메뉴 건너뛰기




Volumn 34, Issue 4, 2002, Pages 469-482

In vitro motility analysis of thin filaments from failing and non-failing human heart: Troponin from failing human hearts induces slower filament sliding and higher Ca2+ sensitivity

Author keywords

Ca2+ regulation; Heart failure; In vitro motility; Phosphorylation; Troponin

Indexed keywords

ACTIN; CALCIUM ION; MYOSIN HEAVY CHAIN; TROPOMYOSIN; TROPONIN I; TROPONIN T; CALCIUM; ISOPROTEIN; PHOSPHATASE; PHOSPHOTRANSFERASE; TROPONIN;

EID: 0036547621     PISSN: 00222828     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmcc.2002.1528     Document Type: Article
Times cited : (35)

References (53)
  • 1
    • 0032145260 scopus 로고    scopus 로고
    • Cellular and molecular aspects of contractile dysfunction in heart failure
    • Mittmann C., Eschenhagen T., Scholz H. Cellular and molecular aspects of contractile dysfunction in heart failure. Cardiovasc Res. 39:1998;267-275.
    • (1998) Cardiovasc Res , vol.39 , pp. 267-275
    • Mittmann, C.1    Eschenhagen, T.2    Scholz, H.3
  • 2
    • 0345490810 scopus 로고    scopus 로고
    • Origin of contractile dysfunction in heart failure: Calcium cycling versus myofilaments
    • Perez N.G., Hashimoto K., McCune S., Altschuld R.A., Marban E. Origin of contractile dysfunction in heart failure: calcium cycling versus myofilaments. Circulation. 99:1999;1077-1083.
    • (1999) Circulation , vol.99 , pp. 1077-1083
    • Perez, N.G.1    Hashimoto, K.2    McCune, S.3    Altschuld, R.A.4    Marban, E.5
  • 4
    • 0027222795 scopus 로고
    • Control of myofilament activation in heart failure
    • Solaro J., Powers F., Gao L., Gwathmey J. Control of myofilament activation in heart failure. Circulation. 87 (Suppl. VII):1993;VII-38-VII-43.
    • (1993) Circulation , vol.87 , Issue.7 SUPPL.
    • Solaro, J.1    Powers, F.2    Gao, L.3    Gwathmey, J.4
  • 5
    • 0023814263 scopus 로고
    • Changes in myofibrillar content and Mg-ATPase activity in ventricular tissues from patients with heart failure caused by coronary artery disease, cardiomyopathy, or mitral valve insufficiency
    • Pagani E., Alousi A., Grant A., Older T., Dziuban S., Allen P. Changes in myofibrillar content and Mg-ATPase activity in ventricular tissues from patients with heart failure caused by coronary artery disease, cardiomyopathy, or mitral valve insufficiency. Circ Res. 63:1988;380-385.
    • (1988) Circ Res , vol.63 , pp. 380-385
    • Pagani, E.1    Alousi, A.2    Grant, A.3    Older, T.4    Dziuban, S.5    Allen, P.6
  • 6
    • 0026491850 scopus 로고
    • Responsiveness of the myofilaments to Ca2+ in human heart failure: Implications for Ca2+ and force regulation
    • Hajjar R.J., Grossman W., Gwathmey J.K. Responsiveness of the myofilaments to Ca2+ in human heart failure: implications for Ca2+ and force regulation. Basic Res Cardiol. 87:1992;143-159.
    • (1992) Basic Res Cardiol , vol.87 , pp. 143-159
    • Hajjar, R.J.1    Grossman, W.2    Gwathmey, J.K.3
  • 7
    • 0030015928 scopus 로고    scopus 로고
    • Myofibrillar calcium sensitivity of isometric tension is increased in human dilated cardiomyopathies
    • Wolff M., Buck S., Stoker S., Greaser M., Mentzer R. Myofibrillar calcium sensitivity of isometric tension is increased in human dilated cardiomyopathies. J Clin Invest. 98:1996;167-176.
    • (1996) J Clin Invest , vol.98 , pp. 167-176
    • Wolff, M.1    Buck, S.2    Stoker, S.3    Greaser, M.4    Mentzer, R.5
  • 8
    • 17744416349 scopus 로고    scopus 로고
    • Changes in essential myosin light chain isoform expression provide a molecular basis for isometric force regulation in the failing human heart
    • Morano I., Hadicke K., Haase H., Bohm M., Erdmann E., Schaub M.C. Changes in essential myosin light chain isoform expression provide a molecular basis for isometric force regulation in the failing human heart. J Mol Cell Cardiol. 29:1997;1177-1187.
    • (1997) J Mol Cell Cardiol , vol.29 , pp. 1177-1187
    • Morano, I.1    Hadicke, K.2    Haase, H.3    Bohm, M.4    Erdmann, E.5    Schaub, M.C.6
  • 9
    • 0000973094 scopus 로고    scopus 로고
    • Altered contractile function in heart failure
    • de Tombe P.P. Altered contractile function in heart failure. Cardiovasc Res. 37:1998;367-380.
    • (1998) Cardiovasc Res , vol.37 , pp. 367-380
    • De Tombe, P.P.1
  • 12
    • 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 J.W., Owen V.J., Burton P.B., Stienen G.J. Effect of protein kinase A on calcium sensitivity of force and its sarcomere length dependence in human cardiomyocytes. Cardiovasc Res. 46:2000;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.4    Stienen, G.J.5
  • 15
    • 0028983138 scopus 로고
    • Cardiac V1 and V3 myosins differ in their hydrolytic and mechanical activities in vitro
    • VanBuren P., Harris D.E., Alpert N.R., Warshaw D.M. Cardiac V1 and V3 myosins differ in their hydrolytic and mechanical activities in vitro. Circ Res. 77:1995;439-444.
    • (1995) Circ Res , vol.77 , pp. 439-444
    • VanBuren, P.1    Harris, D.E.2    Alpert, N.R.3    Warshaw, D.M.4
  • 16
    • 85031061616 scopus 로고    scopus 로고
    • Contribution of cardiac myosin isoforms to calcium-sensitive mechanical performance: Implications in human myocardial failure
    • Alix S.L., Begin K.J., LeWinter M.M., Alpert N.R., VanBuren P. Contribution of cardiac myosin isoforms to calcium-sensitive mechanical performance: implications in human myocardial failure. Biophys J. 80:2001;260a.
    • (2001) Biophys J , vol.80
    • Alix, S.L.1    Begin, K.J.2    LeWinter, M.M.3    Alpert, N.R.4    VanBuren, P.5
  • 18
    • 0030056230 scopus 로고    scopus 로고
    • Maximal actomyosin ATPase activity and in vitro myosin motility are unaltered in human mitral regurgitation heart failure
    • Nguyen T.T., Hayes E., Mulieri L.A., Leavitt B.J., ter Keurs H.E., Alpert N.R., Warshaw D.M. Maximal actomyosin ATPase activity and in vitro myosin motility are unaltered in human mitral regurgitation heart failure. Circ Res. 79:1996;222-226.
    • (1996) Circ Res , vol.79 , pp. 222-226
    • Nguyen, T.T.1    Hayes, E.2    Mulieri, L.A.3    Leavitt, B.J.4    Ter Keurs, H.E.5    Alpert, N.R.6    Warshaw, D.M.7
  • 19
    • 0025934457 scopus 로고
    • Troponin T isoform expression in humans. A comparison among normal and failing heart, fetal heart and adult and fetal skeletal muscle
    • Anderson P.A.W., Malouf N.N., Oakeley A.E., Pagani E.D., Allen P.D. Troponin T isoform expression in humans. A comparison among normal and failing heart, fetal heart and adult and fetal skeletal muscle. Circ Res. 69:1991;1226-1233.
    • (1991) Circ Res , vol.69 , pp. 1226-1233
    • Anderson, P.A.W.1    Malouf, N.N.2    Oakeley, A.E.3    Pagani, E.D.4    Allen, P.D.5
  • 21
    • 0029811697 scopus 로고    scopus 로고
    • Cardiac troponin T isoform expression correlates with pathophysiological descriptors in patients who underwent corrective surgery for congenital heart disease
    • Saba Z., Nassar R., Ungerleider R., Oakeley A., Anderson P. Cardiac troponin T isoform expression correlates with pathophysiological descriptors in patients who underwent corrective surgery for congenital heart disease. Circulation. 94:1996;472-476.
    • (1996) Circulation , vol.94 , pp. 472-476
    • Saba, Z.1    Nassar, R.2    Ungerleider, R.3    Oakeley, A.4    Anderson, P.5
  • 23
    • 0033514391 scopus 로고    scopus 로고
    • Protein kinase A (PKA)-dependent troponin-I phosphorylation and PKA regulatory subunits are decreased in human dilated cardiomyopathy
    • Zakhary D.R., Moravec C.S., Stewart R.W., Bond M. Protein kinase A (PKA)-dependent troponin-I phosphorylation and PKA regulatory subunits are decreased in human dilated cardiomyopathy. Circulation. 99:1999;505-510.
    • (1999) Circulation , vol.99 , pp. 505-510
    • Zakhary, D.R.1    Moravec, C.S.2    Stewart, R.W.3    Bond, M.4
  • 24
    • 0032830884 scopus 로고    scopus 로고
    • Functional analysis of human cardiac troponin by the in vitro motility assay: Comparison of adult, foetal and failing hearts
    • Purcell I.F., Bing W., Marston S.B. Functional analysis of human cardiac troponin by the in vitro motility assay: comparison of adult, foetal and failing hearts. Cardiovasc Res. 43:1999;884-891.
    • (1999) Cardiovasc Res , vol.43 , pp. 884-891
    • Purcell, I.F.1    Bing, W.2    Marston, S.B.3
  • 26
    • 0028953460 scopus 로고
    • In vitro motility analysis of actin-tropomyosin regulation by troponin and Ca2+: The thin filament is switched as a single cooperative unit
    • Fraser I.D.C., Marston S.B. In vitro motility analysis of actin-tropomyosin regulation by troponin and Ca2+: the thin filament is switched as a single cooperative unit. J Biol Chem. 270:1995;7836-7841.
    • (1995) J Biol Chem , vol.270 , pp. 7836-7841
    • Fraser, I.D.C.1    Marston, S.B.2
  • 27
    • 0020021291 scopus 로고
    • Preparation of myosin and its subfragments from rabbit skeletal muscle
    • Margossian S.S., Lowey S. Preparation of myosin and its subfragments from rabbit skeletal muscle. Methods Enzymol. 85:1982;55-71.
    • (1982) Methods Enzymol , vol.85 , pp. 55-71
    • Margossian, S.S.1    Lowey, S.2
  • 29
    • 0020015131 scopus 로고
    • Preparation of troponin and its subunits
    • Potter J.D. Preparation of troponin and its subunits. Methods Enzymol. 85:1982;241-263.
    • (1982) Methods Enzymol , vol.85 , pp. 241-263
    • Potter, J.D.1
  • 30
    • 0034625768 scopus 로고    scopus 로고
    • Investigation of a truncated troponin T that causes familial hypertrophic cardiomyopathy: Ca2+ regulatory properties of reconstituted thin filaments depend on the ratio of mutant to wild-type peptide
    • Redwood C., Lohmann K., Bing W., Esoposito G., Elliott K., Abdulrazzak H., Knott A., Purcell I., Marston S., Watkins H. Investigation of a truncated troponin T that causes familial hypertrophic cardiomyopathy: Ca2+ regulatory properties of reconstituted thin filaments depend on the ratio of mutant to wild-type peptide. Circ Res. 86:2000;1146-1152.
    • (2000) Circ Res , vol.86 , pp. 1146-1152
    • Redwood, C.1    Lohmann, K.2    Bing, W.3    Esoposito, G.4    Elliott, K.5    Abdulrazzak, H.6    Knott, A.7    Purcell, I.8    Marston, S.9    Watkins, H.10
  • 31
    • 0028915702 scopus 로고
    • The effects of phosphorylation of cardiac troponin-I on its interactions with actin and troponin-C
    • Al-Hillawi E., Bhandari D.G., Trayer H.R., Trayer I.P. The effects of phosphorylation of cardiac troponin-I on its interactions with actin and troponin-C. Eur J Biochem. 228:1995;962-970.
    • (1995) Eur J Biochem , vol.228 , pp. 962-970
    • Al-Hillawi, E.1    Bhandari, D.G.2    Trayer, H.R.3    Trayer, I.P.4
  • 32
    • 0029118276 scopus 로고
    • In vitro motility analysis of smooth muscle caldesmon control of actin-tropomyosin filament movement
    • Fraser I.D.C., Marston S.B. In vitro motility analysis of smooth muscle caldesmon control of actin-tropomyosin filament movement. J Biol Chem. 270:1995;19688-19693.
    • (1995) J Biol Chem , vol.270 , pp. 19688-19693
    • Fraser, I.D.C.1    Marston, S.B.2
  • 33
    • 0029822489 scopus 로고    scopus 로고
    • A simple method for automatic tracking of actin filaments in the motility assay
    • Marston S.B., Fraser I.D.C., Wu B., Roper G. A simple method for automatic tracking of actin filaments in the motility assay. J Muscle Res Cell Motil. 17:1996;497-506.
    • (1996) J Muscle Res Cell Motil , vol.17 , pp. 497-506
    • Marston, S.B.1    Fraser, I.D.C.2    Wu, B.3    Roper, G.4
  • 35
    • 0030721473 scopus 로고    scopus 로고
    • Troponin I and troponin T interact with troponin C to produce different Ca2+-dependent effects on actin-tropomyosin filament motility
    • Bing W., Fraser I.D.C., Marston S.B. Troponin I and troponin T interact with troponin C to produce different Ca2+-dependent effects on actin-tropomyosin filament motility. Biochem J. 327:1997;335-340.
    • (1997) Biochem J , vol.327 , pp. 335-340
    • Bing, W.1    Fraser, I.D.C.2    Marston, S.B.3
  • 36
    • 0026498643 scopus 로고
    • Cross-bridge dynamics in human ventricular myocardium. Regulation of contractility in the failing heart [published erratum appear in Circulation 1994 Jan. 89(1): 509]
    • Hajjar R.J., Gwathmey J.K. Cross-bridge dynamics in human ventricular myocardium. Regulation of contractility in the failing heart [published erratum appear in Circulation 1994 Jan. 89(1): 509]. Circulation. 86:1992;1819-1826.
    • (1992) Circulation , vol.86 , pp. 1819-1826
    • Hajjar, R.J.1    Gwathmey, J.K.2
  • 38
    • 0034971165 scopus 로고    scopus 로고
    • Mutations that alter the surface charge of alpha-tropomyosin are associated with dilated cardiomyopathy
    • Olson T.M., Kishimoto N.Y., Whitby F.G., Michels V.V. Mutations that alter the surface charge of alpha-tropomyosin are associated with dilated cardiomyopathy. J Mol Cell Cardiol. 33:2001;723-732.
    • (2001) J Mol Cell Cardiol , vol.33 , pp. 723-732
    • Olson, T.M.1    Kishimoto, N.Y.2    Whitby, F.G.3    Michels, V.V.4
  • 40
    • 85031059453 scopus 로고    scopus 로고
    • Comparison of the functional effects of mutations in troponin T which cause dilated and hypertrophic cardiomyopathies
    • Robinson P., Butt M., Knott A., Abdulrazzak H., Marston S., Watkins H., Redwood C.S. Comparison of the functional effects of mutations in troponin T which cause dilated and hypertrophic cardiomyopathies. Biophys J. 82:2002;391a.
    • (2002) Biophys J , vol.82
    • Robinson, P.1    Butt, M.2    Knott, A.3    Abdulrazzak, H.4    Marston, S.5    Watkins, H.6    Redwood, C.S.7
  • 41
    • 0028943382 scopus 로고
    • Molecular basis of human cardiac troponin T isoforms expressed in the developing, adult, and failing heart
    • Anderson P., Greig A., Mark T., Malouf N., Oakeley A., Ungerleider R., Allen P., Kay B. Molecular basis of human cardiac troponin T isoforms expressed in the developing, adult, and failing heart. Circ Res. 76:1995;681-686.
    • (1995) Circ Res , vol.76 , pp. 681-686
    • Anderson, P.1    Greig, A.2    Mark, T.3    Malouf, N.4    Oakeley, A.5    Ungerleider, R.6    Allen, P.7    Kay, B.8
  • 42
    • 0023664228 scopus 로고
    • Isolation and functional comparison of bovine cardiac troponin T isoforms
    • Tobacman L.S., Lee R.S. Isolation and functional comparison of bovine cardiac troponin T isoforms. J Biol Chem. 262:1987;4059-4064.
    • (1987) J Biol Chem , vol.262 , pp. 4059-4064
    • Tobacman, L.S.1    Lee, R.S.2
  • 43
    • 0030992773 scopus 로고    scopus 로고
    • Slow skeletal troponin I gene transfer, expression, and myofilament incorporation enhances adult cardiac myocyte contractile function
    • Westfall M.V., Rust E.M., Metzger J.M. Slow skeletal troponin I gene transfer, expression, and myofilament incorporation enhances adult cardiac myocyte contractile function. Proc Natl Acad Sci USA. 94:1997;5444-5449.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 5444-5449
    • Westfall, M.V.1    Rust, E.M.2    Metzger, J.M.3
  • 45
    • 0035844277 scopus 로고    scopus 로고
    • A proteolytic NH2-terminal truncation of cardiac troponin I that is up-regulated in simulated microgravity
    • Yu Z.B., Zhang L.F., Jin J.P. A proteolytic NH2-terminal truncation of cardiac troponin I that is up-regulated in simulated microgravity. J Biol Chem. 276:2001;15753-15760.
    • (2001) J Biol Chem , vol.276 , pp. 15753-15760
    • Yu, Z.B.1    Zhang, L.F.2    Jin, J.P.3
  • 47
    • 0032498523 scopus 로고    scopus 로고
    • Breakdown and release of myofilament proteins during ischemia and ischemia/reperfusion in rat hearts - Identification of degradation products and effects on the pCa-force relation
    • VanEyk J., Powers F., Law W., Larue C., Hedges R., Solaro R. Breakdown and release of myofilament proteins during ischemia and ischemia/reperfusion in rat hearts - identification of degradation products and effects on the pCa-force relation. Circ Res. 82:1998;261-271.
    • (1998) Circ Res , vol.82 , pp. 261-271
    • VanEyk, J.1    Powers, F.2    Law, W.3    Larue, C.4    Hedges, R.5    Solaro, R.6
  • 49
    • 0031940516 scopus 로고    scopus 로고
    • Troponin I phosphorylation and myofilament calcium sensitivity during decompensated cardiac hypertrophy
    • McConnell B.K., Moravec C.S., Bond M. Troponin I phosphorylation and myofilament calcium sensitivity during decompensated cardiac hypertrophy. Am J Physiol. 274:1998;H385-H396.
    • (1998) Am J Physiol , vol.274
    • McConnell, B.K.1    Moravec, C.S.2    Bond, M.3
  • 51
    • 0032128254 scopus 로고    scopus 로고
    • In vitro phosphorylation of cardiac troponin I by protein kinase Cbeta2 decreases cardiomyocyte calcium responsiveness and contractility in transgenic mouse hearts
    • Takeishi Y., Chu G., Kirkpatrick D.M., Li Z., Wakasaki H., Kranias E.G., King G.L., Walsh R.A. In vitro phosphorylation of cardiac troponin I by protein kinase Cbeta2 decreases cardiomyocyte calcium responsiveness and contractility in transgenic mouse hearts. J Clin Invest. 102:1998;72-78.
    • (1998) J Clin Invest , vol.102 , pp. 72-78
    • Takeishi, Y.1    Chu, G.2    Kirkpatrick, D.M.3    Li, Z.4    Wakasaki, H.5    Kranias, E.G.6    King, G.L.7    Walsh, R.A.8
  • 52
    • 0024399052 scopus 로고
    • Identification of sites phosphorylated in bovine cardiac troponin I and troponin T by protein kinase C and comparative substrate activity of synthetic peptides containing the phosphorylation sites
    • Noland T., Raynor R., Kuo J. Identification of sites phosphorylated in bovine cardiac troponin I and troponin T by protein kinase C and comparative substrate activity of synthetic peptides containing the phosphorylation sites. J Biol Chem. 264:1989;20778-20785.
    • (1989) J Biol Chem , vol.264 , pp. 20778-20785
    • Noland, T.1    Raynor, R.2    Kuo, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.