin affects Ca2+ sensitivity of skeletal muscle contraction. J Appl Physiol 92: 1661-1670, 2002.
    • (2002) J Appl Physiol , vol.92 , pp. 1661-1670
    • Szczesna, D.1    Zhao, J.2    Jones, M.3    Zhi, G.4    Stull, J.5    Potter, J.D.6
  • 44
    • 0942276371 scopus 로고    scopus 로고
    • + binding of human cardiac myosin regulatory light chain affect cardiac muscle contraction
    • Szczesna-Cordary D, Guzman G, Ng SS, Zhao J. Familial hypertrophic cardiomyopathy-linked alterations in Ca2+ binding of human cardiac myosin regulatory light chain affect cardiac muscle contraction. J Biol Chem 279: 3535-3542, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 3535-3542
    • Szczesna-Cordary, D.1    Guzman, G.2    Ng, S.S.3    Zhao, J.4
  • 47
    • 0029913456 scopus 로고    scopus 로고
    • The neck region of the myosin motor domain acts as a lever arm to generate movement
    • Uyeda TQ, Abramson PD, Spudich JA. The neck region of the myosin motor domain acts as a lever arm to generate movement. Proc Natl Acad Sci USA 93: 4459-4464, 1996.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4459-4464
    • Uyeda, T.Q.1    Abramson, P.D.2    Spudich, J.A.3
  • 48
    • 0024991350 scopus 로고
    • Myosin step size. Estimation from slow sliding movement of actin over low densities of heavy meromyosin
    • Uyeda TQ, Kron SJ, Spudich JA. Myosin step size. Estimation from slow sliding movement of actin over low densities of heavy meromyosin. J Mol Biol 214: 699-710, 1990.
    • (1990) J Mol Biol , vol.214 , pp. 699-710
    • Uyeda, T.Q.1    Kron, S.J.2    Spudich, J.A.3
  • 49
    • 26944449015 scopus 로고    scopus 로고
    • Load-dependent kinetics of myosin-V can explain its high processivity
    • Veigel C, Schmitz S, Wang F, Sellers JR. Load-dependent kinetics of myosin-V can explain its high processivity. Nat Cell Biol 7: 861-869, 2005.
    • (2005) Nat Cell Biol , vol.7 , pp. 861-869
    • Veigel, C.1    Schmitz, S.2    Wang, F.3    Sellers, J.R.4
  • 50
    • 84879163358 scopus 로고    scopus 로고
    • Contractile protein phosphorylation predicts human heart disease phenotypes
    • Walker LA, Fullerton DA, Buttrick PM. Contractile protein phosphorylation predicts human heart disease phenotypes. Am J Physiol Heart Circ Physiol 304: H1644-H1650, 2013.
    • (2013) Am J Physiol Heart Circ Physiol , vol.304 , pp. H1644-H1650
    • Walker, L.A.1    Fullerton, D.A.2    Buttrick, P.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.