← Back to Search
Emergence Of The Mature Myosin Phenotype In The Rat Diaphragm Muscle.
W. LaFramboise, M. Daood, R. D. Guthrie, S. Schiaffino, P. Moretti, B. Brozanski, M. Ontell, G. Butler-Browne, R. Whalen, M. Ontell
Published 1991 · Biology, Medicine
Download PDFAnalyze on Scholarcy
Immunohistochemical analysis of myosin heavy chain (MHC) isoform expression in perinatal and adult rat diaphragm muscles was performed with antibodies which permitted the identification of all known MHC isoforms found in typical rat muscles. Isoform switching, leading to the emergence of the adult phenotype, was more complex than had been previously described. As many as four isoforms could be coexpressed in a single myofiber. Elimination of developmental isoforms did not usually result in the myofiber immediately achieving its adult phenotype. Activation of genes for specific adult isoforms might be delayed to puberty. For example, two of the three fast MHCs, MHC2X and MHC2A appeared perinatally, while MHC2B did not appear until 30 days postnatal. By Day 60 this isoform was present in approximately 27% of the myofibers, but in most myofibers expression of this isoform was transient (i.e., at Day greater than or equal to 115, less than 4% of the myofibers expressed MHC2B). Fibers which contained MHC beta/slow during the late fetal and early neonatal period coexpressed MHCemb. A marked increase in the frequency of fibers containing MHC beta/slow occurred between 4 and 21 days postnatal. These slow fibers arose from a population of myofibers which expressed MHCemb and MHCneo during their development, and they accounted for the majority of slow fibers found in the adult diaphragm. The adult myosin phenotype of the diaphragm myofibers (as determined with immunocytochemistry, and 5% SDS-PAGE) was not achieved until the rat was greater than or equal to 115 days old.
This paper references
Myosin isozyme transitions occurring during the postnatal development of the rat soleus muscle.
G. Butler-Browne (1984)
Effects of hypothyroidism on myosin isozyme transitions in developing rat muscle
G. Butler-Browne (1984)
Identification of a novel form of myosin light chain present in embryonic muscle tissue and cultured muscle cells.
R. Whalen (1978)
Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.
H. Towbin (1979)
Testosterone-induced changes in contractile protein isoforms in the sexually dimorphic temporalis muscle of the guinea pig.
G. Lyons (1986)
Developmental aspects of diaphragm muscle cells : structural and functional organization
G. Sieck (1991)
Quantitation of proteins on Coomassie blue-stained polyacrylamide gels based on spectrophotometric determination of electroeluted dye.
J. Malloy (1984)
Histochemical and physiological characteristics of the rat diaphragm.
J. Metzger (1985)
Oxidative potential in developing rat diaphragm, EDL, and soleus muscle fibers.
D. Smith (1988)
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)
Thyroid hormone induces a nerve-independent precocious expression of fast myosin heavy chain mRNA in rat hindlimb skeletal muscle.
S. D. Russell (1988)
A comparison of eight different chromogen protocols for the demonstration of immunoreactive neurofilaments or glial filaments in rat cerebellum using the peroxidase-antiperoxidase method and monoclonal antibodies.
J. Trojanowski (1983)
Morphometric analysis of the developing mouse soleus muscle.
M. Ontell (1988)
Mechanisms of precocious puberty induced in male rats by pituitary grafts.
R. Aguilar (1988)
Neuromuscular transmission in new‐born rats
P. A. Redfern (1970)
Transition of myosin isozymes during development of human masseter muscle. Persistence of developmental isoforms during postnatal stage.
N. Soussi-Yanicostas (1990)
Comparison of myosins from the masseter muscle of adult rat, mouse and guinea-pig. Persistence of neonatal-type isoforms in the murine muscle.
A. D'albis (1986)
High resolution two-dimensional electrophoresis of proteins.
P. O'Farrell (1975)
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
U. Laemmli (1970)
Hormonal control of myosin heavy chain genes during development of skeletal muscles.
N. Rubinstein (1988)
Myosin transitions in developing fast and slow muscles of the rat hindlimb.
G. Lyons (1983)
Cellular and molecular biology of muscle development : Edited by L.H. Kedes and F.E. Stockdale; Alan R. Liss; New York, 1989; xxxv + 1059 pages, $195.00
R. M. Simmons (1990)
Muscle Fiber Types Expressing Different Myosin Heavy Chain Isoforms. Their Functional Properties and Adaptive Capacity
S. Schiaffino (1990)
Three myosin heavy-chain isozymes appear sequentially in rat muscle development
R. Whalen (1981)
Co-expression of multiple myosin heavy chain genes, in addition to a tissue-specific one, in extraocular musculature
D. Wieczorek (1985)
Myosin heavy chain composition of single fibres from normal human muscle.
D. Biral (1988)
Three fast myosin heavy chains in adult rat skeletal muscle
A. Baer (1988)
Developmental and hormonal regulation of sarcomeric myosin heavy chain gene family.
V. Mahdavi (1987)
Actin and myosin multigene families: their expression during the formation of skeletal muscle.
Buckingham Me (1985)
Type 1, 2A, and 2B myosin heavy chain electrophoretic analysis of rat muscle fibers.
D. Danieli Betto (1986)
Slow myosin in developing rat skeletal muscle
M. Narusawa (1987)
Organogenesis of the mouse extensor digitorum logus muscle: a quantitative study.
M. Ontell (1984)
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)
Thyroidal and neural control of myosin transitions during development of rat fast and slow muscles
B. Gambke (1983)
A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels.
B. Oakley (1980)
Electrophoretic separation and immunological identification of type 2X myosin heavy chain in rat skeletal muscle.
W. LaFramboise (1990)
Altered developmental changes of neuromuscular junction in hypo‐ and hyperthyroid rats
K. Kawa (1982)
This paper is referenced by
Skeletal muscle glucose transporter protein responses to antenatal glucocorticoids in the ovine fetus.
S. Gray (2006)
functiondeficiency impairs mouse diaphragm isotonic Combined myofibrillar and mitochondrial creatine
Alan P. Koretsky (2015)
Myosin heavy chain expression in respiratory muscles of the rat.
W. LaFramboise (1992)
Composition of newly forming motor units in prenatal rat intercostal muscle
P. Sheard (1996)
Characterization of the myosin heavy chains of avian adult fast muscles at the protein and mRNA levels
J. I. Rushbrook (2004)
myosin heavy chain colocalization muscle: force, shortening velocity, and patterns of A continuum of myofibers in adult rabbit extraocular
LaDora V Thompson (2015)
and Die during the Neonatal Period Mice Lacking Skeletal Muscle Actin Show Reduced Muscle Strength and Growth Deficits
J. Joya (2008)
Plasticity in Skeletal , Cardiac , and Smooth Muscle Invited Review : Plasticity and energetic demands of contraction in skeletal and cardiac muscle
G. Sieck (2001)
Pulse electrophoresis of muscle myosin heavy chains in sodium dodecyl sulfate-polyacrylamide gels.
J. A. Sant'Ana Pereira (2001)
Clenbuterol-induced fiber type transition in the soleus of adult rats
D. Criswell (2006)
Transient expression of a slow-tonic MHC isoform by extrafusal fibers in the developing rat
J. Kučera (2004)
Multiple mechanisms regulate muscle fiber diversity
P. Gunning (1991)
Acetylcholine receptor formation in mouse-chick chimera.
G. Auda-Boucher (1997)
The mATPase histochemical profile of rat type IIX fibres: correlation with myosin heavy chain immunolabelling
José A. A. Sant'Ana Pereira (2004)
Skeletal muscle fibre types: detection methods and embryonic determinants.
M. Zhang (1998)
Antenatal and postnatal influences on preterm diaphragm function
Christine Astell (2018)
DISTRIBUTION OF MYOSIN ISOFORMS IN SKELETAL MUSCLE
M. Wada (1995)
Contractile protein gene expression in primary myotubes of embryonic mouse hindlimb muscles.
M. Ontell (1993)
Diaphragm myosin heavy chain composition shifts in aging chronically-undernourished Fischer 344 male rats
B. Ameredes (1998)
PROTEIN SYNTHESIS AND MYOSIN HEAVY CHAIN mRNA IN THE RAT DIAPHRAGM DURING MECHANICAL VENTILATION
R. Shanely (2002)
Rat diaphragm during postnatal development. I. Changes in distribution of muscle fibre type and in oxidative potential.
M. Fratacci (1996)
Myofibrillar proteins in developing white muscle of the Arctic charr, Salvelinus alpinus (L.)
I. Martinez (1994)
Reappearance of the minor α-sarcomeric actins in postnatal muscle.
T. Collins (1997)
Effect of chronic denervation and denervation-reinnervation on cytoplasmic creatine kinase transcript accumulation.
C. Washabaugh (2001)
Myosin isoforms and muscle fiber characteristics in equine gluteus medius muscle
A. Serrano (1996)
Chapter 83 – Functional Development of Respiratory Muscles
G. Sieck (2004)
Mechanisms underlying myosin heavy chain expression during development of the rat diaphragm muscle.
P. Geiger (2006)
The histochemical profiles of Histology and Histopathology
F. Gil ()
Phenotype of adult mouse muscle myoblasts reflects their fiber type of origin.
J. D. Rosenblatt (1996)
Myosin isoform switching during assembly of the Drosophila flight muscle thick filament lattice
Z. Orfanos (2013)
Nuclear genetic control of mitochondrial translation in skeletal muscle revealed in patients with mitochondrial myopathy.
F. Sasarman (2002)
Myofibrillar or mitochondrial creatine kinase deficiency alone does not impair mouse diaphragm isotonic function.
J. Watchko (2000)See more