Online citations, reference lists, and bibliographies.
← Back to Search

Myosin Heavy Chain Expression In Respiratory Muscles Of The Rat.

W. LaFramboise, J. Watchko, B. Brozanski, M. Daood, R. Guthrie
Published 1992 · Biology, Medicine

Cite This
Download PDF
Analyze on Scholarcy
Myosin heavy chain (MHC) isoforms of hind limb adult rat muscles and muscles with a range of respiratory activities were analyzed by a sodium dodecyl sulfate polyacrylamide gel electrophoresis technique that allowed electrophoretic separation of the three fast and one slow MHC isoform found in typical rat muscle. Costal and crural diaphragm muscle samples expressed a mixture of MHC beta/slow, MHC2A, and MHC2X but little MHC2B. In contrast, MHC2B was the dominant MHC isoform in the genioglossus, intercostal, and three abdominal muscles, all of which exhibited minimal expression of MHC beta/slow. The amount of MHC2X (relative to total MHC composition) was similar in the diaphragm, genioglossus, and transversus abdominis muscles, while considerably less was detected in the rectus abdominis and external oblique muscles. These results indicate that MHC2X is broadly and variably distributed among respiratory muscles. Furthermore, these data suggest that a large portion of 2X fibers (containing MHC2X), which cannot be detected by standard histochemical analysis, may be present in the genioglossus and transversus abdominis muscles as has been demonstrated for the diaphragm muscle. We speculate that an association exists between the level of MHC2X expression and frequency of respiratory recruitment.
This paper references
Physiological types and histochemical profiles in motor units of the cat gastrocnemius
R. Burke (1973)
Myosin isozyme transitions occurring during the postnatal development of the rat soleus muscle.
G. Butler-Browne (1984)
Shortening velocity in single fibers from adult rabbit soleus muscles is correlated with myosin heavy chain composition.
P. Reiser (1985)
Alternative myosin hinge regions are utilized in a tissue-specific fashion that correlates with muscle contraction speed.
V. Collier (1990)
Expression of myosin heavy chain isoforms in stimulated fast and slow rat muscles
S. Ausoni (1990)
A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels.
B. Oakley (1980)
Detection of cholecystokinin in spermatogenic cells.
H. Persson (1988)
Chronic denervation of rat diaphragm: Selective maintenance of adult fast myosin heavy chains
Ugo Carraro (1982)
Changes in skeletal-muscle myosin isoenzymes with hypertrophy and exercise.
P. Gregory (1986)
Myosin heavy chain isoforms and velocity of shortening of type 2 skeletal muscle fibres.
S. Schiaffino (1988)
A sensitive SDS-PAGE method separating myosin heavy chain isoforms of rat skeletal muscles reveals the heterogeneous nature of the embryonic myosin.
U. Carraro (1983)
Muscle Fiber Types Expressing Different Myosin Heavy Chain Isoforms. Their Functional Properties and Adaptive Capacity
S. Schiaffino (1990)
All members of the MHC multigene family respond to thyroid hormone in a highly tissue-specific manner.
S. Izumo (1986)
Evolutionarily conserved sequences of striated muscle myosin heavy chain isoforms. Epitope mapping by cDNA expression.
J. B. Miller (1989)
Electrophoretic separation and immunological identification of type 2X myosin heavy chain in rat skeletal muscle.
W. LaFramboise (1990)
Abdominal muscle use during breathing in the anesthetized dog.
J. Gilmartin (1987)
Inhaled furosemide prevents both the bronchoconstriction and the increase in neutrophil chemotactic activity induced by ultrasonic "fog" of distilled water in asthmatics.
G. Moscato (1991)
Developmental and hormonal regulation of sarcomeric myosin heavy chain gene family.
V. Mahdavi (1987)
Localization of the ATP-binding site in the 23-kDa and 20-kDa regions of the heavy chain of the skeletal muscle myosin head.
S. Maruta (1989)
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
U. Laemmli (1970)
Identification of a novel type 2 fiber population in mammalian skeletal muscle by combined use of histochemical myosin ATPase and anti-myosin monoclonal antibodies.
L. Gorza (1990)
Emergence of the mature myosin phenotype in the rat diaphragm muscle.
W. LaFramboise (1991)
Subunit composition of rodent isomyosins and their distribution in hindlimb skeletal muscles.
R. Tsika (1987)
Dynamic properties of mammalian skeletal muscles.
R. Close (1972)
Type IIB to IIA fiber transformation in intermittently stimulated rabbit muscles.
K. Mabuchi (1982)
Electromyographic activity of intrinsic and extrinsic muscles of the human tongue.
Sauerland Ek (1975)
Type 1, 2A, and 2B myosin heavy chain electrophoretic analysis of rat muscle fibers.
D. Danieli Betto (1986)
Mechanical properties of skinned single fibers of identified types from rat diaphragm.
T. Eddinger (1987)
Molecular genetics of myosin.
C. Emerson (1987)
Modifying preselected sites on proteins: the stretch of residues 633-642 of the myosin heavy chain is part of the actin-binding site.
P. Chaussepied (1988)
Contractile and endurance properties of geniohyoid and diaphragm muscles.
E. van Lunteren (1990)
Transversus abdominis muscle function in humans.
A. De Troyer (1990)

This paper is referenced by
Acute and Chronic Effects of Artificial Rearing on Rat Genioglossus Muscle
Moore (2005)
Laryngeal muscle biology in the Pink1-/- rat model of Parkinson disease.
Tiffany J Glass (2019)
Early Adaptations to Training: Upregulation of α-myosin Heavy Chain Gene Expression
Karolina Rafalski (2007)
Myosin heavy chain profiles and body composition are different in old versus young Standardbred mares.
R. Lehnhard (2004)
Two classes of mammalian skeletal muscle fibers distinguished by metabolite content.
M. Kushmerick (1993)
Chronic clenbuterol administration alters myosin heavy chain composition in standardbred mares.
M. Beekley (2003)
Regulation of myosin heavy chain gene expression after short-term diaphragm inactivation.
L. Yang (1998)
Myosin heavy chain gene expression changes in the diaphragm of patients with chronic lung hyperinflation.
J. Mercadier (1998)
Myosin gene expression in the respiratory muscles.
J. Gea (1997)
Differential expression of lipid and carbohydrate metabolism genes in upper airway versus diaphragm muscle.
E. van Lunteren (2010)
Postnatal expression of myosin lsoforms in the genioglossus and diaphragm muscles.
B. Brozanski (1993)
Mammalianskeletal musclefibers distinguished bycontents of phosphocreatine, ATP,andPi
M. J. Kushmerick (1992)
Metabolic profiles of cat and rat pharyngeal and diaphragm muscles.
E. van Lunteren (1996)
Age-related changes in upper airway muscles morphological and oxidative properties
A. Oliven (2001)
Chronic clenbuterol administration alters myosin heavy chain composition in standardbred mares.
M. Beekley (2003)
E-box sites and a proximal regulatory region of the muscle creatine kinase gene differentially regulate expression in diverse skeletal muscles and cardiac muscle of transgenic mice.
M. Shield (1996)
Histochemical properties of upper airway muscles: comparison of dilator and nondilator muscles.
A. Bracher (1997)
Short Term vs Long Term Dexamethasone Treatment: Effects on Rat Diaphragm Structure and Function
D. Prezant (1998)
Regulation of myosin heavy chain gene expression after short-term diaphragm inactivation.
L. Yang (1998)
Regional Distribution of Myosin Heavy Chain Isoforms in Rib Cage Muscles as a Function of Postnatal Development
R. L. Vazquez (1993)
Contractile properties of the tongue's genioglossus muscle and motor units in the rat
T. G. Sutlive (2000)
Synchronization of presynaptic input to motor units of tongue, inspiratory intercostal, and diaphragm muscles.
A. Rice (2011)
Effect of muscle origin and phenotype on satellite cell muscle-specific gene expression.
W. LaFramboise (2003)
Phenotype and contractile properties of mammalian tongue muscles innervated by the hypoglossal nerve
J. C. Smith (2005)
Myosin heavy chain transitions during development. Functional implications for the respiratory musculature.
J. Watchko (1998)
Short- and long-term effects of testosterone on diaphragm in castrated and normal male rats.
D. Prezant (1997)
Respiration-related discharge of hyoglossus muscle motor units in the rat.
G. Powell (2014)
Semantic Scholar Logo Some data provided by SemanticScholar