pmc logo imageJournal ListSearchpmc logo image
Logo of jphysiolThe Journal of Physiology SiteMembershipSubmissionJ Physiol
J Physiol. 1996 May 15; 493(Pt 1): 219–227.
PMCID: PMC1158963
Force responses following stepwise length changes of rat skeletal muscle fibre types.
S Galler, K Hilber, and D Pette
Department of Physiology, Institute of Zoology, University of Salzburg, Austria.
Abstract
1. Force responses following stepwise length changes of Ca(2+)-activated skinned leg muscle fibres (6 degrees C) of the rat were correlated with their myosin heavy chain (HC) isoforms (myosin HC I, fibre type I; myosin HC IIA, type IIA; myosin HC IID (HC IIX), type IID (type IIX); myosin HC IIB, type IIB) in order to study the mechanical properties of these molecules. 2. Marked differences in the time behaviour of force transients following quick releases of fibre length existed between various muscle fibres, and a conspicuous correlation with their myosin HC complement was noticed (order of velocity: IIB > IID > IIA > > I). No differences were found in the relationship between the applied length step and the resulting force (T1, T2 curves). 3. Our results suggest that the heads of various myosin heavy chain isoforms exhibit different kinetic properties. The differences concern the kinetics of the myosin head movements and the duration of cyclic interactions between myosin heads and thin filaments. The extent of force-generating movements and the mean elongation of attached heads in the isometric state seem to be independent of the isoform.
Full text
Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (1.4M), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References.
Images in this article
Click on the image to see a larger version.
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
  • Bottinelli, R; Betto, R; Schiaffino, S; Reggiani, C. Unloaded shortening velocity and myosin heavy chain and alkali light chain isoform composition in rat skeletal muscle fibres. J Physiol. 1994 Jul 15;478 (:341–349. [PubMed]
  • Bottinelli, R; Canepari, M; Reggiani, C; Stienen, GJ. Myofibrillar ATPase activity during isometric contraction and isomyosin composition in rat single skinned muscle fibres. J Physiol. 1994 Dec 15;481 (:663–675. [PubMed]
  • Brenner, B. Rapid dissociation and reassociation of actomyosin cross-bridges during force generation: a newly observed facet of cross-bridge action in muscle. Proc Natl Acad Sci U S A. 1991 Dec 1;88(23):10490–10494. [PubMed]
  • Edman, KA. The velocity of unloaded shortening and its relation to sarcomere length and isometric force in vertebrate muscle fibres. J Physiol. 1979 Jun;291:143–159. [PubMed]
  • Edman, KA; Reggiani, C; Schiaffino, S; te Kronnie, G. Maximum velocity of shortening related to myosin isoform composition in frog skeletal muscle fibres. J Physiol. 1988 Jan;395:679–694. [PubMed]
  • Eisenberg, E; Hill, TL; Chen, Y. Cross-bridge model of muscle contraction. Quantitative analysis. Biophys J. 1980 Feb;29(2):195–227. [PubMed]
  • Ford, LE; Huxley, AF; Simmons, RM. Tension responses to sudden length change in stimulated frog muscle fibres near slack length. J Physiol. 1977 Jul;269(2):441–515. [PubMed]
  • Ford, LE; Huxley, AF; Simmons, RM. The relation between stiffness and filament overlap in stimulated frog muscle fibres. J Physiol. 1981 Feb;311:219–249. [PubMed]
  • Ford, LE; Nakagawa, K; Desper, J; Seow, CY. Effect of osmotic compression on the force-velocity properties of glycerinated rabbit skeletal muscle cells. J Gen Physiol. 1991 Jan;97(1):73–88. [PubMed]
  • Galler, S. Stretch activation of skeletal muscle fibre types. Pflugers Arch. 1994 Jun;427(3-4):384–386. [PubMed]
  • Galler, S; Hilber, K. Unloaded shortening of skinned mammalian skeletal muscle fibres: effects of the experimental approach and passive force. J Muscle Res Cell Motil. 1994 Aug;15(4):400–412. [PubMed]
  • Galler, S; Hutzler, C; Haller, T. Effects of taurine on Ca2(+)-dependent force development of skinned muscle fibre preparations. J Exp Biol. 1990 Sep;152:255–264. [PubMed]
  • Galler, S; Schmitt, TL; Pette, D. Stretch activation, unloaded shortening velocity, and myosin heavy chain isoforms of rat skeletal muscle fibres. J Physiol. 1994 Aug 1;478 Pt 3:513–521. [PubMed]
  • Heinl, P; Kuhn, HJ; Rüegg, JC. Tension responses to quick length changes of glycerinated skeletal muscle fibres from the frog and tortoise. J Physiol. 1974 Mar;237(2):243–258. [PubMed]
  • Huxley, AF; Simmons, RM. Proposed mechanism of force generation in striated muscle. Nature. 1971 Oct 22;233(5321):533–538. [PubMed]
  • Huxley, HE. The mechanism of muscular contraction. Science. 1969 Jun 20;164(886):1356–1365. [PubMed]
  • Irving, M; St Claire Allen, T; Sabido-David, C; Craik, JS; Brandmeier, B; Kendrick-Jones, J; Corrie, JE; Trentham, DR; Goldman, YE. Tilting of the light-chain region of myosin during step length changes and active force generation in skeletal muscle. Nature. 1995 Jun 22;375(6533):688–691. [PubMed]
  • Irving, M; Lombardi, V; Piazzesi, G; Ferenczi, MA. Myosin head movements are synchronous with the elementary force-generating process in muscle. Nature. 1992 May 14;357(6374):156–158. [PubMed]
  • Lombardi, V; Piazzesi, G; Linari, M. Rapid regeneration of the actin-myosin power stroke in contracting muscle. Nature. 1992 Feb 13;355(6361):638–641. [PubMed]
  • McNally, EM; Kraft, R; Bravo-Zehnder, M; Taylor, DA; Leinwand, LA. Full-length rat alpha and beta cardiac myosin heavy chain sequences. Comparisons suggest a molecular basis for functional differences. J Mol Biol. 1989 Dec 5;210(3):665–671. [PubMed]
  • Martyn, DA; Gordon, AM. Force and stiffness in glycerinated rabbit psoas fibers. Effects of calcium and elevated phosphate. J Gen Physiol. 1992 May;99(5):795–816. [PubMed]
  • Metzger, JM; Moss, RL. Calcium-sensitive cross-bridge transitions in mammalian fast and slow skeletal muscle fibers. Science. 1990 Mar 2;247(4946):1088–1090. [PubMed]
  • Moisescu, DG; Thieleczek, R. Calcium and strontium concentration changes within skinned muscle preparations following a change in the external bathing solution. J Physiol. 1978 Feb;275:241–262. [PubMed]
  • Oakley, BR; Kirsch, DR; Morris, NR. A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels. Anal Biochem. 1980 Jul 1;105(2):361–363. [PubMed]
  • Pette, D; Staron, RS. Cellular and molecular diversities of mammalian skeletal muscle fibers. Rev Physiol Biochem Pharmacol. 1990;116:1–76. [PubMed]
  • Rayment, I; Holden, HM; Whittaker, M; Yohn, CB; Lorenz, M; Holmes, KC; Milligan, RA. Structure of the actin-myosin complex and its implications for muscle contraction. Science. 1993 Jul 2;261(5117):58–65. [PubMed]
  • Saito, K; Aoki, T; Aoki, T; Yanagida, T. Movement of single myosin filaments and myosin step size on an actin filament suspended in solution by a laser trap. Biophys J. 1994 Mar;66(3 Pt 1):769–777. [PubMed]
  • Schiaffino, S; Gorza, L; Sartore, S; Saggin, L; Ausoni, S; Vianello, M; Gundersen, K; Lømo, T. Three myosin heavy chain isoforms in type 2 skeletal muscle fibres. J Muscle Res Cell Motil. 1989 Jun;10(3):197–205. [PubMed]
  • Termin, A; Staron, RS; Pette, D. Myosin heavy chain isoforms in histochemically defined fiber types of rat muscle. Histochemistry. 1989;92(6):453–457. [PubMed]