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Volumn 141, Issue 1, 2013, Pages 133-139

Effect of muscle length on cross-bridge kinetics in intact cardiac trabeculae at body temperature

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; VENTRICULAR MYOSIN;

EID: 84872233230     PISSN: 00221295     EISSN: 15407748     Source Type: Journal    
DOI: 10.1085/jgp.201210894     Document Type: Article
Times cited : (38)

References (53)
  • 1
    • 4444343856 scopus 로고    scopus 로고
    • Cardiac length dependence of force and force redevelopment kinetics with altered cross-bridge cycling
    • Adhikari, B.B., M. Regnier, A.J. Rivera, K.L. Kreutziger, and D.A. Martyn. 2004. Cardiac length dependence of force and force redevelopment kinetics with altered cross-bridge cycling. Biophys. J. 87:1784-1794. http://dx.doi.org/10.1529/biophysj.103.039131
    • (2004) Biophys , vol.87 , pp. 1784-1794
    • Adhikari, B.B.1    Regnier, M.2    Rivera, A.J.3    Kreutziger, K.L.4    Martyn, D.A.5
  • 2
    • 52549111114 scopus 로고    scopus 로고
    • Differential contribution of cardiac sarcomeric proteins in the myofibrillar force response to stretch
    • Ait Mou, Y., J.Y. le Guennec, E. Mosca, P.P. de Tombe, and O. Cazorla. 2008. Differential contribution of cardiac sarcomeric proteins in the myofibrillar force response to stretch. Pflugers Arch. 457:25-36. http://dx.doi.org/10.1007/s00424-008-0501-x
    • (2008) Pflugers Arch. , vol.457 , pp. 25-36
    • Ait Mou, Y.1    le Guennec, J.Y.2    Mosca, E.3    de Tombe, P.P.4    Cazorla, O.5
  • 3
    • 0022393490 scopus 로고
    • The cellular basis of the lengthtension relation in cardiac muscle
    • Allen, D.G., and J.C. Kentish. 1985. The cellular basis of the lengthtension relation in cardiac muscle. J. Mol. Cell. Cardiol. 17:821-840. http://dx.doi.org/10.1016/S0022-2828(85)80097-3
    • (1985) J. Mol. Cell. Cardiol. , vol.17 , pp. 821-840
    • Allen, D.G.1    Kentish, J.C.2
  • 4
    • 33750865119 scopus 로고    scopus 로고
    • Ca2+ regulates the kinetics of tension development in intact cardiac muscle
    • Baker, A.J., V.M. Figueredo, E.C. Keung, and S.A. Camacho. 1998. Ca2+ regulates the kinetics of tension development in intact cardiac muscle. Am. J. Physiol. 275:H744-H750.
    • (1998) Am. J. Physiol. , vol.275
    • Baker, A.J.1    Figueredo, V.M.2    Keung, E.C.3    Camacho, S.A.4
  • 5
    • 0028656403 scopus 로고
    • Myofibrillar ATPase activity during isometric contraction and isomyosin composition in rat single skinned muscle fibres
    • Bottinelli, R., M. Canepari, C. Reggiani, and G.J. Stienen. 1994. Myofibrillar ATPase activity during isometric contraction and isomyosin composition in rat single skinned muscle fibres. J. Physiol. 481:663-675.
    • (1994) J. Physiol. , vol.481 , pp. 663-675
    • Bottinelli, R.1    Canepari, M.2    Reggiani, C.3    Stienen, G.J.4
  • 6
    • 2042451727 scopus 로고
    • Rate of force generation in muscle: correlation with actomyosin ATPase activity in solution
    • U.S.A.
    • Brenner, B., and E. Eisenberg. 1986. Rate of force generation in muscle: correlation with actomyosin ATPase activity in solution. Proc. Natl. Acad. Sci. USA. 83:3542-3546. http://dx.doi.org/10.1073/pnas.83.10.3542
    • (1986) Proc. Natl. Acad. Sci. , vol.83 , pp. 3542-3546
    • Brenner, B.1    Eisenberg, E.2
  • 7
    • 0038650580 scopus 로고    scopus 로고
    • Reduced length-dependent cross-bridge recruitment in skinned fiber preparations of human failing myocardium
    • Brixius, K., P. Savidou-Zaroti, W. Bloch, and R.H. Schwinger. 2003. Reduced length-dependent cross-bridge recruitment in skinned fiber preparations of human failing myocardium. Eur. J. Appl. Physiol. 89:249-256. http://dx.doi.org/10.1007/s00421-002-0782-2
    • (2003) Eur. J. Appl. Physiol. , vol.89 , pp. 249-256
    • Brixius, K.1    Savidou-Zaroti, P.2    Bloch, W.3    Schwinger, R.H.4
  • 8
    • 64049083187 scopus 로고    scopus 로고
    • Temporal changes in expression of connexin 43 after load-induced hypertrophy in vitro
    • Bupha-Intr, T., K.M. Haizlip, and P.M. Janssen. 2009. Temporal changes in expression of connexin 43 after load-induced hypertrophy in vitro. Am. J. Physiol. Heart Circ. Physiol. 296:H806-H814. http://dx.doi.org/10.1152/ajpheart.01058.2008
    • (2009) Am. J. Physiol. Heart Circ. Physiol. , vol.296
    • Bupha-Intr, T.1    Haizlip, K.M.2    Janssen, P.M.3
  • 9
    • 33845357154 scopus 로고    scopus 로고
    • Filament compliance effects can explain tension overshoots during force development
    • Campbell, K.S. 2006. Filament compliance effects can explain tension overshoots during force development. Biophys. J. 91:4102-4109. http://dx.doi.org/10.1529/biophysj.106.087312
    • (2006) Biophys. J. , vol.91 , pp. 4102-4109
    • Campbell, K.S.1
  • 10
    • 34147122743 scopus 로고    scopus 로고
    • The rate of tension recovery in cardiac muscle correlates with the relative residual tension prevailing after restretch
    • Campbell, K.S., and A.M. Holbrook. 2007. The rate of tension recovery in cardiac muscle correlates with the relative residual tension prevailing after restretch. Am. J. Physiol. Heart Circ. Physiol. 292:H2020-H2022. http://dx.doi.org/10.1152/ajpheart.00714.2006
    • (2007) Am. J. Physiol. Heart Circ. Physiol. , vol.292
    • Campbell, K.S.1    Holbrook, A.M.2
  • 11
    • 0038440669 scopus 로고    scopus 로고
    • Cycling crossbridges increase myocardial stiffness at submaximal levels of Ca2+ activation
    • Campbell, K.S., J.R. Patel, and R.L. Moss. 2003. Cycling crossbridges increase myocardial stiffness at submaximal levels of Ca2+ activation. Biophys. J. 84:3807-3815. http://dx.doi.org/10.1016/S0006-3495(03)75108-X
    • (2003) Biophys. J. , vol.84 , pp. 3807-3815
    • Campbell, K.S.1    Patel, J.R.2    Moss, R.L.3
  • 12
    • 35148840164 scopus 로고    scopus 로고
    • Interaction between myosin heavy chain and troponin isoforms modulate cardiac myofiber contractile dynamics
    • Chandra, M., M.L. Tschirgi, S.J. Ford, B.K. Slinker, and K.B. Campbell. 2007. Interaction between myosin heavy chain and troponin isoforms modulate cardiac myofiber contractile dynamics. Am. J. Physiol. Regul. Integr. Comp. Physiol. 293:R1595-R1607. http://dx.doi.org/10.1152/ajpregu.00157.2007
    • (2007) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.293
    • Chandra, M.1    Tschirgi, M.L.2    Ford, S.J.3    Slinker, B.K.4    Campbell, K.B.5
  • 13
    • 33645456962 scopus 로고    scopus 로고
    • Decline of contractility during ischemia-reperfusion injury: actin glutathionylation and its effect on allosteric interaction with tropomyosin
    • Chen, F.C., and O. Ogut. 2006. Decline of contractility during ischemia-reperfusion injury: actin glutathionylation and its effect on allosteric interaction with tropomyosin. Am. J. Physiol. Cell Physiol. 290:C719-C727. http://dx.doi.org/10.1152/ajpcell.00419.2005
    • (2006) Am. J. Physiol. Cell Physiol. , vol.290
    • Chen, F.C.1    Ogut, O.2
  • 14
    • 0037403175 scopus 로고    scopus 로고
    • Cardiac myofilaments: Mechanics and regulation
    • de Tombe, P.P. 2003. Cardiac myofilaments: mechanics and regulation. J. Biomech. 36:721-730. http://dx.doi.org/10.1016/S0021-9290(02)00450-5
    • (2003) J. Biomech. , vol.36 , pp. 721-730
    • de Tombe, P.P.1
  • 15
    • 35348863108 scopus 로고    scopus 로고
    • Impact of temperature on cross-bridge cycling kinetics in rat myocardium
    • de Tombe, P.P., and G.J. Stienen. 2007. Impact of temperature on cross-bridge cycling kinetics in rat myocardium. J. Physiol. 584:591-600. http://dx.doi.org/10.1113/jphysiol.2007.138693
    • (2007) J. Physiol. , vol.584 , pp. 591-600
    • de Tombe, P.P.1    Stienen, G.J.2
  • 17
    • 0035862210 scopus 로고    scopus 로고
    • Cross-bridge interaction kinetics in rat myocardium are accelerated by strong binding of myosin to the thin filament
    • Fitzsimons, D.P., J.R. Patel, and R.L. Moss. 2001. Cross-bridge interaction kinetics in rat myocardium are accelerated by strong binding of myosin to the thin filament. J. Physiol. 530:263-272. http://dx.doi.org/10.1111/j.1469-7793.2001.0263l.x
    • (2001) J. Physiol. , vol.530 , pp. 263-272
    • Fitzsimons, D.P.1    Patel, J.R.2    Moss, R.L.3
  • 18
    • 0028388717 scopus 로고
    • Myofilament Ca2+ sensitivity in intact versus skinned rat ventricular muscle
    • Gao, W.D., P.H. Backx, M. Azan-Backx, and E. Marban. 1994. Myofilament Ca2+ sensitivity in intact versus skinned rat ventricular muscle. Circ. Res. 74:408-415. http://dx.doi.org/10.1161/01.RES.74.3.408
    • (1994) Circ. Res. , vol.74 , pp. 408-415
    • Gao, W.D.1    Backx, P.H.2    Azan-Backx, M.3    Marban, E.4
  • 19
    • 0027337513 scopus 로고
    • Ca2+ and segment length dependence of isometric force kinetics in intact ferret cardiac muscle
    • Hancock, W.O., D.A. Martyn, and L.L. Huntsman. 1993. Ca2+ and segment length dependence of isometric force kinetics in intact ferret cardiac muscle. Circ. Res. 73:603-611. http://dx.doi.org/10.1161/01.RES.73.4.603
    • (1993) Circ. Res. , vol.73 , pp. 603-611
    • Hancock, W.O.1    Martyn, D.A.2    Huntsman, L.L.3
  • 20
    • 0029665139 scopus 로고    scopus 로고
    • Influence of Ca2+ on force redevelopment kinetics in skinned rat myocardium
    • Hancock, W.O., D.A. Martyn, L.L. Huntsman, and A.M. Gordon. 1996. Influence of Ca2+ on force redevelopment kinetics in skinned rat myocardium. Biophys. J. 70:2819-2829. http://dx.doi.org/10.1016/S0006-3495(96)79851-X
    • (1996) Biophys. J. , vol.70 , pp. 2819-2829
    • Hancock, W.O.1    Martyn, D.A.2    Huntsman, L.L.3    Gordon, A.M.4
  • 21
    • 39749193968 scopus 로고    scopus 로고
    • Cardiac function and modulation of sarcomeric function by length
    • Hanft, L.M., F.S. Korte, and K.S. McDonald. 2008. Cardiac function and modulation of sarcomeric function by length. Cardiovasc. Res. 77:627-636. http://dx.doi.org/10.1093/cvr/cvm099
    • (2008) Cardiovasc. Res. , vol.77 , pp. 627-636
    • Hanft, L.M.1    Korte, F.S.2    McDonald, K.S.3
  • 22
    • 0035001869 scopus 로고    scopus 로고
    • Effects of isoflurane on intracellular calcium and myocardial crossbridge kinetics in tetanized papillary muscles
    • Hannon, J.D., M.J. Cody, and P.R. Housmans. 2001. Effects of isoflurane on intracellular calcium and myocardial crossbridge kinetics in tetanized papillary muscles. Anesthesiology. 94:856-861. http://dx.doi.org/10.1097/00000542-200105000-00025
    • (2001) Anesthesiology , vol.94 , pp. 856-861
    • Hannon, J.D.1    Cody, M.J.2    Housmans, P.R.3
  • 23
    • 0034828977 scopus 로고    scopus 로고
    • Loaded shortening and power output in cardiac myocytes are dependent on myosin heavy chain isoform expression
    • Herron, T.J., F.S. Korte, and K.S. McDonald. 2001. Loaded shortening and power output in cardiac myocytes are dependent on myosin heavy chain isoform expression. Am. J. Physiol. Heart Circ. Physiol. 281:H1217-H1222.
    • (2001) Am. J. Physiol. Heart Circ. Physiol. , vol.281
    • Herron, T.J.1    Korte, F.S.2    McDonald, K.S.3
  • 24
    • 70349668973 scopus 로고    scopus 로고
    • PKC phosphorylation of titin's PEVK element: A novel and conserved pathway for modulating myocardial stiffness
    • Hidalgo, C., B. Hudson, J. Bogomolovas, Y. Zhu, B. Anderson, M. Greaser, S. Labeit, and H. Granzier. 2009. PKC phosphorylation of titin's PEVK element: a novel and conserved pathway for modulating myocardial stiffness. Circ. Res. 105:631-638. http://dx.doi.org/10.1161/CIRCRESAHA.109.198465
    • (2009) Circ. Res. , vol.105 , pp. 631-638
    • Hidalgo, C.1    Hudson, B.2    Bogomolovas, J.3    Zhu, Y.4    Anderson, B.5    Greaser, M.6    Labeit, S.7    Granzier, H.8
  • 25
    • 0020657907 scopus 로고
    • Force generation in experimental tetanus, KCl contracture, and oxygen and glucose deficiency contracture in mammalian myocardium
    • Holubarsch, C. 1983. Force generation in experimental tetanus, KCl contracture, and oxygen and glucose deficiency contracture in mammalian myocardium. Pflugers Arch. 396:277-284. http://dx.doi.org/10.1007/BF01063931
    • (1983) Pflugers Arch. , vol.396 , pp. 277-284
    • Holubarsch, C.1
  • 26
    • 78649742900 scopus 로고    scopus 로고
    • 54th Bowditch Lecture: Myocardial contractionrelaxation coupling
    • Janssen, P.M.L. 2010a. 54th Bowditch Lecture: Myocardial contractionrelaxation coupling. Am. J. Physiol. Heart Circ. Physiol. 299:H1741-H1749. http://dx.doi.org/10.1152/ajpheart.00759.2010
    • (2010) Am. J. Physiol. Heart Circ. Physiol. , vol.299
    • Janssen, P.M.L.1
  • 27
    • 77958063805 scopus 로고    scopus 로고
    • Kinetics of cardiac muscle contraction and relaxation are linked and determined by properties of the cardiac sarcomere
    • Janssen, P.M.L. 2010b. Kinetics of cardiac muscle contraction and relaxation are linked and determined by properties of the cardiac sarcomere. Am. J. Physiol. Heart Circ. Physiol. 299:H1092-H1099. http://dx.doi.org/10.1152/ajpheart.00417.2010
    • (2010) Am. J. Physiol. Heart Circ. Physiol. , vol.299
    • Janssen, P.M.L.1
  • 28
    • 0036088280 scopus 로고    scopus 로고
    • Myofilament properties comprise the rate-limiting step for cardiac relaxation at body temperature in the rat
    • Janssen, P.M.L., L.B. Stull, and E. Marbán. 2002. Myofilament properties comprise the rate-limiting step for cardiac relaxation at body temperature in the rat. Am. J. Physiol. Heart Circ. Physiol. 282:H499-H507.
    • (2002) Am. J. Physiol. Heart Circ. Physiol. , vol.282
    • Janssen, P.M.L.1    Stull, L.B.2    Marbán, E.3
  • 29
    • 76649119460 scopus 로고    scopus 로고
    • Nonlinear least-squares data fitting in Excel spreadsheets
    • Kemmer, G., and S. Keller. 2010. Nonlinear least-squares data fitting in Excel spreadsheets. Nat. Protoc. 5:267-281. http://dx.doi.org/10.1038/nprot.2009.182
    • (2010) Nat. Protoc. , vol.5 , pp. 267-281
    • Kemmer, G.1    Keller, S.2
  • 30
    • 34249715111 scopus 로고    scopus 로고
    • Sarcomere length dependence of rat skinned cardiac myocyte mechanical properties: dependence on myosin heavy chain
    • Korte, F.S., and K.S. McDonald. 2007. Sarcomere length dependence of rat skinned cardiac myocyte mechanical properties: dependence on myosin heavy chain. J. Physiol. 581:725-739. http://dx.doi.org/10.1113/jphysiol.2007.128199
    • (2007) J. Physiol. , vol.581 , pp. 725-739
    • Korte, F.S.1    McDonald, K.S.2
  • 31
    • 0020477578 scopus 로고
    • Phosphorylation of troponin I and phospholamban during catecholamine stimulation of rabbit heart
    • Kranias, E.G., and R.J. Solaro. 1982. Phosphorylation of troponin I and phospholamban during catecholamine stimulation of rabbit heart. Nature. 298:182-184. http://dx.doi.org/10.1038/298182a0
    • (1982) Nature , vol.298 , pp. 182-184
    • Kranias, E.G.1    Solaro, R.J.2
  • 33
    • 14844344027 scopus 로고    scopus 로고
    • Regulation of cardiac contractile function by troponin I phosphorylation
    • Layland, J., R.J. Solaro, and A.M. Shah. 2005. Regulation of cardiac contractile function by troponin I phosphorylation. Cardiovasc. Res. 66:12-21. http://dx.doi.org/10.1016/j.cardiores.2004.12.022
    • (2005) Cardiovasc. Res. , vol.66 , pp. 12-21
    • Layland, J.1    Solaro, R.J.2    Shah, A.M.3
  • 34
    • 84865040769 scopus 로고    scopus 로고
    • The rates of Ca2+ dissociation and cross-bridge detachment from ventricular myofibrils as reported by a fluorescent cardiac troponin C
    • Little, S.C., B.J. Biesiadecki, A. Kilic, R.S. Higgins, P.M. Janssen, and J.P. Davis. 2012. The rates of Ca2+ dissociation and cross-bridge detachment from ventricular myofibrils as reported by a fluorescent cardiac troponin C. J. Biol. Chem. 287:27930-27940. http://dx.doi.org/10.1074/jbc.M111.337295
    • (2012) J. Biol. Chem. , vol.287 , pp. 27930-27940
    • Little, S.C.1    Biesiadecki, B.J.2    Kilic, A.3    Higgins, R.S.4    Janssen, P.M.5    Davis, J.P.6
  • 35
    • 55649083104 scopus 로고    scopus 로고
    • Troponin phosphorylation and myofilament Ca2+-sensitivity in heart failure: increased or decreased
    • Marston, S.B., and P.P. de Tombe. 2008. Troponin phosphorylation and myofilament Ca2+-sensitivity in heart failure: increased or decreased? J. Mol. Cell. Cardiol. 45:603-607. http://dx.doi.org/10.1016/j.yjmcc.2008.07.004
    • (2008) J. Mol. Cell. Cardiol. , vol.45 , pp. 603-607
    • Marston, S.B.1    de Tombe, P.P.2
  • 36
    • 0036924212 scopus 로고    scopus 로고
    • A simple model with myofilament compliance predicts activation-dependent crossbridge kinetics in skinned skeletal fibers
    • Martyn, D.A., P.B. Chase, M. Regnier, and A.M. Gordon. 2002. A simple model with myofilament compliance predicts activation-dependent crossbridge kinetics in skinned skeletal fibers. Biophys. J. 83:3425-3434. http://dx.doi.org/10.1016/S0006-3495(02)75342-3
    • (2002) Biophys. J. , vol.83 , pp. 3425-3434
    • Martyn, D.A.1    Chase, P.B.2    Regnier, M.3    Gordon, A.M.4
  • 37
    • 79958865867 scopus 로고    scopus 로고
    • The interdependence of Ca2+ activation, sarcomere length, and power output in the heart
    • McDonald, K.S. 2011. The interdependence of Ca2+ activation, sarcomere length, and power output in the heart. Pflugers Arch. 462:61-67. http://dx.doi.org/10.1007/s00424-011-0949-y
    • (2011) Pflugers Arch. , vol.462 , pp. 61-67
    • McDonald, K.S.1
  • 38
    • 42049093454 scopus 로고    scopus 로고
    • Dissociation of force decline from calcium decline by preload in isolated rabbit myocardium
    • Monasky, M.M., K.D. Varian, J.P. Davis, and P.M.L. Janssen. 2008. Dissociation of force decline from calcium decline by preload in isolated rabbit myocardium. Pflugers Arch. 456:267-276. http:// dx.doi.org/10.1007/s00424-007-0394-0
    • (2008) Pflugers Arch. , vol.456 , pp. 267-276
    • Monasky, M.M.1    Varian, K.D.2    Davis, J.P.3    Janssen, P.M.L.4
  • 39
    • 77951622329 scopus 로고    scopus 로고
    • Increased phosphorylation of tropomyosin, troponin I, and myosin light chain-2 after stretch in rabbit ventricular myocardium under physiological conditions
    • Monasky, M.M., B.J. Biesiadecki, and P.M. Janssen. 2010. Increased phosphorylation of tropomyosin, troponin I, and myosin light chain-2 after stretch in rabbit ventricular myocardium under physiological conditions. J. Mol. Cell. Cardiol. 48:1023-1028. http://dx.doi.org/10.1016/j.yjmcc.2010.03.004
    • (2010) J. Mol. Cell. Cardiol. , vol.48 , pp. 1023-1028
    • Monasky, M.M.1    Biesiadecki, B.J.2    Janssen, P.M.3
  • 40
    • 0024422888 scopus 로고
    • Protection of human left ventricular myocardium from cutting injury with 2,3-butanedione monoxime
    • Mulieri, L.A., G. Hasenfuss, F. Ittleman, E.M. Blanchard, and N.R. Alpert. 1989. Protection of human left ventricular myocardium from cutting injury with 2,3-butanedione monoxime. Circ. Res. 65:1441-1449. http://dx.doi.org/10.1161/01.RES.65.5.1441
    • (1989) Circ. Res. , vol.65 , pp. 1441-1449
    • Mulieri, L.A.1    Hasenfuss, G.2    Ittleman, F.3    Blanchard, E.M.4    Alpert, N.R.5
  • 41
    • 29944433957 scopus 로고    scopus 로고
    • Effect of muscle dimensions on trabecular contractile performance under physiological conditions
    • Raman, S., M.A. Kelley, and P.M.L. Janssen. 2006. Effect of muscle dimensions on trabecular contractile performance under physiological conditions. Pflugers Arch. 451:625-630. http://dx.doi.org/10.1007/s00424-005-1500-9
    • (2006) Pflugers Arch. , vol.451 , pp. 625-630
    • Raman, S.1    Kelley, M.A.2    Janssen, P.M.L.3
  • 42
    • 0026665940 scopus 로고
    • A method to reconstruct myocardial sarcomere lengths and orientations at transmural sites in beating canine hearts
    • Rodriguez, E.K., W.C. Hunter, M.J. Royce, M.K. Leppo, A.S. Douglas, and H.F. Weisman. 1992. A method to reconstruct myocardial sarcomere lengths and orientations at transmural sites in beating canine hearts. Am. J. Physiol. 263:H293-H306.
    • (1992) Am. J. Physiol. , vol.263
    • Rodriguez, E.K.1    Hunter, W.C.2    Royce, M.J.3    Leppo, M.K.4    Douglas, A.S.5    Weisman, H.F.6
  • 44
    • 84861765888 scopus 로고    scopus 로고
    • Contractile parameters and occurrence of alternans in isolated rat myocardium at supra-physiological stimulation frequency
    • Slabaugh, J.L., L. Brunello, S. Gyorke, and P.M. Janssen. 2012. Contractile parameters and occurrence of alternans in isolated rat myocardium at supra-physiological stimulation frequency. Am. J. Physiol. Heart Circ. Physiol. 302:H2267-H2275. http://dx.doi.org/10.1152/ajpheart.01004.2011
    • (2012) Am. J. Physiol. Heart Circ. Physiol. , vol.302
    • Slabaugh, J.L.1    Brunello, L.2    Gyorke, S.3    Janssen, P.M.4
  • 45
    • 33749003228 scopus 로고    scopus 로고
    • Contributions of stretch activation to length-dependent contraction in murine myocardium
    • Stelzer, J.E., and R.L. Moss. 2006. Contributions of stretch activation to length-dependent contraction in murine myocardium. J. Gen. Physiol. 128:461-471. http://dx.doi.org/10.1085/jgp.200609634
    • (2006) J. Gen. Physiol. , vol.128 , pp. 461-471
    • Stelzer, J.E.1    Moss, R.L.2
  • 46
    • 4444368240 scopus 로고    scopus 로고
    • Roles of phosphorylation of myosin binding protein-C and troponin I in mouse cardiac muscle twitch dynamics
    • Tong, C.W., R.D. Gaffin, D.C. Zawieja, and M. Muthuchamy. 2004. Roles of phosphorylation of myosin binding protein-C and troponin I in mouse cardiac muscle twitch dynamics. J. Physiol. 558:927-941. http://dx.doi.org/10.1113/jphysiol.2004.062539
    • (2004) J. Physiol. , vol.558 , pp. 927-941
    • Tong, C.W.1    Gaffin, R.D.2    Zawieja, D.C.3    Muthuchamy, M.4
  • 47
    • 34250809531 scopus 로고    scopus 로고
    • Frequency-dependent acceleration of relaxation involves decreased myofilament calcium sensitivity
    • Varian, K.D., and P.M.L. Janssen. 2007. Frequency-dependent acceleration of relaxation involves decreased myofilament calcium sensitivity. Am. J. Physiol. Heart Circ. Physiol. 292:H2212-H2219. http://dx.doi.org/10.1152/ajpheart.00778.2006
    • (2007) Am. J. Physiol. Heart Circ. Physiol. , vol.292
    • Varian, K.D.1    Janssen, P.M.L.2
  • 48
    • 33646417619 scopus 로고    scopus 로고
    • Measurement of myofilament calcium sensitivity at physiological temperature in intact cardiac trabeculae
    • Varian, K.D., S. Raman, and P.M.L. Janssen. 2006. Measurement of myofilament calcium sensitivity at physiological temperature in intact cardiac trabeculae. Am. J. Physiol. Heart Circ. Physiol. 290:H2092-H2097. http://dx.doi.org/10.1152/ajpheart.01241.2005
    • (2006) Am. J. Physiol. Heart Circ. Physiol. , vol.290
    • Varian, K.D.1    Raman, S.2    Janssen, P.M.L.3
  • 51
    • 0028919177 scopus 로고
    • Rate of tension development in cardiac muscle varies with level of activator calcium
    • Wolff, M.R., K.S. McDonald, and R.L. Moss. 1995. Rate of tension development in cardiac muscle varies with level of activator calcium. Circ. Res. 76:154-160. http://dx.doi.org/10.1161/01.RES.76.1.154
    • (1995) Circ. Res. , vol.76 , pp. 154-160
    • Wolff, M.R.1    McDonald, K.S.2    Moss, R.L.3
  • 52
    • 79851497074 scopus 로고    scopus 로고
    • Lengthening-contractions in isolated myocardium impact force development and worsen cardiac contractile function in the mdx mouse model of muscular dystrophy
    • Xu, Y., D.A. Delfín, J.A. Rafael-Fortney, and P.M.L. Janssen. 2011a. Lengthening-contractions in isolated myocardium impact force development and worsen cardiac contractile function in the mdx mouse model of muscular dystrophy. J. Appl. Physiol. 110:512-519. http://dx.doi.org/10.1152/japplphysiol.00253.2010
    • (2011) J. Appl. Physiol. , vol.110 , pp. 512-519
    • Xu, Y.1    Delfín, D.A.2    Rafael-Fortney, J.A.3    Janssen, P.M.L.4
  • 53
    • 80054702316 scopus 로고    scopus 로고
    • Effect of twitch interval dura tion on the contractile function of subsequent twitches in isolated rat, rabbit, and dog myocardium under physiological conditions
    • Xu, Y., M.M. Monasky, N. Hiranandani, K.M. Haizlip, G.E. Billman, and P.M. Janssen. 2011b. Effect of twitch interval dura tion on the contractile function of subsequent twitches in isolated rat, rabbit, and dog myocardium under physiological conditions. J. Appl. Physiol. 111:1159-1167. http://dx.doi.org/10.1152/japplphysiol.01170.2010
    • (2011) J. Appl. Physiol. , vol.111 , pp. 1159-1167
    • Xu, Y.1    Monasky, M.M.2    Hiranandani, N.3    Haizlip, K.M.4    Billman, G.E.5    Janssen, P.M.6


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