Developmental and hormonal regulation of sarcomeric myosin heavy chain gene family.

Mahdavi, Vijak; Izumo, Seigo; Nadal-Ginard, B

doi:10.1161/01.res.60.6.804

Cited by 182 publications

(77 citation statements)

References 55 publications

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“…Expression of the fast phenotype is, however, co-regulated by thyroid hormone (671,674). For example, the postnatal expression of SERCA1a is completely dependent on thyroid hormone (675,676) and the transition from fetal to adult fast MHC isoforms is delayed in hypothyroidism (677)(678)(679). In the adult animal this responsiveness of fast muscles is greatly diminished, in contrast to slow muscles, which are highly sensitive to changes in the thyroid status.…”

Section: [J4] Skeletal Musclementioning

confidence: 99%

American Thyroid Association Guide to Investigating Thyroid Hormone Economy and Action in Rodent and Cell Models

Bianco

Anderson

Forrest

et al. 2014

Thyroid

175

106

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Section: [J4] Skeletal Musclementioning

confidence: 99%

American Thyroid Association Guide to Investigating Thyroid Hormone Economy and Action in Rodent and Cell Models

Bianco

Anderson

Forrest

et al. 2014

Thyroid

175

106

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“…Several MHC isoforms have been identified in mouse striated muscle, and their expression is restricted to a subset of muscle fibers. For example, slow-twitch type I fibers express slow MHC I (␤-cardiac myosin; Mahdavi et al, 1987;Saez and Leinwand, 1986) and the ATPase of MHC I is low compared with that of MHC isoforms expressed in fast-twitch fibers (reviewed in Schiaffino and Reggiani, 1996). Adult fast type II fibers express either MHC-2a, MHC-2b, or MHC-2x, which are associated with IIA, IIB, and IIX fibers, respectively, although individual fibers can express more than one MHC isoform (Staron and Pette, 1993).…”

Section: Introductionmentioning

confidence: 99%

Novel murine clonal cell lines either express slow or mixed (fast and slow) muscle markers following differentiation in vitro

Peltzer

Colman

Cebrián

et al. 2008

Developmental Dynamics

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We have investigated whether the phenotype of myogenic clones derived from satellite cells of different muscles from the transgenic immortomouse depended on muscle type origin. Clones derived from neonatal, or 6-to 12-week-old fast and slow muscles, were analyzed for myosin and enolase isoforms as phenotypic markers. All clones derived from slow-oxidative muscles differentiated into myotubes with a preferentially slow contractile phenotype, whereas some clones derived from rapid-glycolytic or neonatal muscles expressed both fast and slow myosin isoforms. Thus, muscle origin appears to bias myosin isoform expression in myotubes. The neonatal clone (WTt) was cultivated in various medium and substrate conditions, allowing us to determine optimized conditions for their differentiation. Matrigel allowed expressions of adult myosin isoforms, and an isozymic switch from embryonic ␣-toward muscle-specific ␤-enolase, never previously observed in vitro. These cells will be a useful model for in vitro studies of muscle fiber maturation and plasticity.

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“…The functional heterogeneity of muscles can be explained by their MyHC isoform content (Botinelli, 2001). MyHC is encoded by a multigene family, the members of which are expressed in a tissue-specific and developmentally regulated manner (Wydro et al, 1983;Mahdavi et al, 1987). Several MyHC isoforms have been described in skeletal muscles, including two developmental isoforms (embryonic and neonatal/ perinatal/fetal), one slow isoform (MyHC I/ß) and three fast isoforms (MyHC IIA, IIX/IID and IIB) (Staron et al, 1993;Pette and Staron, 2000).…”

Section: Introductionmentioning

confidence: 99%

Myosin heavy chain isoforms in postnatal muscle development of mice

Agbulut¹,

Noirez²,

Beaumont³

et al. 2003

Biology of the Cell

230

220

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In this study, using a high-resolution gel electrophoresis technique, we have characterized the myosin heavy chain composition in different skeletal muscle of the mouse during postnatal development. The pattern of myosin heavy chain expression was studied in four hind limb muscles, the diaphragm, the tongue and the masseter. All of these muscles displayed the usual sequential transitions from embryonic to neonatal and to adult myosin heavy chain isoforms but more interestingly these transitions occur with a distinct chronology in the different muscles. In addition, our results demonstrated a transitory pattern of expression for certain adult myosin heavy chain isoforms in the soleus and the tongue. In the soleus muscle IIB and in the tongue IIA myosin heavy chain isoforms were detected only for a short time during postnatal life. Our results demonstrate that muscles of the mouse with different functions are subjected to a distinct programs of myosin isoform transitions during postnatal muscle development. This study describes new data which will help us to understand both postnatal muscle development in transgenic mouse muscles as well as in muscle pathology.

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Developmental and hormonal regulation of sarcomeric myosin heavy chain gene family.

Cited by 182 publications

References 55 publications

American Thyroid Association Guide to Investigating Thyroid Hormone Economy and Action in Rodent and Cell Models

American Thyroid Association Guide to Investigating Thyroid Hormone Economy and Action in Rodent and Cell Models

Novel murine clonal cell lines either express slow or mixed (fast and slow) muscle markers following differentiation in vitro

Myosin heavy chain isoforms in postnatal muscle development of mice

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