Abstract
We compared soleus muscles from two strains of mice, NMRI and C57. Soleus muscles from NMRI mice produced slower twitches and lower maximum tetanic force (F o) but higher maximum tetanic stress (S o), (owing to their smaller weight). Their Hill's velocity constant (b) was lower, but their force constant (a/S o), their maximum velocity of unloaded shortening (V u) and their maximal mechanical power (P max) were similar. All soleus muscles contained two isomyosins (SM2 and IM) and the two myosin heavy chains (MHC1 and MHC2A) corresponding to type I fibres and type IIA fibres; however, soleus muscles from NMRI strain had higher proportions of isomyosin SM2 and of myosin heavy chain 2A. Regression equations were computed between the mechanical variables and the myosin heavy chain content. Using a simple hypothesis, the results were used to estimate the mechanical properties of type I and type IIA fibres. We conclude that type IIA fibres from soleus muscle are mechanically more similar to slow-twitch type I fibres than to fast-twitch type II fibres. The results also suggest a hypothesis to account for the diversity of isomyosins, by a matching diversity of mechanical properties based on a separate physiological control of the three factors that control P max.
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d'Albis A, Janmot C, Béchet JJ (1986) Comparison of myosins from the masseter muscle of adult rat, mouse and guineapig. Persistence of neo-natal type isoforms in the murine muscle. Eur J Biochem 156: 291–296
Asmussen G, Maréchal G (1989) Maximal shortening velocities, isomyosins and fibre types in soleus muscle of mice, rats and guinea-pigs. J Physiol (Lond) 416: 245–254
Bottinelli R, Schiaffino S, Reggiani C (1991) Force-velocity relations and myosin heavy chain isoform compositions of skinned fibres from rat skeletal muscle. J Physiol (Lond) 437: 655–672
Bottinelli R, Betto R, Schiaffino S, Reggiani C (1992) Myosin heavy chain and myosin light chain composition and shortening velocity composition of rat skeletal muscle. J Muscle Res Cell Motil 13: 225
Biral D, Betto R, Danieli-Betto D, Salviati G (1988) Myosin heavy chain composition of single fibres from normal human muscle. Biochem J 250: 307–308
Brooke MH, Kaiser KK (1970) Three “myosin adenosine triphosphatase” systems: the nature of their pH lability and sulfhydryl dependance. J Histochem Cytochem 18: 670–672
Brooks SV, Faulkner JA (1988) Contractile properties of skeletal muscles from young, adult and aged mice. J Physiol (Lond) 404: 71–82
Brooks SV, Faulkner JA, McCubbrey DA (1990) Power output of slow and fast skeletal muscle of mice. J Appl Physiol 68: 1282–1285
Carraro U, Catani C (1983) A sensitive SDS-PAGE method separating myosin heavy chain isoforms of rat skeletal muscle reveals the heterogenous nature of the embryonic myosin. Biochem Biophys Res Commun 116: 793–802
Carraro U, Catani C, Degani A, Rizzi C (1990) Myosin expression in denervated fast and slow-twitch muscles: fiber modulation and substitution. In: Pette D (ed) The dynamic state of muscle fibers, de Gruyter, Berlin, pp 247–262
Cecchi G, Colomo F, Lombardi V (1978) Force-velocity relation in normal and nitrate-treated frog single fibres during rise of tension in an isometric tetanus. J Physiol (Lond) 285: 257–273
Danieli-Betto D, Zerbato E, Betto R (1986) Type I, IIa and IIb myosin heavy chain electrophoretic analysis of rat muscle fibres. Biochem Biophys Res Commun 138: 981–987
Edman KAP (1979) The velocity of unloaded shortening and its relation to sarcomere length and isometric force in vertebrate muscle fibres. J Physiol (Lond) 291: 143–159
Fitzsimons RB, Hoh JFY (1983) Myosin isoenzymes in fasttwitch and slow-twitch muscles of normal and dystrophic mice. J Physiol (Lond) 343: 539–550
Gorza L (1990) Identification of a novel type 2 fiber population in mammalian skeletal muscle by combined use of histochemical ATPase and anti-myosin monoclonal antibodies. J Histochem Cytochem 38: 257–265
Greaser ML, Moss RL, Reiser PJ (1988) Variations in contractile properties of rabbit single muscle fibres in relation to troponin T isoforms and myosin light chains. J Physiol (Lond) 406: 85–98
Gregory P, Low RB, Stirewalt WS (1986) Changes in skeletal myosin isoenzymes with hypertrophy and exercise. Biochem J 238: 53–63
Lewis DM, Parry M, Rowlerson A (1982) Isometric contractions of motor units and immunochemistry of mouse soleus muscle. J Physiol (Lond) 325: 393–401
Luff AR (1981) Dynamic properties of the inferior rectus, extensor digitorum longus, diaphragm and soleus muscles of the mouse. J Physiol (Lond) 313: 161–171
Maréchal G, Beckers-Bleukx G (1990) Force-velocity relationship of isomyosins SM2 and IM of mouse soleus (Strain NMRI). In: Maréchal G, Carraro U (eds) Muscle and motility, vol 2. Intercept, Newcastle upon Tyne, pp 291–297
Maréchal G, Plaghki L (1979) The deficit of the isometric tetanic tension redeveloped after a release of frog muscle at a constant velocity. J Gen Physiol 73: 453–467
Maréchal G, Schwartz K, Beckers-Bleukx G, Ghins E (1984) Isozymes of myosin in growing and regenerating rat muscles. Eur J Biochem 138: 421–428
Maréchal G, Biral D, Beckers-Bleukx G, Colson-Van Schoor M (1989) Subunit composition of native myosin isozymes of some striated mammalian muscles. Biomed Biochim Acta 48: S 417-S 421
Marini JF, Pons F, Anoal M, Leger J, Leger JJ (1989) Antimyosin heavy chain monoclonal antibodies reveal two IIB (fast) fiber subtypes. J Histochem Cytochem 37: 1721–1729
Parry DJ, DiCori S (1990) The relationship between post-tetanic potentiation of motor units and myosin isoforms in mouse soleus muscle. Can J Physiol Pharmacol 68: 51–56
Pette D, Staron RS (1990) Cellular and molecular diversities of mammalian skeletal muscle fibers. Rev Physiol Biochem Pharmacol 116: 2–76
Ranatunga KW (1984) The force-velocity relation of rat fast- and slow-twitch muscles examined at different temperatures. J Physiol (Lond) 351: 517–529
Ranatunga KW, Thomas PE (1990) Correlation between shortening velocity, force-velocity relation and histochemical fibre-type composition in rat muscle. J Muscle Res Cell Motil 11: 240–250
Reiser PJ, Moss RL, Giulian GG, Greaser ML (1985) Shortening velocity in single fibers from adult rabbit soleus muscle is correlated with myosin heavy chain composition. J Biol Chem 260: 9077–9080
Reiser PJ, Moss RL, Giulian GG, Greaser ML (1985) Shortening velocity and myosin heavy chains of developing rabbit muscle fibers. J Biol Chem 260: 14 403–14 405
Reiser RJ, Kasper CE, Moss RL (1987) Myosin subunits and contractile properties of single fibers from hypokinetic rat muscles. J Appl Physiol 63: 2293–2300
Rizzi C, Carraro U (1991) Electroendosmotic preparative gel electrophoresis and peptide mapping of slow and three fast myosin heavy chains: inter- and intra-specific polymorphism. Basic Appl Myol 1: 43–54
Rome LC, Funke RP, Alexander R McN, Lutz G, Aldridge H, Scott F, Freadman M (1988) Why animals have different muscle fibre types. Nature 335: 824–827
Rome LC, Sosnicki AA, Goble DO (1990) Maximum velocity of shortening of three fibres types from horse soleus muscle: implications for scaling with body size. J Physiol (Lond) 431: 173–185
Schiaffino S, Gorza L, Sartore S, Saggin L, Ausoni S, Vianello M, Gundersen K, Lömo T (1989) Three myosin heavy chain isoforms in type 2 skeletal muscle fibres. J Muscle Res Cell Motil 10: 197–205
Staron SR, Pette D (1986) Correlation between myofibrillar ATPase activity and myosin heavy chain composition in rabbit muscle fibers. Histochemistry 86: 19–23, 34
Staron SR, Pette D (1987) The multiplicity of combinations of myosin light chains and heavy chains in histochemically typed single fibres. Rabbit soleus muscle. Biochem J 243: 687–693
Staron SR, Pette D (1987) The multiplicity of combinations of myosin light chains and heavy chains in histochemically typed single fibres. Rabbit tibialis anterior muscle. Biochem J 243: 695–699
Sweeney HL, Kushmerick MJ, Mabuchi K, Sréter FA, Gergely J (1986) Velocity of shortening and myosin isozymes in two types of rabbit fast-twitch muscle fibers. Am J Physiol 251: C 431-C 434
Sweeney HL, Kushmerick MJ, Mabuchi K, Sréter FA, Gergely J (1988) Myosin alkali light chain and heavy chain variations correlate with altered shortening velocity of isolated skeletal muscle fibers. J Biol Chem 263: 9034–9039
Termin A, Pette D (1991) Myosin heavy chain based isomyosins in developing adult fast-twitch and slow-twitch muscles. Eur J Biochem 195: 577–584
Termin A, Staron RS, Pette D (1989) Myosin heavy chain isoforms in histochemically defined fiber types of rat muscle. Histochemistry 92: 453–457
Woledge RC, Curtin NA, Homsher E (1985) Energetic aspects of muscle contraction. Monographs of the Royal Society No 41. Academic Press, London
Yamaoka K, Tanigawara Y, Nakagawa T, Uno T (1981) Pharmacokinetic analysis program (multi) for microcomputer. J Pharm Dyn 4: 879–885
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Maréchal, G., Beckers-Bleukx, G. Force-velocity relation and isomyosins in soleus muscles from two strains of mice (C57 and NMRI). Pflügers Arch. 424, 478–487 (1993). https://doi.org/10.1007/BF00374911
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DOI: https://doi.org/10.1007/BF00374911