← Back to Search
Three Myosin Heavy-chain Isozymes Appear Sequentially In Rat Muscle Development
R. Whalen, S. Sell, G. Butler-Browne, K. Schwartz, P. Bouveret, I. Pinset-Härström
Published 1981 · Chemistry, Medicine
Download PDFAnalyze on Scholarcy
Three different heavy-chain isozymes of myosin appear sequentially in rat muscle during the period from late gestation to about three weeks of age. In part these changes can be related to changes in innervation taking place during this period.
This paper references
The immunological specificity of myosins from cross-striated muscles as revealed by quantitative microcomplement fixation and enzyme inhibition by antisera.
S. Bruggmann (1975)
Plasticity of Muscle: Edited by Dirk Pette. pp 625. Walter de Gruyter, Berlin. 1980. DM160 ISBN 3-11-007961-5
John Illingorth (1981)
Homology between the primary structure of α-fetoprotein, deduced from a complete cDNA sequence, and serum albumin
S. W. Law (1981)
Dynamic properties of fast and slow skeletal muscles of the rat during development
R. Close (1964)
ELECTRON MICROSCOPE STUDIES ON THE STRUCTURE OF NATURAL AND SYNTHETIC PROTEIN FILAMENTS FROM STRIATED MUSCLE.
H. Huxley (1963)
The detection of DNA-binding proteins by protein blotting
B. Bowen (1980)
Distribution of light chains in fast skeletal myosin
S. Lowey (1979)
Differences among myosins synthesized in non-myogenic cells, presumptive myoblasts, and myoblasts.
J. C. Chi (1975)
Identification of a novel form of myosin light chain present in embryonic muscle tissue and cultured muscle cells.
R. Whalen (1978)
Electrophoretic analysis of multiple forms of myosin in fast-twitch and slow-twitch muscles of the chick.
J. F. Hoh (1976)
Structural and functional changes of myosin during development: comparison with adult fast, slow and cardiac myosin.
F. Sréter (1975)
Purification and structural analysis of myosins from brain and other non-muscle tissues.
K. Burridge (1975)
Developmental changes of the primary structure and histidine methylation in rabbit skeletal muscle myosin.
G. Huszár (1972)
Effect of adenosine triphosphate, inorganic phosphate and divalent cations on the size and structure of synthetic myosin filaments. An electron microscope study.
I. Pinset-Härström (1979)
Polyneuronal innervation of skeletal muscle in new‐born rats and its elimination during maturation.
M. C. Brown (1976)
Recent developments in the molecular genetics of human hemoglobin
D. Weatherall (1979)
Nonmuscle contractile proteins: the role of actin and myosin in cell motility and shape determination.
M. Clarke (1977)
Fast and slow myosin in developing muscle fibres
G. Gauthier (1978)
Myosin types during the development of embryonic chicken fast and slow muscles.
N. Rubinstein (1977)
Differentiation of myosin in chick embryos.
T. Masaki (1974)
Myosin types in cultured muscle cells
M. Cantini (1980)
Development of a mammalian fast muscle: dynamic and biochemical properties correlated
D. B. Drachman (1973)
Myofibrillar proteins of developing and dystrophic skeletal muscle
H. John (1976)
Contractile protein isozymes in muscle development: identification of an embryonic form of myosin heavy chain.
R. Whalen (1979)
Immunochemical evidence for structural homologies between mammalian cardiac and skeletal myosins
K. Schwartz (1978)
The adaptive response of skeletal muscle to increased use
S. Salmons (1981)
Why are fetal muscles slow?
A. Kelly (1980)
Myogenic and neurogenic contributions to the development of fast and slow twitch muscles in rat.
N. Rubinstein (1978)
An electrophoretic study of native myosin isozymes and of their subunit content.
A. D'albis (1979)
Assembly of immunoglobulin heavy chain genes
H. Molgaard (1980)
Regulation of non-muscle myosin assembly by calmodulin-dependent light chain kinase
J. Scholey (1980)
CONTRACTILE PROTEIN ISOZYMES IN MUSCLE DEVELOPMENT: THE EMBRYONIC PHENOTYPE
R. Whalen (1980)
Detection of antibodies specific to sodium dodecyl sulfate-treated proteins.
A. Lompre (1979)
Light chain phosphorylation alters the conformation of skeletal muscle myosin.
C. J. Ritz-Gold (1980)
Effect of ageing of myosin on its ability to form synthetic filaments and on proteolysis of the LC2 light chain.
I. Pinset-Härström (1979)
Comparison of adult, embryonic, and dystrophic myosin heavy chains from chicken muscle by sodium dodecyl sulfate/polyacrylamide gel electrophoresis and peptide mapping.
J. I. Rushbrook (1979)
Identification of the essential light chains of myosin.
J. Dow (1971)
Immunochemical evidence for the species-specificity of mammalian cardiac myosin and heavy meromyosin.
K. Schwartz (1977)
Fast and slow muscles in tissue culture synthesise only fast myosin
N. Rubinstein (1979)
Comparative structural analysis of myosin after limited tryptic hydrolysis by use of two-dimensional gel electrophoresis.
A. Brevet (1978)
Differentiation of fast and slow muscles in the cat hind limb
A. Buller (1960)
Myosin from fetal hearts contains the skeletal muscle embryonic light chain
R. Whalen (1980)
Use of antibodies against dodecylsulfate-denatured heavy meromyosins to probe structural differences between muscular myosin isoenzymes.
K. Schwartz (1980)
Transitions in contractile protein isozymes during muscle cell differentiation.
R. Whalen (1979)
Studies on the chymotryptic digestion of myosin. Effects of divalent cations on proteolytic susceptibility.
A. Weeds (1977)
Myoblast myosin phosphorylation is a prerequisite for actin-activation
STYLIANOS P. Scordilis (1977)
The limited tryptic cleavage of chymotryptic S-1: an approach to the characterization of the actin site in myosin heads.
D. Mornet (1979)
Rabbit skeletal myosin isoenzymes from fetal, fast-twitch and slow-twitch muscles
J. Hoh (1979)
This paper is referenced by
Parvalbumin, a Neuronal Protein in Brain Cell Cultures
G. Pfyffer (1984)
Selective synthesis and degradation of slow skeletal myosin heavy chains in developing muscle fibers
G. Dhoot (1986)
Myosin types and fiber types in cardiac muscle. III. Nodal conduction tissue
L. Gorza (1986)
Pink lateral muscle in the carp (Cyprinus carpio L.): histochemical properties and myosin composition
P. Scapolo (2005)
Polymorphism of myosin isoenzymes and myosin heavy chains in histochemically typed skeletal muscles of the roach (Rutilus rutilus L., Cyprinidae, fish)
J. Karasinski (1989)
Two distinct nonmuscle myosin-heavy-chain mRNAs are differentially expressed in various chicken tissues. Identification of a novel gene family of vertebrate non-sarcomeric myosin heavy chains.
Y. Katsuragawa (1989)
Cardiac troponin T in developing, regenerating and denervated rat skeletal muscle.
Leopoldo Saggin (1990)
Developmentally regulated expression of three slow isoforms of myosin heavy chain: diversity among the first fibers to form in avian muscle.
S. Page (1992)
Muscle growth and myosin isoform transitions during development of a small teleost fish, Poecilia reticulata (Peters) (Atheriniformes, Poeciliidae): a histochemical, immunohistochemical, ultrastructural and morphometric study
A. Veggetti (2004)
The larval development of lateral musculature in gilthead sea bream Sparus aurata and sea bass Dicentrarchus labrax
G. Ramírez-Zarzosa (2004)
Myosin heavy chain gene expression changes in the diaphragm of patients with chronic lung hyperinflation.
J. Mercadier (1998)
Effects of controllable stress on masticatory behaviour and muscle structure: partial protective effect of clomipramine.
N. Hartmann (1999)
Effect of muscle origin and phenotype on satellite cell muscle-specific gene expression.
W. LaFramboise (2003)
RT-PCRof myosin heavy chain mRNA expression by
Fadia Haddad (2015)
Identification and pattern of transitions of some developmental and adult isoforms of fast troponin T in some human and rat skeletal muscles
M. Sabry (2005)
Embryonic myosin heavy chain as a differentiation marker of developing human skeletal muscle and rhabdomyosarcoma. A monoclonal antibody study.
S. Schiaffino (1986)
Myosin transitions in chronic stimulation do not involve embryonic isozymes
R. Hoffman (1985)
Myosin isoforms in normal and dystrophic chickens.
J. I. Rushbrook (1987)
Identification and developmental expression of a novel embryonic myosin heavy-chain gene in chicken.
A. A. Lagrutta (1989)
Relationship of primary and secondary myogenesis to fiber type development in embryonic chick muscle.
B. Fredette (1991)
Embryonic and fetal rat myoblasts express different phenotypes following differentiation in vitro.
C. Pin (1993)
Fibre type differentiation during postnatal development of miniature pig skeletal muscles.
V. Horák (1995)
Expression of myosin heavy chain isoforms and myogenesis of intrafusal fibres in rat muscle spindles
T. Soukup (1995)
Postnatal development and plasticity of specialized muscle fiber characteristics in the hindlimb.
D. Garry (1996)
Evidence for differential post-translational modifications of slow myosin heavy chain during murine skeletal muscle development
A. Maggs (2004)
Molecular and cellular mechanisms involved in the generation of fiber diversity during myogenesis.
P. Wigmore (2002)
Single nucleotide polymorphisms, haplotypes and combined genotypes in MYH3 gene and their associations with growth and carcass traits in Qinchuan cattle
L. Wang (2012)
Calcium transients in developing mouse skeletal muscle fibres
Joana Capote (2005)
The role of titin and nebulin in myofibril assembly in cultured embryonic chick muscle cells
M. Kurpakus (1988)
Organization of Muscle-Specific Genes in the Rodent Genome
H. Czosnek (1983)
Quantitation of myosin in muscle.
A. Everett (1983)
Regenerating adult chicken skeletal muscle and satellite cell cultures express embryonic patterns of myosin and tropomyosin isoforms.
R. Matsuda (1983)See more