Literature DB >> 8735707

Force responses following stepwise length changes of rat skeletal muscle fibre types.

S Galler1, K Hilber, D Pette.   

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.

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Year:  1996        PMID: 8735707      PMCID: PMC1158963          DOI: 10.1113/jphysiol.1996.sp021377

Source DB:  PubMed          Journal:  J Physiol        ISSN: 0022-3751            Impact factor:   5.182


  29 in total

1.  Rapid dissociation and reassociation of actomyosin cross-bridges during force generation: a newly observed facet of cross-bridge action in muscle.

Authors:  B Brenner
Journal:  Proc Natl Acad Sci U S A       Date:  1991-12-01       Impact factor: 11.205

2.  Myosin head movements are synchronous with the elementary force-generating process in muscle.

Authors:  M Irving; V Lombardi; G Piazzesi; M A Ferenczi
Journal:  Nature       Date:  1992-05-14       Impact factor: 49.962

Review 3.  Cellular and molecular diversities of mammalian skeletal muscle fibers.

Authors:  D Pette; R S Staron
Journal:  Rev Physiol Biochem Pharmacol       Date:  1990       Impact factor: 5.545

4.  Full-length rat alpha and beta cardiac myosin heavy chain sequences. Comparisons suggest a molecular basis for functional differences.

Authors:  E M McNally; R Kraft; M Bravo-Zehnder; D A Taylor; L A Leinwand
Journal:  J Mol Biol       Date:  1989-12-05       Impact factor: 5.469

5.  Myosin heavy chain isoforms in histochemically defined fiber types of rat muscle.

Authors:  A Termin; R S Staron; D Pette
Journal:  Histochemistry       Date:  1989

6.  Rapid regeneration of the actin-myosin power stroke in contracting muscle.

Authors:  V Lombardi; G Piazzesi; M Linari
Journal:  Nature       Date:  1992-02-13       Impact factor: 49.962

7.  Structure of the actin-myosin complex and its implications for muscle contraction.

Authors:  I Rayment; H M Holden; M Whittaker; C B Yohn; M Lorenz; K C Holmes; R A Milligan
Journal:  Science       Date:  1993-07-02       Impact factor: 47.728

8.  Effects of taurine on Ca2(+)-dependent force development of skinned muscle fibre preparations.

Authors:  S Galler; C Hutzler; T Haller
Journal:  J Exp Biol       Date:  1990-09       Impact factor: 3.312

9.  Force and stiffness in glycerinated rabbit psoas fibers. Effects of calcium and elevated phosphate.

Authors:  D A Martyn; A M Gordon
Journal:  J Gen Physiol       Date:  1992-05       Impact factor: 4.086

10.  Effect of osmotic compression on the force-velocity properties of glycerinated rabbit skeletal muscle cells.

Authors:  L E Ford; K Nakagawa; J Desper; C Y Seow
Journal:  J Gen Physiol       Date:  1991-01       Impact factor: 4.086

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  24 in total

1.  Shortening properties of two biochemically defined muscle fibre types of the Norway lobster Nephrops norvegicus L.

Authors:  J M Holmes; K Hilber; S Galler; D M Neil
Journal:  J Muscle Res Cell Motil       Date:  1999-04       Impact factor: 2.698

2.  Energy transfer during stress relaxation of contracting frog muscle fibres.

Authors:  M Mantovani; N C Heglund; G A Cavagna
Journal:  J Physiol       Date:  2001-12-15       Impact factor: 5.182

3.  The effects of ramp stretches on active contractions in intact mammalian fast and slow muscle fibres.

Authors:  G Mutungi; K W Ranatunga
Journal:  J Muscle Res Cell Motil       Date:  2001       Impact factor: 2.698

4.  Stretch activation and myosin heavy chain isoforms of rat, rabbit and human skeletal muscle fibres.

Authors:  S Galler; K Hilber; D Pette
Journal:  J Muscle Res Cell Motil       Date:  1997-08       Impact factor: 2.698

5.  Functional properties of skinned rabbit skeletal and cardiac muscle preparations containing alpha-cardiac myosin heavy chain.

Authors:  Oleg Andruchov; Yishu Wang; Olena Andruchova; Stefan Galler
Journal:  Pflugers Arch       Date:  2004-01-16       Impact factor: 3.657

6.  Cross-bridge number, position, and angle in target zones of cryofixed isometrically active insect flight muscle.

Authors:  Richard T Tregear; Mary C Reedy; Yale E Goldman; Kenneth A Taylor; Hanspeter Winkler; Clara Franzini-Armstrong; Hiroyuki Sasaki; Carmen Lucaveche; Michael K Reedy
Journal:  Biophys J       Date:  2004-05       Impact factor: 4.033

7.  Influence of fast and slow alkali myosin light chain isoforms on the kinetics of stretch-induced force transients of fast-twitch type IIA fibres of rat.

Authors:  Oleg Andruchov; Stefan Galler
Journal:  Pflugers Arch       Date:  2007-10-25       Impact factor: 3.657

Review 8.  Molecular basis of the catch state in molluscan smooth muscles: a catchy challenge.

Authors:  Stefan Galler
Journal:  J Muscle Res Cell Motil       Date:  2008-11-28       Impact factor: 2.698

9.  Quantitative evaluation of the relationship between Ca2+ sensitivity and sarcomere length in rat soleus after 14-day hindlimb suspension.

Authors:  V A Kurushin; E V Ponomareva; I V Ogneva; E N Lipets; B S Shenkman
Journal:  Dokl Biol Sci       Date:  2009 Jan-Feb

10.  Improvement of the measurements on skinned muscle fibres by fixation of the fibre ends with glutaraldehyde.

Authors:  K Hilber; S Galler
Journal:  J Muscle Res Cell Motil       Date:  1998-05       Impact factor: 2.698

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