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Myosin Gene Expression In The Respiratory Muscles.

J. Gea
Published 1997 · Biology, Medicine

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Myosin is one of the basic structural components of skeletal muscles. Its interaction with actin results in muscle contraction. The myosin molecule is composed of two heavy (MyHC) and two light chains (MyLC) that, together with the adenosine triphosphatase (ATPase) activity, determine the functional characteristics of the fibre. Both MyHC and MyLC present different isoforms. The main MyHC isoforms in adult mammals are the slow MyHC (MyHC-I) and fast MyHCs (MyHC-IIa, MyHC-IIb and MyHC-IIx). Muscle fibres can express only one isoform or coexpress different forms. The muscle phenotype is the product of genome plus environmental stimuli. The family of genes that codifies the MyHC isoforms is located in two different clusters, each isoform being encoded by a separate gene. The gene corresponding to slow MyHC is located in chromosome 14, both in humans and in mice. The other genes are positioned in chromosome 17 in humans, and in chromosome 11 in mice. The transcriptional and translational mechanisms that control the expression of MyHC isoforms are not well known, although it is believed that the main regulation is dependent on mechanical signals. These signals are probably mediated by a biochemical messenger. As a general rule, fast MyHC genes seem to be expressed "by default", whereas the slow MyHC gene would be expressed as a response to changes in load. So far, few studies have analysed the in vivo regulation of MyHC gene expression in respiratory muscles. It has recently been reported that breathing against moderate levels of inspiratory resistance quickly induces an increase in the genetic expression of slow MyHC in the diaphragm. This suggests the possibility of eliciting a phenotypic adaptation of respiratory muscles using specific training protocols.
This paper references
Postnatal expression of myosin lsoforms in the genioglossus and diaphragm muscles.
B. Brozanski (1993)
Organization of the human skeletal myosin heavy chain gene cluster.
S. Yoon (1992)
Myosin heavy chain expression in respiratory muscles of the rat.
W. LaFramboise (1992)
Fibre types, calcium‐sequestering proteins and metabolic enzymes in denervated and chronically stimulated muscles of the rat.
K. Gundersen (1988)
Synchronously stimulated skeletal muscle graft for myocardial repair. An experimental study.
M. Dewar (1984)
Time course of soleus muscle myosin expression during hindlimb suspension and recovery.
D. Thomason (1987)
An age-related type IIB to IIX myosin heavy chain switching in rat skeletal muscle.
L. Larsson (1993)
Shortening velocity in single fibers from adult rabbit soleus muscles is correlated with myosin heavy chain composition.
P. Reiser (1985)
Effects of endurance training on myosin heavy-chain isoforms and enzyme activity in the rat diaphragm
T. Sugiura (2004)
Adaptation of rat extensor digitorum longus to overload and increased activity
R. Frischknecht (2004)
Myosin alkali light chain and heavy chain variations correlate with altered shortening velocity of isolated skeletal muscle fibers.
H. Sweeney (1988)
Interaction of compensatory hypertrophy and hindlimb suspension on myosin isoform expression
RW Tsika (1987)
Skeletal muscle adaptations during early phase of heavy-resistance training in men and women.
R. S. Staron (1994)
Myosin heavy chain composition and enzyme-histochemical and physiological properties of a novel fast-twitch motor unit type.
L. Larsson (1991)
Three slow myosin heavy chains sequentially expressed in developing mammalian skeletal muscle.
S. Hughes (1993)
Regional Distribution of Myosin Heavy Chain Isoforms in Rib Cage Muscles as a Function of Postnatal Development
R. L. Vazquez (1993)
Effects of chronic low frequency stimulation on structural and metabolic properties of hindlimb suspended rat soleus muscle
F. Canon (2004)
Skeletal muscle fibre types, physical performance, physical activity and attitude to physical activity in women and men. A follow-up from age 16 to 27.
B. Glenmark (1994)
Type IIx myosin heavy chain transcripts are expressed in type IIb fibers of human skeletal muscle.
V. Smerdu (1994)
Force-velocity relation and myosin heavy chain isoform composition in skinned fibres of rat skeletal muscle
R Bottinelli (1991)
Effect of spaceflight on skeletal muscle: mechanical properties and myosin isoform content of a slow muscle.
V. Caiozzo (1994)
In vivo 31P-NMR spectroscopy of chronically stimulated canine skeletal muscle.
B. Clark (1988)
Genes for skeletal muscle myosin heavy chains are clustered and are not located on the same mouse chromosome as a cardiac myosin heavy chain gene.
A. Weydert (1985)
Invited review: Neural control of phenotypic expression in mammalian muscle fibers
D. Pette (1985)
Stretch and force generation induce rapid hypertrophy and myosin isoform gene switching in adult skeletal muscle.
G. Goldspink (1991)
Acute and Chronic Response of Skeletal Muscle to Resistance Exercise
P. Abernethy (1994)
Cellular and molecular diversities of mammalian skeletal muscle fibres
D Pette (1990)
Interaction of various mechanical activity models in regulation of myosin heavy chain isoform expression.
G. Diffee (1993)
All members of the MHC multigene family respond to thyroid hormone in a highly tissue-specific manner.
S. Izumo (1986)
Coordinate changes in the expression of troponin subunit and myosin heavy-chain isoforms during fast-to-slow transition of low-frequency-stimulated rabbit muscle.
T. Leeuw (1993)
Incorporation of nascent myosin heavy chains into thick filaments of cardiac myocytes in thyroid-treated rabbits
M. Wenderoth (1987)
Expression of myosin heavy chain isoforms in stimulated fast and slow rat muscles
S. Ausoni (1990)
Clon ing and characterisation of an IGF-1 isoform expressed in skeletal muscle
S Yang (1996)
Myosin heavy chain isoforms of human muscle after short-term spaceflight.
M. Y. Zhou (1995)
The myoD gene family: nodal point during specification of the muscle cell lineage.
H. Weintraub (1991)
Fiber transformation and fiber replacement in chronically stimulated muscle.
D. Pette (1992)
Biochemical transformation of canine skeletal muscle for use in cardiac-assist devices.
C. D. Ianuzzo (1990)
Ultrastructural distribution of myosin heavy chain mRNA in cardiac tissue: a comparison of frozen and LR White embedment.
M. Wenderoth (1991)
Skeletal muscle adaptations to endurance training in 60- to 70-yr-old men and women.
A. Coggan (1992)
Changes in myosin heavy chain isoform expression of overloaded rat skeletal muscles.
T. Sugiura (1993)
Human cardiac myosin heavy chain genes and their linkage in the genome
L. Saez (1987)
Skeletal muscle myosin heavy chain composition and resistance training.
G. Adams (1993)
Effects of endurance exercise on isomyosin patterns in fast- and slow-twitch skeletal muscles.
D. Fitzsimons (1990)
comere disruption and myosin isoform expression in the diaphragm of COPD patients
M Orozco-Levi
Spatial distribution of myosin mRNA in cardiac tissue by in situ hybridization techniques
D Dix (1988)
Myosin heavy chain isoforms and velocity of shortening of type 2 skeletal muscle fibres.
S. Schiaffino (1988)
Spatial distribution of myosin mRNA in cardiac tissue by in situ hybridization techniques Biology of isolated adult cardiac myocites
D Dix (1988)
Age dependence of myosin heavy chain transitions induced by creatine depletion in rat skeletal muscle.
G. Adams (1995)
Myofibrillar ATPase activity during isometric contraction and isomyosin composition in rat single skinned muscle fibres.
R. Bottinelli (1994)
In situ hybridization and immunocytochemistry in serial sections of rabbit skeletal muscle to detect myosin expression.
D. Dix (1988)
Interaction of compensatory overload and hindlimb suspension on myosin isoform expression.
R. Tsika (1987)
Force‐velocity relations and myosin heavy chain isoform compositions of skinned fibres from rat skeletal muscle.
R. Bottinelli (1991)
Interactions between motoneurones and muscles in respect of the characteristic speeds of their responses
A. Buller (1960)
The effects of denervation on contractile properties or rat skeletal muscle.
H. Finol (1981)
Muscle Fiber Types Expressing Different Myosin Heavy Chain Isoforms. Their Functional Properties and Adaptive Capacity
S. Schiaffino (1990)
Cloning and characterisation of an IGF-1 isoform expressed in skeletal muscle
S Yang (1996)
Myosin isoenzyme transitions in muscle development, maturation, and disease.
E. Bandman (1985)
Myosin heavy chain mRNA expression in the canine diaphragm pre- and postinspiratory resistive breathing
J Gea (1997)
Diaphragm muscle fiber injury after inspiratory resistive breathing.
E. Zhu (1997)
Contractile and biochemical properties of rat soleus and plantaris after hindlimb suspension.
G. Diffee (1991)
Three myosin heavy-chain isozymes appear sequentially in rat muscle development
R. Whalen (1981)
Myosin isoforms in mammalian skeletal muscle.
S. Schiaffino (1994)
Type 2X-myosin heavy chain is coded by a muscle fiber type-specific and developmentally regulated gene
C. Denardi (1993)
Sensitive detection of myosin heavy chain composition in skeletal muscle under different loading conditions.
S. Fauteck (1995)
Myosin heavy chain phenotype in regenerating skeletal muscle is affected by thyroid hormone.
S. Devor (1995)
Skeletal muscle fiber types, physical activity in women and men: a follow-up from age 16 to 27
B. Glenmark (1994)
ATPase Activity of Myosin Correlated with Speed of Muscle Shortening
M. Bárány (1967)
Interaction of nerve activity and skeletal muscle mechanical activity in regulating isomyosin expression
KM Baldwin (1989)
Effects of lengthened immobilization on functional and histochemical properties of rabbit tibialis anterioris anterior muscle
MC Pattullo (1992)
Biochemical Aspects of Physical Exercise
G. Benzi (1986)
Morphological changes during fiber type transitions in low-frequency-stimulated rat fast-twitch muscle
M. Delp (2004)
Respiratory muscle fatigue resistance relates to myosin phenotype and SDH activity during development.
J. Watchko (1993)
Canine diaphragm muscle after 1 yr of continuous electrical stimulation: its potential as a myocardial substitute.
M. Acker (1987)
Exercise-induced ultrastructural changes in skeletal muscle.
H. Hoppeler (1986)
Fast-to-slow transition in myosin heavy chain expression of rabbit muscle fibres induced by chronic low-frequency stimulation.
S. Aigner (1992)
Muscle fiber types identified by monoclonal antibodies to myosin heavy chains
S. Schiaffino (1986)
Three slow myosin heavy chains sequentially expressed in developing mammalian muscle
SM Hughes (1993)
Identification of a novel type 2 fiber population in mammalian skeletal muscle by combined use of MyHC-I MyHC-II FEV1 93% pred FEV1
L. Gorza (1990)
Mechanical properties of skinned single fibers of identified types from rat diaphragm.
T. Eddinger (1987)
Development, innervation, and activity-pattern induced changes in skeletal muscle.
F. Jólesz (1981)
Cardiac alpha- and beta-myosin heavy chain genes are organized in tandem.
V. Mahdavi (1984)
Exercise and training during graded leg ischaemia in healthy man with special reference to effects on skeletal muscle.
C. Sundberg (1994)
Histochemical and biochemical characteristics of the transient hypertrophy of the denervated rat hemidiaphragm
D. Hopkins (1983)
Diaphragm muscle fiber injury following inspiratory resistive breathing
E Zhu (1997)
Five myosin heavy chain genes are organized as a multigene complex in the human genome
N Soussi-Yanicostas (1993)
Postnatal expression of myosin isoforms in an expiratory muscle--external abdominal oblique.
J. Watchko (1992)
Skeletal muscle myosin light chains are essential for physiological speeds of shortening
S. Lowey (1993)
Significance of impulse activity in the transformation of skeletal muscle type
S. Salmons (1976)
Adaptive changes concerning the type of fibres and isoforms of myosin in the external intercostal muscle of COPD patients
J Gea (1996)
The Dynamic State of Muscle Fibers
D. Pette (1991)
Cellular and molecular diversities of mammalian skeletal muscle fibers.
D. Pette (1990)
Effects of lengthened immobilization on functional and histochemical properties of rabbit tibialis anterior muscle
M. Pattullo (1992)
Myosin heavy chain isoforms in single fibres from m. vastus lateralis of sprinters: influence of training.
J. L. Andersen (1994)
Altered gene expression in fast-twitch muscle induced by chronic low-frequency stimulation.
D. Pette (1992)
Gene expression in skeletal muscle in response to stretch and force generation.
G. Goldspink (1992)
Changes in myosin heavy chain isoforms during chronic low-frequency stimulation of rat fast hindlimb muscles. A single-fiber study.
A. Termin (1989)
Activity-induced regulation of myosin isoform distribution: comparison of two contractile activity programs.
G. Diffee (1993)
Ultrastructural analysis of left ventricular hypertrophy in rabbits.
M. Goldstein (1974)
The relation between intrinsic speed of shortening and duration of the active state of muscle.
R. Close (1965)
Reciprocal changes in myosin isoform expression in rabbit fast skeletal muscle resulting from the application and removal of chronic electrical stimulation.
C. Brownson (1992)
Effects of denervation on the distribution of myosin isozymes in skeletal muscle fibers
G. F. Gauthier (1982)
Mechanics and energetics of animal locomotion
R. M. Alexander (1977)
An agerelated type IIb to IIx myosin heavy chain switching in rat skeletal muscle
L Larsson (1993)
Leinwand histochemical myosin ATPase and antimyosin monoclonal antibodies
V Smerdu (1990)
Changes in myosin heavy chain expression of overload rat skeletal muscles
T Sugiura (1993)
Myosin Heavy Chain Gene Expression in Bovine Fetuses and Neonates Representing Genotypes with Contrasting Patterns of Growth
M. T. Gore (1995)
Cotranslational assembly of myosin heavy chain in developing cultured skeletal muscle.
W. Isaacs (1987)
Models of disuse: a comparison of hindlimb suspension and immobilization.
R. Fitts (1986)
Multigene family for sarcomeric myosin heavy chain in mouse and human DNA: localization on a single chromosome.
L. Leinwand (1983)
Chemical energetics of slow- and fast-twitch muscles of the mouse
M. Crow (1982)
Five skeletal myosin heavy chain genes are organized as a multigene complex in the human genome.
N. Soussi-Yanicostas (1993)
Adaptations of diaphragm and medial gastrocnemius muscles to inactivity.
W. Z. Zhan (1992)
Distribution of myosin heavy chain mRNA in normal and hyperthyroid heart.
B. Eisenberg (1991)
Sarcomere disruption and myosin isoform expression in the diaphragm of COPD patients
M Orozco-Levi (1966)
Do type IIb fibres of human muscle correspond to IIx/d or to IIb of rats
Sant'Ana Pereira JAA (1994)
Control of myosin heavy chain expression: interaction of hypothyroidism and hindlimb suspension.
G. Diffee (1991)

This paper is referenced by
Actualización en los mecanismos de disfunción muscular en la EPOC
J. Gea (2008)
Redox remodelling in diaphragm muscle adaptation to chronic sustained hypoxia
Philip Lewis (2014)
Activación de células satélite en el músculo intercostal de pacientes con EPOC
J. Guiral (2008)
Respiratory Disorders Chronic Obstructive Pulmonary Disease
J. Gea (2010)
Muscle Dysfunction in COPD Metabolic derangements in COPD muscle dysfunction
Luis Puente-Maestu (2013)
Muscle plasticity: Response to training and detraining
A. Bruton (2002)
Estructura básica de los músculos respiratorios y periféricos en el perro beagle
J. B. Gáldiz (2002)
Dual influence of disease and increased load on diaphragm muscle in heart failure.
E. De Sousa (2001)
Adherent Primary Cultures of Mouse Intercostal Muscle Fibers for Isolated Fiber Studies
P. Robison (2011)
diaphragm: coexpression patterns and effect of COPD Developmental myosin heavy chains in the adult human
Sanford Levine (2013)
[Analysis of respiratory muscle structure and tumor necrosis and insulin-like growth factor expression in chronic obstructive pulmonary disease: are samples valid if obtained during thoracotomy performed because of localized pulmonary neoplasia?].
C. Casadevall (2004)
Morfometría fibrilar del músculo intercostal externo. Comparación entre los lados dominante y no dominante en pacientes con EPOC severa
María Ángeles Jiménez-Fuentes (1998)
Skeletal Muscle Adaptations to Disease States
J. Gea (2006)
Skeletal muscle dysfunction in chronic obstructive pulmonary disease and chronic heart failure: underlying mechanisms and therapy perspectives.
H. Gosker (2000)
Activación de células satélite en el músculo intercostal de pacientes con EPOC
J. Martinez-Llorens (2008)
Ventilation and respiratory mechanics.
A. W. Sheel (2012)
Structure and function of the respiratory muscles in patients with COPD: impairment or adaptation?
M. Orozco-Levi (2003)
Actividad metabólica del músculo intercostal externo en pacientes con EPOC
M. Pastó (2001)
Mitochondrial electron transport chain function is enhanced in inspiratory muscles of patients with chronic obstructive pulmonary disease.
F. Ribera (2003)
Metabolic derangements in COPD muscle dysfunction.
Luis Puente-Maestú (2013)
Homogeneidad celular en las diversas porciones del diafragma
María Ángeles Jiménez-Fuentes (1998)
The respiratory muscles: cellular and molecular physiology.
M. Decramer (1997)
[Activation of satellite cells in the intercostal muscles of patients with chronic obstructive pulmonary disease].
J. Martinez-Llorens (2008)
chronic obstructive pulmonary disease Parasternal intercostal muscle remodeling in severe
Joseph B. Shrager (2015)
Developmental myosin heavy chains in the adult human diaphragm: coexpression patterns and effect of COPD.
T. Nguyen (2000)
Parasternal intercostal muscle remodeling in severe chronic obstructive pulmonary disease.
S. Levine (2006)
Molecular and physiological events in respiratory muscles and blood of rats exposed to inspiratory threshold loading.
M. Domínguez-Álvarez (2014)
Procion orange tracer dye technique vs. identification of intrafibrillar fibronectin in the assessment of sarcolemmal damage
J. Palacio (2002)
[Basic structure of respiratory and peripheral muscles in the beagle dog].
J. B. Gáldiz (2002)
Muscle dysfunction in chronic obstructive pulmonary disease: update on causes and biological findings.
J. Gea (2015)
The uniqueness of speech among motor systems
Raymond D. Kent (2004)
Análisis estructural y expresión de los factores de necrosis tumoral y crecimiento insulina-like en los músculos respiratorios de pacientes con EPOC. ¿Son válidas las muestras obtenidas en el curso de una toracotomía por neoplasia pulmonar localizada?
C. Casadevall (2004)
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