메뉴 건너뛰기




Volumn 20, Issue 5-6, 1999, Pages 443-456

Measured and modeled properties of mammalian skeletal muscle. I. The effects of post-activation potentiation on the time course and velocity dependencies of force production

Author keywords

[No Author keywords available]

Indexed keywords

MYOSIN LIGHT CHAIN;

EID: 0032831309     PISSN: 01424319     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1005590901220     Document Type: Article
Times cited : (49)

References (56)
  • 1
    • 0029949353 scopus 로고    scopus 로고
    • The effect of muscle length on intracellular calcium and force in single fibres from mouse skeletal muscle
    • Balnave CD and Allen DG (1996) The effect of muscle length on intracellular calcium and force in single fibres from mouse skeletal muscle. J Physiol 492: 705-713.
    • (1996) J Physiol , vol.492 , pp. 705-713
    • Balnave, C.D.1    Allen, D.G.2
  • 2
    • 0022538450 scopus 로고
    • Gradation of isometric tension by different activation rates in motor units of cat flexor carpi radialis muscle
    • Botterman BR, Iwamoto GA and Gonyea WJ (1986) Gradation of isometric tension by different activation rates in motor units of cat flexor carpi radialis muscle. J Neurophysiol 56: 494-506.
    • (1986) J Neurophysiol , vol.56 , pp. 494-506
    • Botterman, B.R.1    Iwamoto, G.A.2    Gonyea, W.J.3
  • 3
    • 0343919977 scopus 로고
    • Crossbridge attachment during isotonic shortening in single skinned rabbit psoas fibers
    • abstract
    • Brenner B (1983) Crossbridge attachment during isotonic shortening in single skinned rabbit psoas fibers. Biophys J 41: 33a (abstract).
    • (1983) Biophys J , vol.41
    • Brenner, B.1
  • 4
    • 0024007477 scopus 로고
    • 2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: Implications for regulation of muscle contraction
    • 2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: implications for regulation of muscle contraction. Proc Natl Acad Sci USA 85: 3265-3269.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 3265-3269
    • Brenner, B.1
  • 5
    • 0031596236 scopus 로고    scopus 로고
    • Feline caudofemoralis muscle. Muscle fiber properties, architecture, and motor innervation
    • Brown IE, Satoda T, Richmond FJR and Loeb GE (1998) Feline caudofemoralis muscle. Muscle fiber properties, architecture, and motor innervation. Exp Brain Res 121: 76-91.
    • (1998) Exp Brain Res , vol.121 , pp. 76-91
    • Brown, I.E.1    Satoda, T.2    Richmond, F.J.R.3    Loeb, G.E.4
  • 6
    • 0003293696 scopus 로고
    • A damaged state in cat caudofemoralis muscle induced by high forces
    • abstract
    • Brown IE and Loeb GE (1995) A damaged state in cat caudofemoralis muscle induced by high forces. Can J Physiol Pharmacol 73: Ai (abstract).
    • (1995) Can J Physiol Pharmacol , vol.73
    • Brown, I.E.1    Loeb, G.E.2
  • 7
    • 0000328923 scopus 로고    scopus 로고
    • The physiological relevance of potentiation in mammalian fast-twitch skeletal muscle
    • abstract
    • Brown IE and Loeb GE (1997) The physiological relevance of potentiation in mammalian fast-twitch skeletal muscle. Soc Neurosci Abstr 23: 1049 (abstract).
    • (1997) Soc Neurosci Abstr , vol.23 , pp. 1049
    • Brown, I.E.1    Loeb, G.E.2
  • 8
    • 17744413294 scopus 로고    scopus 로고
    • Post-activation potentiation: A clue for simplifying models of muscle dynamics
    • Brown IE and Loeb GE (1998) Post-activation potentiation: a clue for simplifying models of muscle dynamics. Am Zool 38: 743-754.
    • (1998) Am Zool , vol.38 , pp. 743-754
    • Brown, I.E.1    Loeb, G.E.2
  • 9
    • 0001770945 scopus 로고    scopus 로고
    • A reductionist approach to creating and using neuromusculoskeletal models
    • Winters JM and Crago PE (eds.) Springer-Verlag, New York
    • Brown IE and Loeb GE (1999) A reductionist approach to creating and using neuromusculoskeletal models. In: Winters JM and Crago PE (eds.) Biomechanics and Neural Control of Movement. Springer-Verlag, New York.
    • (1999) Biomechanics and Neural Control of Movement
    • Brown, I.E.1    Loeb, G.E.2
  • 10
    • 0017073564 scopus 로고
    • The effect of activation history on tension production by individual muscle units
    • Burke RE, Rudomin P and Zajac FEI (1976) The effect of activation history on tension production by individual muscle units. Brain Res 109: 515-529.
    • (1976) Brain Res , vol.109 , pp. 515-529
    • Burke, R.E.1    Rudomin, P.2    Zajac, F.E.I.3
  • 11
    • 0013915014 scopus 로고
    • Contraction kinetics of striated muscle fibres following quick changes in load
    • Civan MM and Podolsky RJ (1966) Contraction kinetics of striated muscle fibres following quick changes in load. J Physiol 184: 511-534.
    • (1966) J Physiol , vol.184 , pp. 511-534
    • Civan, M.M.1    Podolsky, R.J.2
  • 12
    • 0014307445 scopus 로고
    • The after-effects of repetitive stimulation on the isometric twitch contraction of rat fast skeletal muscle
    • Close R and Hoh JFY (1968) The after-effects of repetitive stimulation on the isometric twitch contraction of rat fast skeletal muscle. J Physiol 197: 461-477.
    • (1968) J Physiol , vol.197 , pp. 461-477
    • Close, R.1    Hoh, J.F.Y.2
  • 13
    • 0015290308 scopus 로고
    • The relations between sarcomere length and characteristics of isometric twitch contractions of frog sartorius muscle
    • Close RI (1972) The relations between sarcomere length and characteristics of isometric twitch contractions of frog sartorius muscle. J Physiol 220: 745-762.
    • (1972) J Physiol , vol.220 , pp. 745-762
    • Close, R.I.1
  • 14
    • 85025365054 scopus 로고
    • An x-ray and light-diffraction study of the filament lattice of striated muscle in the living state and in rigor
    • Elliott GF, Lowy J and Worthington CR (1963) An x-ray and light-diffraction study of the filament lattice of striated muscle in the living state and in rigor. J Mol Biol 6: 295-306.
    • (1963) J Mol Biol , vol.6 , pp. 295-306
    • Elliott, G.F.1    Lowy, J.2    Worthington, C.R.3
  • 15
    • 0029986039 scopus 로고    scopus 로고
    • Calcium uptake and release modulated by counter-ion conductances in the sarcoplasmic reticulum of skeletal muscle
    • Fink RH and Veigel C (1996) Calcium uptake and release modulated by counter-ion conductances in the sarcoplasmic reticulum of skeletal muscle. [Review] Acta Physiol Scand 156: 387-396.
    • (1996) Acta Physiol Scand , vol.156 , pp. 387-396
    • Fink, R.H.1    Veigel, C.2
  • 16
    • 0019820645 scopus 로고
    • Influence of osmotic compression on calcium activation and tension in skinned muscle fibers of the rabbit
    • Godt RE and Maughan DW (1981) Influence of osmotic compression on calcium activation and tension in skinned muscle fibers of the rabbit. Pflügers Arch 391: 334-337.
    • (1981) Pflügers Arch , vol.391 , pp. 334-337
    • Godt, R.E.1    Maughan, D.W.2
  • 17
    • 0002952484 scopus 로고
    • Cross-bridges in rigor fibres of rabbit psoas muscle support negative forces
    • abstract
    • Goldman YE, McCray JA and Vallette DP (1988) Cross-bridges in rigor fibres of rabbit psoas muscle support negative forces. J Physiol 398: 72P (abstract).
    • (1988) J Physiol , vol.398
    • Goldman, Y.E.1    McCray, J.A.2    Vallette, D.P.3
  • 18
    • 0013905011 scopus 로고
    • The variation in isometric tension with sarcomere length in vertebral muscle fibres
    • Gordon AM, Huxley AF and Julian FJ (1966) The variation in isometric tension with sarcomere length in vertebral muscle fibres. J Physiol 184: 170-192.
    • (1966) J Physiol , vol.184 , pp. 170-192
    • Gordon, A.M.1    Huxley, A.F.2    Julian, F.J.3
  • 19
    • 0029131790 scopus 로고
    • Myosin phosphorylation augments force-displacement and force-velocity relationships of mouse fast muscle
    • Grange RW, Cory CR, Vandenboom R and Houston ME (1995) Myosin phosphorylation augments force-displacement and force-velocity relationships of mouse fast muscle. Am J Physiol 269: C713-C724.
    • (1995) Am J Physiol , vol.269
    • Grange, R.W.1    Cory, C.R.2    Vandenboom, R.3    Houston, M.E.4
  • 20
    • 0009741419 scopus 로고
    • The nature of the isometric twitch
    • Hartree W and Hill AV (1921) The nature of the isometric twitch. J Physiol 55: 389-411.
    • (1921) J Physiol , vol.55 , pp. 389-411
    • Hartree, W.1    Hill, A.V.2
  • 22
    • 0029095005 scopus 로고
    • Sliding distance per ATP molecule hydrolyzed by myosin heads during isotonic shortening of skinned muscle fibers
    • Higuchi H and Goldman YE (1995) Sliding distance per ATP molecule hydrolyzed by myosin heads during isotonic shortening of skinned muscle fibers. Biophys J 69: 1491-1507.
    • (1995) Biophys J , vol.69 , pp. 1491-1507
    • Higuchi, H.1    Goldman, Y.E.2
  • 23
    • 0016180488 scopus 로고
    • Theoretical formalism for the sliding filament model of contraction of striated muscle. Part I
    • Hill TL (1974) Theoretical formalism for the sliding filament model of contraction of striated muscle. Part I [Review]. Prog Biophys Mol Biol 28: 267-340.
    • (1974) Prog Biophys Mol Biol , vol.28 , pp. 267-340
    • Hill, T.L.1
  • 24
    • 0025314137 scopus 로고
    • Myosin phosphorylation, twitch potentiation, and fatigue in human skeletal muscle
    • Houston ME and Grange RW (1990) Myosin phosphorylation, twitch potentiation, and fatigue in human skeletal muscle. Can J Physiol Pharmacol 68: 908-913.
    • (1990) Can J Physiol Pharmacol , vol.68 , pp. 908-913
    • Houston, M.E.1    Grange, R.W.2
  • 25
    • 33847013578 scopus 로고
    • Muscle structure and theories of contraction
    • Huxley AF (1957) Muscle structure and theories of contraction. Prog Biophys Mol Biol 7: 255-318.
    • (1957) Prog Biophys Mol Biol , vol.7 , pp. 255-318
    • Huxley, A.F.1
  • 27
    • 77049131135 scopus 로고
    • X-ray analysis and the problem of muscle
    • Huxley HE (1953) X-ray analysis and the problem of muscle. Proc R Soc Lond (Biol) 141: 59-62.
    • (1953) Proc R Soc Lond (Biol) , vol.141 , pp. 59-62
    • Huxley, H.E.1
  • 28
    • 0018701747 scopus 로고
    • The effect on tension of non-uniform distribution of length changes applied to frog muscle fibres
    • Julian FJ and Morgan DL (1979) The effect on tension of non-uniform distribution of length changes applied to frog muscle fibres. J Physiol 293: 379-392.
    • (1979) J Physiol , vol.293 , pp. 379-392
    • Julian, F.J.1    Morgan, D.L.2
  • 29
    • 0016815857 scopus 로고
    • Variation of muscle stiffness with force at increasing speeds of shortening
    • Julian FJ and Sollins R (1975) Variation of muscle stiffness with force at increasing speeds of shortening. J Gen Physiol 66: 287-302.
    • (1975) J Gen Physiol , vol.66 , pp. 287-302
    • Julian, F.J.1    Sollins, R.2
  • 30
    • 0019390460 scopus 로고
    • Enhancement and diminution of mechanical tension evoked by staircase and by tetanus in rat muscle
    • Krarup C (1981) Enhancement and diminution of mechanical tension evoked by staircase and by tetanus in rat muscle. J Physiol 311: 355-372.
    • (1981) J Physiol , vol.311 , pp. 355-372
    • Krarup, C.1
  • 31
    • 0029757994 scopus 로고    scopus 로고
    • Myosin light chain phosphorylation affects the structure of rabbit skeletal muscle thick filaments
    • Levine RJC, Kensler RW, Yang Z, Stull JT and Sweeney HL (1996) Myosin light chain phosphorylation affects the structure of rabbit skeletal muscle thick filaments. Biophys J 71: 898-907.
    • (1996) Biophys J , vol.71 , pp. 898-907
    • Levine, R.J.C.1    Kensler, R.W.2    Yang, Z.3    Stull, J.T.4    Sweeney, H.L.5
  • 32
    • 0025690381 scopus 로고
    • The contractile response during steady lengthening of stimulated frog muscle fibres
    • Lombardi V and Piazzesi G (1990) The contractile response during steady lengthening of stimulated frog muscle fibres. J Physiol 431: 141-171.
    • (1990) J Physiol , vol.431 , pp. 141-171
    • Lombardi, V.1    Piazzesi, G.2
  • 33
    • 0023145253 scopus 로고
    • Posttetanic potentiation and skeletal muscle fatigue: Interactions with caffeine
    • Macintosh BR and Gardiner PF (1987) Posttetanic potentiation and skeletal muscle fatigue: interactions with caffeine. Can J Physiol Pharmacol 65(2): 260-268.
    • (1987) Can J Physiol Pharmacol , vol.65 , Issue.2 , pp. 260-268
    • Macintosh, B.R.1    Gardiner, P.F.2
  • 34
    • 0029961277 scopus 로고    scopus 로고
    • Relationship between short-range stiffness and yielding in type-identified, chemically skinned muscle fibers from the cat triceps surac muscles
    • Malamud JG, Godt RE and Nichols TR (1996) Relationship between short-range stiffness and yielding in type-identified, chemically skinned muscle fibers from the cat triceps surac muscles. J Neurophysiol 76: 2280-2289.
    • (1996) J Neurophysiol , vol.76 , pp. 2280-2289
    • Malamud, J.G.1    Godt, R.E.2    Nichols, T.R.3
  • 35
    • 0024157190 scopus 로고
    • Length and myofilament spacing-dependent changes in calcium sensitivity of skeletal fibres: Effects of pH and ionic strength
    • Martyn DA and Gordon AM (1988) Length and myofilament spacing-dependent changes in calcium sensitivity of skeletal fibres: effects of pH and ionic strength. J Muscle Res Cell Motil 9: 428-445.
    • (1988) J Muscle Res Cell Motil , vol.9 , pp. 428-445
    • Martyn, D.A.1    Gordon, A.M.2
  • 36
    • 0024312136 scopus 로고
    • Variations in cross-bridge attachment rate and tension with phosphorylation of myosin in mammalian skinned skeletal muscle fibers
    • Metzger JM, Greaser ML and Moss RL (1989) Variations in cross-bridge attachment rate and tension with phosphorylation of myosin in mammalian skinned skeletal muscle fibers. J Gen Physiol 93: 855-883.
    • (1989) J Gen Physiol , vol.93 , pp. 855-883
    • Metzger, J.M.1    Greaser, M.L.2    Moss, R.L.3
  • 40
    • 19244383408 scopus 로고
    • Myosin light chain phosphorylation in fast and slow skeletal muscle in situ
    • Moore RL and Stull JT (1984) Myosin light chain phosphorylation in fast and slow skeletal muscle in situ. Am J Physiol 247: C462-C471.
    • (1984) Am J Physiol , vol.247
    • Moore, R.L.1    Stull, J.T.2
  • 41
    • 0023784840 scopus 로고
    • Myofibrillar calcium sensitivity modulation: Influence of light chain phosphorylation and positive inotropic drugs on skinned frog skeletal muscle
    • Morano I, Piazzesi G and Rüegg JC (1988) Myofibrillar calcium sensitivity modulation: influence of light chain phosphorylation and positive inotropic drugs on skinned frog skeletal muscle. Adv Exp Med Biol 226: 129-137.
    • (1988) Adv Exp Med Biol , vol.226 , pp. 129-137
    • Morano, I.1    Piazzesi, G.2    Rüegg, J.C.3
  • 42
    • 0020644495 scopus 로고
    • 2+ sensitivity of tension development by single skeletal muscle fibers at stretched lengths
    • 2+ sensitivity of tension development by single skeletal muscle fibers at stretched lengths. Biophys J 43: 115-119.
    • (1983) Biophys J , vol.43 , pp. 115-119
    • Moss, R.L.1    Swinford, A.2    Greaser, M.L.3
  • 43
    • 0031972823 scopus 로고    scopus 로고
    • Phosphorylation of myosin regulatory tight chain eliminates force-dependent changes in relaxation rates in skeletal muscle
    • Patel JR, Diffee GM, Huang XT and Moss RL (1998) Phosphorylation of myosin regulatory tight chain eliminates force-dependent changes in relaxation rates in skeletal muscle. Biophys J 74: 360-368.
    • (1998) Biophys J , vol.74 , pp. 360-368
    • Patel, J.R.1    Diffee, G.M.2    Huang, X.T.3    Moss, R.L.4
  • 44
    • 0021961219 scopus 로고
    • The effect of myosin phosphorylation on the contractile properties of skinned rabbit skeletal muscle fibers
    • Persechini A, Stull JT and Cooke R (1985) The effect of myosin phosphorylation on the contractile properties of skinned rabbit skeletal muscle fibers. J Biol Chem 260: 7951-7954.
    • (1985) J Biol Chem , vol.260 , pp. 7951-7954
    • Persechini, A.1    Stull, J.T.2    Cooke, R.3
  • 45
    • 0029982683 scopus 로고    scopus 로고
    • Mechanics of feline soleus: I. Effect of fascicle length and velocity on force output
    • Scott SH, Brown IE and Loeb GE (1996) Mechanics of feline soleus: I. Effect of fascicle length and velocity on force output. J Muscle Res Cell Motil 17: 205-218.
    • (1996) J Muscle Res Cell Motil , vol.17 , pp. 205-218
    • Scott, S.H.1    Brown, I.E.2    Loeb, G.E.3
  • 46
    • 0021166284 scopus 로고
    • Length dependence of changes in sarcoplasmic calcium concentration and myofibrillar calcium sensitivity in striated muscle fibres
    • Stephenson DG and Wendt IR (1984) Length dependence of changes in sarcoplasmic calcium concentration and myofibrillar calcium sensitivity in striated muscle fibres. J Muscle Res Cell Motil 5: 243-272.
    • (1984) J Muscle Res Cell Motil , vol.5 , pp. 243-272
    • Stephenson, D.G.1    Wendt, I.R.2
  • 47
    • 0020334224 scopus 로고
    • Effects of sarcomere length on the force-pCa relation in fast-and slow-twitch skinned muscle fibres from the rat
    • Stephenson DG and Williams DA (1982) Effects of sarcomere length on the force-pCa relation in fast-and slow-twitch skinned muscle fibres from the rat. J Physiol 333: 637-653.
    • (1982) J Physiol , vol.333 , pp. 637-653
    • Stephenson, D.G.1    Williams, D.A.2
  • 48
    • 0021895461 scopus 로고
    • Temperature-dependent calcium sensitivity changes in skinned muscle fibres of rat and toad
    • Stephenson DG and Williams DA (1985) Temperature-dependent calcium sensitivity changes in skinned muscle fibres of rat and toad. J Physiol 360: 1-12.
    • (1985) J Physiol , vol.360 , pp. 1-12
    • Stephenson, D.G.1    Williams, D.A.2
  • 50
    • 0023901322 scopus 로고
    • Myosin light chain phosphorylation and contractile performance of human skeletal muscle
    • Stuart DS, Lingley MD, Grange RW and Houston ME (1988) Myosin light chain phosphorylation and contractile performance of human skeletal muscle. Can J Physiol Pharmacol 66: 49-54.
    • (1988) Can J Physiol Pharmacol , vol.66 , pp. 49-54
    • Stuart, D.S.1    Lingley, M.D.2    Grange, R.W.3    Houston, M.E.4
  • 52
    • 0027300234 scopus 로고
    • Myosin light chain phosphorylation in vertebrate striated muscle: Regulation and function
    • Sweeney HL, Bowman BF and Stull JT (1993) Myosin light chain phosphorylation in vertebrate striated muscle: regulation and function. Am J Physiol 264: C1085-C1095.
    • (1993) Am J Physiol , vol.264
    • Sweeney, H.L.1    Bowman, B.F.2    Stull, J.T.3
  • 53
    • 0025061076 scopus 로고
    • Alteration of cross-bridge kinetics by myosin light chain phosphorylation in rabbit skeletal muscle: Implications for regulation of actin-myosin interaction
    • Sweeney HL and Stull JT (1990) Alteration of cross-bridge kinetics by myosin light chain phosphorylation in rabbit skeletal muscle: Implications for regulation of actin-myosin interaction. Proc Natl Acad Sci USA 87: 414-418.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 414-418
    • Sweeney, H.L.1    Stull, J.T.2
  • 54
    • 0030430459 scopus 로고    scopus 로고
    • Phosphorylation of myosin and twitch potentiation in fatigued skeletal muscle
    • Vandenboom R and Houston ME (1996) Phosphorylation of myosin and twitch potentiation in fatigued skeletal muscle. Can J Physiol Pharmacol 74: 1315-1321.
    • (1996) Can J Physiol Pharmacol , vol.74 , pp. 1315-1321
    • Vandenboom, R.1    Houston, M.E.2
  • 55
    • 0021145619 scopus 로고
    • Twitch characteristics in relation to muscle architecture and actual muscle length
    • Woittiez RD, Huijing PA and Rozendal RH (1984) Twitch characteristics in relation to muscle architecture and actual muscle length. Pflügers Arch 401: 374-379.
    • (1984) Pflügers Arch , vol.401 , pp. 374-379
    • Woittiez, R.D.1    Huijing, P.A.2    Rozendal, R.H.3
  • 56
    • 0031692828 scopus 로고    scopus 로고
    • Changes in interfilament spacing mimic the effects of myosin regulatory light chain phosphorylation in rabbit psoas fibers
    • Yang Z, Stull JT, Levine RJC and Sweeney HL (1998) Changes in interfilament spacing mimic the effects of myosin regulatory light chain phosphorylation in rabbit psoas fibers. J Struct Biol 122: 139-148.
    • (1998) J Struct Biol , vol.122 , pp. 139-148
    • Yang, Z.1    Stull, J.T.2    Levine, R.J.C.3    Sweeney, H.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.