Slow myosin in developing rat skeletal muscle.

Narusawa, Mitsuo; Fitzsimons, Robin B.; Izumo, Seigo; Nadal-Ginard, B; Rubinstein, Neal A.; Kelly, Alan M.

doi:10.1083/jcb.104.3.447

Cited by 245 publications

(150 citation statements)

References 46 publications

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“…The appearance of slow myosin (followed, in some cases, by its disappearance) did not follow curves parallel to those for intermediate and fast myosins. As previously stated [31], synthesis of slow myosin is an early event in skeletal myogenesis. Here, the level of this isoform increased continuously in the soleus, from about 40% of total myosin a few days after birth to about 80% at one month.…”

Section: Discussionmentioning

confidence: 83%

Specific programs of myosin expression in the postnatal development of rat muscles

d’Albis

Couteaux

Janmot

et al. 1989

European Journal of Biochemistry

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The expression of myosin during postnatal development was studied in a dozen muscles of the rat. All muscles displayed the usual sequential transitions from embryonic to neonatal and to adult isomyosins. However, we observed that these transitions did not take place uniformly. Thus, half-transition times for the appearance of the adult intermediate and fast myosin extended from seven days for diaphragm, the most precocious muscle of all those examined, to 23 days for male rat masseter. Besides the large differences between their half-transition times, we noticed that the transition curves displayed different slopes, covering different periods. Differences between muscles mainly affected the neonatal-to-adult transition rather than the embryonic-to-neonatal transition, since the embryonic-type myosin disappeared from all muscles examined except for one, at about the Same time, by the end of the first week after birth. In addition, the appearance of slow myosin varied for each muscle and did not follow curves parallel to those for intermediate and fast myosins. These results indicate that each muscle of the rat is subjected to a specific program of myosin isoform transitions during postnatal development.

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Section: Discussionmentioning

confidence: 83%

Specific programs of myosin expression in the postnatal development of rat muscles

d’Albis

Couteaux

Janmot

et al. 1989

European Journal of Biochemistry

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“…These muscles differ from each other in their contraction speed, their metabolic properties, and in the type of myosin found in their myofilaments. While diversity among myotubes, at least in terms of MHC composition, is a characteristic of avian muscle from the inception of myotube formation (Miller et al, 19851, the first myotubes that form in rodent muscle (primary myotubes) are homogeneous (Narusawa et al, 1987). Therefore, the heterogeneity of mammalian muscle must develop either by selective "up"-and "down"-regulation of specific myosin genes within a homogeneous myofiber population and/or by the formation of an additional population of myotubes (secondary myotubes), which have a different genetic program.…”

Section: Discussionmentioning

confidence: 99%

“…While rodent myotubes, unlike chicken myotubes (Miller et al, 19851, are initially homogeneous in that they express the same myosin isoforms (Narusawa et al, 1987), diversity in contractile protein gene expression ultimately emerges, with distinctive types of slow and fast myofibers being present in mature muscle (cf. Pette and Staron, 1990).…”

Section: Introductionmentioning

confidence: 99%

“…The time course of contractile protein gene expression in the somites Lyons et al, 1990a) and in the hindlimb muscles (Ontell et al, 1993) of the embryonic mouse (<15 days gestation) has been described with in situ hybridization. It has been demonstrated that there is no differential accumulation of contractile protein transcripts in the crural muscles of the mouse hindlimb throughout the embryonic period (Ontell et al, 1993); however, evidence has been presented that differential accumulation of contractile proteins begins in rat hindlimbs during the fetal period (Narusawa et al, 1987;Condon et al, 1990;Lyons et al, 1990b).…”

Section: Introductionmentioning

confidence: 99%

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Modulation of contractile protein gene expression in fetal murine crural muscles: Emergence of muscle diversity

Ontell

Sopper

Lyons

et al. 1993

Developmental Dynamics

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The modulation of contractile protein gene expression in mouse crural muscles (i.e., muscles located in the region between the knee and ankle) during the fetal period (defined as 15 days gestation to birth), resulting in diversity among and within these muscles, has been evaluated with in situ hybridization and correlated with morphogenetic events in the extensor digitorum longus and soleus muscles. During the fetal period extensive secondary myotube formation occurs in the crural muscles, and the myotubes become innervated (Ontell and Kozeka [1984a,bl Am.

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“…The specificity and characterization of these mAbs against MHC isoforms have been previously established. The mAbs NOQ7-5-4D is specific to type I MHC (Narusawa et al, 1987;Petrof et al, 1992;Rubinstein and Hoh, 2000), MY-32 to all fast-type MHCs (Havenith et al, 1990;Monemi et al, 2000), SC-71 to type IIa MHC (Schiaffino et al, 1989;Stal et al, 1994;Monemi et al, 2000), ALD-58 to MHC-ton (Shafiq et al, 1984;, BA-G5 to MHC-␣ (Michel et al, 1996), F1.652 to MHC-emb (Michel et al, 1996), and N2.261 to MHC-neo (Michel et al, 1996).…”

Section: Immunocytochemistrymentioning

confidence: 99%

Adult human mylohyoid muscle fibers express slow‐tonic, α‐cardiac, and developmental myosin heavy‐chain isoforms

Wang

et al. 2004

Anat. Rec.

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Some adult cranial muscles have been reported to contain unusual myosin heavy-chain (MHC) isoforms (i.e., slow-tonic, ␣-cardiac, embryonic, and neonatal), which exhibit distinct contractile properties. In this study, adult human mylohyoid (MH) muscles obtained from autopsies were investigated to detect the unusual MHC isoforms. For comparison, the biceps brachii and masseter muscles of the same subjects were also examined. Serial cross-sections from the muscles studied were incubated with a panel of isoform-specific anti-MHC monoclonal antibodies that distinguish major and unusual MHC isoforms. On average, the slow type I and fast type II MHC-containing fibers in the MH muscle accounted for 54% and 46% of the fibers, respectively. In contrast to limb and trunk muscles, the adult human MH muscle was characterized by a large proportion of hybrid fibers (85%) and a small percentage of pure fibers (15%; P Ͻ 0.01). Of the fast fiber types, the proportion of the type IIa MHC-containing fibers (92%) was much greater than that of the type IIx MHC-containing fibers (8%; P Ͻ 0.01). Our data demonstrated that the adult human MH fibers expressed the unusual MHC isoforms that were also identified in the masseter, but not in the biceps brachii. These isoforms were demonstrated by immunocytochemistry and confirmed by electrophoretic immunoblotting. Fiber-to-fiber comparisons showed that the unusual MHC isoforms were coexpressed with the major MHC isoforms (i.e., MHCI, IIa, and IIx), thus forming various major/unusual (or m/u) MHC hybrid fiber types. Interestingly, the unusual MHC isoforms were expressed in a fiber type-specific manner. The slow-tonic and ␣-cardiac MHC isoforms were coexpressed predominantly with slow type I MHC isoform, whereas the developmental MHC isoforms (i.e., embryonic and neonatal) coexisted primarily with fast type IIa MHC isoform. There were no MH fibers that expressed exclusively unusual MHC isoforms. Approximately 81% of the slow type I MHC-containing fibers expressed slow-tonic and ␣-cardiac MHC isoforms, whereas 80% of the fast type IIa MHC-containing fibers expressed neonatal MHC isoform. The m/u hybrid fibers (82% of the total fiber population) were found to constitute the predominant fiber types in the adult human MH muscle. At least seven m/u MHC hybrid fiber types were identified in the adult human MH muscle. The most common m/u hybrid fiber types were found to be the MHCI/slow-tonic/␣-cardiac and MHCIIa/neonatal, which accounted for 39% and 33% of the total fiber population, respectively. The multiplicity of MHC isoforms in the adult MH fibers is believed to be related to embryonic origin, innervation pattern, and unique functional requirements.

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Slow myosin in developing rat skeletal muscle.

Cited by 245 publications

References 46 publications

Specific programs of myosin expression in the postnatal development of rat muscles

Specific programs of myosin expression in the postnatal development of rat muscles

Modulation of contractile protein gene expression in fetal murine crural muscles: Emergence of muscle diversity

Adult human mylohyoid muscle fibers express slow‐tonic, α‐cardiac, and developmental myosin heavy‐chain isoforms

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