Please confirm you are human (Sign Up for free to never see this)
← Back to Search
Force‐velocity Relations And Myosin Heavy Chain Isoform Compositions Of Skinned Fibres From Rat Skeletal Muscle.
R. Bottinelli, S. Schiaffino, C. Reggiani
Published 1991 · Chemistry, Medicine
Save to my Library
Download PDFAnalyze on Scholarcy
1. This study was performed to assess whether muscle contractile properties are related to the presence of specific myosin heavy chain (MHC) isoforms. 2. Force‐velocity relations and MHC isoform composition were determined in seventy‐four single skinned muscle fibres from rat soleus, extensor digitorum longus and plantaris muscles. 3. Four groups of fibres were identified according to their MHC isoform composition determined by monoclonal antibodies: type 1 (slow), and types 2A, 2B and 2X (fast). 4. With respect to maximum velocity of shortening (V0), the fibres formed a continuum between 0.35 and 2.84 L/s (muscle lengths per second) at 12 degrees C. V0 in type 1 fibres (slow fibres) was between 0.35 and 0.95 L/s (0.639 +/‐ 0.038 L/s; mean +/‐ S.E. of mean). V0 in type 2 fibres (fast fibres) was consistently higher than 0.91 L/s. Ranges of V0 in the three fast fibre types mostly overlapped. Type 2A and 2X fibres had similar mean V0 values (1.396 +/‐ 0.084 and 1.451 +/‐ 0.066 L/s respectively); type 2B fibres showed a higher mean V0 value (1.800 +/‐ 0.109 L/s) than type 2A and 2X fibres. 5. Mean values of a/P0, an index of the curvature of force‐velocity relations, allowed us to identify two groups of fibres: a high curvature group comprised of type 1 (mean a/P0, 0.066 +/‐ 0.007) and 2A (0.066 +/‐ 0.024) fibres and a low curvature group comprised of type 2B (0.113 +/‐ 0.013) and 2X (0.132 +/‐ 0.008) fibres. 6. Maximal power output was lower in slow fibres than in fast fibres, and among fast fibres it was lower in type 2A fibres than in type 2X and 2B. 7. Force per unit cross‐sectional area was less in slow fibres than in fast fibres. There was no relation between fibre type and cross‐sectional area. 8. The results suggest that MHC composition is just one of the determinants of shortening velocity and of other muscle contractile properties.
This paper references
Histochemical manifestations of age and endurance training in skeletal muscle fibers.
L. C. Maxwell (1973)
Correlation between troponin-T and myosin
D. PETTE (1990)
Differences in maximum velocity of shortening along single muscle fibres of the frog.
K. A. Edman (1985)
Energetic Aspects of Muscle Contraction
A. Somlyo (1986)
Changes in myosin heavy chain isoforms during chronic low-frequency stimulation of rat fast hindlimb muscles. A single-fiber study.
A. Termin (1989)
Myosin isoenzymic changes
K. SCHWARTZ (1981)
Swelling of skinned muscle fibres of the frog
D. W. MAUGHAN (1977)
Muscle fiber types identified by monoclonal antibodies to myosin heavy chains
S. Schiaffino (1986)
Correlation between myofibrillar ATPase activity and myosin heavy chain composition in rabbit muscle fibers
R. S. Staron (2004)
Variations in contractile properties of rabbit single muscle fibres in relation to troponin T isoforms and myosin light chains.
M. Greaser (1988)
The multiplicity of combinations of myosin light chains and heavy chains in histochemically typed single fibres. Rabbit soleus muscle.
R. S. Staron (1987)
THE MUSCLE FIBRE
A. McComas (1977)
b). The multiplicity of combinations of myosin light chains and heavy chains in histochemically typed single fibres. Rabbit tibialis anterior muscle
S R Staron (1987)
Temperature‐dependence of shortening velocity and rate of isometric tension development in rat skeletal muscle
K. W. Ranatunga (1982)
THREE "MYOSIN ADENOSINE TRIPHOSPHATASE" SYSTEMS: THE NATURE OF THEIR pH LABILITY AND SULFHYDRYL DEPENDENCE
M. Brooke (1970)
Technique for stabilizing the striation pattern in maximally calcium-activated skinned rabbit psoas fibers.
B. Brenner (1983)
The dependence of force and
R. M. SIMMONS (1984)
Correlation between troponin - T and myosin heavy chain isoforms in normal and transforming rabbit muscle fibres
G. BENZI (1990)
Computer programs for calculating total
A. FABIATO (1988)
Varied Expression of Myosin Alkali Light Chains is Associated with Altered Speed of Contraction in Rabbit Fast-Twitch Skeletal Muscles
R. Moss (1990)
B. SCHUBON-MULIERI (1976)
Three fast myosin heavy chains in adult rat skeletal muscle
A. Baer (1988)
Type I, Ila and Ilb myosin heavy chain electrophoretic analysis of rat muscle fibres
D. DANIELI-BETTO (1986)
The dependence of force and shortening velocity on substrate concentration in skinned muscle fibres from Rana temporaria.
M. Ferenczi (1984)
Dynamic properties of fast and slow skeletal muscles of the rat after nerve cross‐union
R. Close (1969)
Three myosin adenosine triphosphatase
K. K. KAISER (1970)
D. A. LIEBERMAN (1973)
Mechanical and histochemical characterization of skeletal muscles from senescent rats.
T. Eddinger (1986)
The energetics of tortoise muscle
R. Woledge (1968)
Computer programs for calculating total from specified free or free from specified total ionic concentrations in aqueous solutions containing multiple metals and ligands.
A. Fabiato (1988)
Mechanical properties of skinned single fibres of identified
R. L. Moss (1987)
The maximum speed of shortening in living and skinned frog muscle fibres.
F. Julian (1986)
Mechanical properties of skinned single fibers of identified types from rat diaphragm.
T. Eddinger (1987)
Double‐hyperbolic force‐velocity relation in frog muscle fibres.
K. A. Edman (1988)
Varied expression of myosin
T. J. EDDINGER (1990)
The multiplicity of combinations of myosin light chains and heavy chains in histochemically typed single fibres. Rabbit tibialis anterior muscle.
R. S. Staron (1987)
Maximum velocity of shortening related to myosin isoform composition in frog skeletal muscle fibres.
K. A. Edman (1988)
Myosin heavy chain composition of single cells from avian slow skeletal muscle is strongly correlated with velocity of shortening during development.
P. Reiser (1988)
Three fast myosin heavy chains
D. PETTE (1988)
Myosin Isoenzymic Changes in Several Models of Rat Cardiac Hypertrophy
J. Mercadier (1981)
Effect of free calcium
B. BRENNER (1980)
Non-hyperbolic force-velocity relationship in single muscle fibres.
K. A. Edman (1976)
Double-hyperbolic force-velocity relation
K.A.P. EDMAN (1988)
All members of the MHC multigene family respond to thyroid hormone in a highly tissue-specific manner.
S. Izumo (1986)
Myosin alkali light chain and heavy chain variations correlate with altered shortening velocity of isolated skeletal muscle fibers.
H. Sweeney (1988)
Functional significance of myosin transitions in single fibers of developing soleus muscle.
P. Reiser (1988)
Swelling of skinned muscle fibers of the frog. Experimental observations.
R. Godt (1977)
Shortening velocity in single fibers from adult rabbit soleus muscles is correlated with myosin heavy chain composition.
P. Reiser (1985)
This paper is referenced by
Myofibrillar ATPase activity of feline muscle fibers expressing slow and fast myosin heavy chains.
R. Talmadge (1995)
Distribution Pattern of Muscle Fibre Types In Soft Palate of the Dog (Canis familiaris, L.)
C. Sánchez-Collado (2014)
Power output of skinned skeletal muscle fibres from the cheetah (Acinonyx jubatus)
T. West (2013)
New perspectives about human laryngeal muscle: single-fiber analyses and interspecies comparisons.
Y. Z. Wu (2000)
Regulation of Jaw-specific Isoforms of Myosin-binding Protein-C and Tropomyosin in Regenerating Cat Temporalis Muscle Innervated by Limb Fast and Slow Motor Nerves
L. Kang (2010)
A curve-fitting procedure to explain changes in muscle force-velocity relationship induced by hyperactivity.
O. Allaf (2002)
Single-fiber and whole muscle analyses of MHC isoform plasticity: interaction between T3 and unloading.
V. Caiozzo (1997)
Resistance training of long duration modulates force and unloaded shortening velocity of single muscle fibres of young women.
O. Pansarasa (2009)
Effects of longitudinal body position and swimming speed on mechanical power of deep red muscle from skipjack tuna (Katsuwonus pelamis).
D. Syme (2002)
Regional variation in parvalbumin isoform expression correlates with muscle performance in common carp (Cyprinus carpio)
Philip J. Brownridge (2009)
Alterations at the Cross-Bridge Level Are Associated with a Paradoxical Gain of Muscle Function In Vivo in a Mouse Model of Nemaline Myopathy
C. Gineste (2014)
Whole-muscle and single-fibre contractile properties and myosin heavy chain isoforms in humans
S. Harridge (2009)
Performance and fibre characteristics of human skeletal muscle during short sprint training and detraining on a cycle ergometer
M.-T. Linossier (1997)
Functional diversity among a family of human skeletal muscle myosin motors
Daniel I. Resnicow (2009)
contractility of developing rat diaphragm muscle Denervation alters myosin heavy chain expression and
Gary C. Sieck (2015)
Effects of stretching stress on the muscle contraction proteins of skeletal muscle myoblasts.
K. Sakiyama (2005)
Plasticity in Skeletal , Cardiac , and Smooth Muscle Invited Review : Plasticity and energetic demands of contraction in skeletal and cardiac muscle
G. Sieck (2001)
Quantifying the effect of age and contraction mode on the force-velocity-power relationship in the knee extensors
Justin R. Paturel (2014)
Characterization of microRNA Function During Skeletal Myogenesis
Martin G. Guess (2014)
Morphological Characterization of the Levator Veli Palatini Muscle in Children Born with Cleft Palates
Rolf Lindman (2001)
Immunohistochemical analysis of laryngeal muscle of horses clinically affected with recurrent laryngeal neuropathy.
C. Steel (2020)
Sternohyoid and diaphragm muscle form and function during postnatal development in the rat
R. O'Connell (2013)
myosin heavy chain isoform ATP consumption rate per cross bridge depends on
Youngsoo Han (2015)
Identification, distribution, and myosin subunit composition of type IIX fibers in mouse muscles
D. Zardini (1994)
Characteristics of Myofibres in the Masseter Muscle of Mice during Postnatal Growth Period
K. Gojo (2002)
Why adult mammalian intrafusal and extrafusal fibers contain different myosin heavy-chain isoforms
J. Walro (1999)
Expression of extraocular myosin heavy chain in rabbit laryngeal muscle
C. Lucas (2004)
The Changes in Myosin Heavy Chain Isoforms After Extraocular Muscle Recession in Rabbits
H. Sa (2009)
Sensitive detection of myosin heavy chain composition in skeletal muscle under different loading conditions.
S. Fauteck (1995)
UNIVERSIDADE ESTADUAL PAULISTA FACULDADE DE CIÊNCIAS AGRÁRIAS E VETERINÁRIAS CÂMPUS DE JABOTICABAL ADAPTAÇÕES DO MÚSCULO GLÚTEO MÉDIO EM EQÜINOS SUBMETIDOS A TREINAMENTO DE RESISTÊNCIA E SUPLEMENTADOS COM DIFERENTES CONCENTRAÇÕES DE ÓLEO DE SOJA
C. Martins (2007)
The Extraocular Muscles
L. McLoon (2011)See more