Three Slow Myosin Heavy Chains Sequentially Expressed in Developing Mammalian Skeletal Muscle

Hughes, Simon M.; Cho, Mildred; Karsch-Mizrachi, Ilene; Travis, Marilyn; Silberstein, L.; Leinwand, Leslie A.; Blau, Helen M.

doi:10.1006/dbio.1993.1178

Cited by 198 publications

(187 citation statements)

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“…Secondary antibodies were HRP-conjugated reagents from Amersham (dilution 1:1,000) that included rabbit anti-mouse Ig (NIF 825) or donkey anti-rabbit Ig (NA 934). The A4.74 monoclonal antibody developed by H. M. Blau that specifically recognizes myosin in type IIA fatigue-resistant fast-twitch fibers (35) was obtained from the Developmental Studies Hybridoma Bank developed under the auspices of the NICHD and maintained by the University of Iowa, Department of Biological Sciences, Iowa City, Iowa, USA.…”

Section: Methodsmentioning

confidence: 99%

“…When heterozygous mutant (+/m) mice were bred with each other, we observed the following genotype frequencies at 30 days of age (n = 146 offspring): normal (+/+), 35.6% (n = 52); heterozygous mutant (+/m), 63.0% (n = 92); and homozygous mutant (m/m), 1.4% (n = 2). These results indicated that (a) the (m/m) genotype was underrepresented at 30 days (P < 0.001 using c 2 analysis), and (b) there was no selection bias against the heterozygous (+/m) genotype by 30 days (P = 0.54 for selection).…”

Section: Targeted Substitution Of Hyperkpp Variant Met1592val Into Momentioning

confidence: 97%

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Targeted mutation of mouse skeletal muscle sodium channel produces myotonia and potassium-sensitive weakness

Hayward¹,

Kim²,

Lee³

et al. 2008

J. Clin. Invest.

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Hyperkalemic periodic paralysis (HyperKPP) produces myotonia and attacks of muscle weakness triggered by rest after exercise or by K + ingestion. We introduced a missense substitution corresponding to a human familial HyperKPP mutation (Met1592Val) into the mouse gene encoding the skeletal muscle voltage-gated Na + channel Na V 1.4. Mice heterozygous for this mutation exhibited prominent myotonia at rest and muscle fibertype switching to a more oxidative phenotype compared with controls. Isolated mutant extensor digitorum longus muscles were abnormally sensitive to the Na + /K + pump inhibitor ouabain and exhibited age-dependent changes, including delayed relaxation and altered generation of tetanic force. Moreover, rapid and sustained weakness of isolated mutant muscles was induced when the extracellular K + concentration was increased from 4 mM to 10 mM, a level observed in the muscle interstitium of humans during exercise. Mutant muscle recovered from stimulation-induced fatigue more slowly than did control muscle, and the extent of recovery was decreased in the presence of high extracellular K + levels. These findings demonstrate that expression of the Met1592Val Na + channel in mouse muscle is sufficient to produce important features of HyperKPP, including myotonia, K + -sensitive paralysis, and susceptibility to delayed weakness during recovery from fatigue.

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Section: Methodsmentioning

confidence: 99%

Section: Targeted Substitution Of Hyperkpp Variant Met1592val Into Momentioning

confidence: 97%

Targeted mutation of mouse skeletal muscle sodium channel produces myotonia and potassium-sensitive weakness

Hayward¹,

Kim²,

Lee³

et al. 2008

J. Clin. Invest.

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“…Sections were washed in PBS to stop the development and then mounted in glycerin-gelatin. Photographs were taken immediately after mounting (17). The monoclonal antibodies G-6 and B-6 were supplied by S. Schiaffino (48).…”

Section: Methodsmentioning

confidence: 99%

Aberrant expression of myosin isoforms in skeletal muscles from mice lacking therev-erbAαorphan receptor gene

Pircher¹,

Chomez²,

Yu³

et al. 2005

American Journal of Physiology-Regulatory, Integrative and Comp

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Aberrant expression of myosin isoforms in skeletal muscles from mice lacking the rev-erbA␣ orphan receptor gene. Am J Physiol Regul Integr Comp Physiol 288: R482-R490, 2005. First published September 16, 2004; doi:10.1152/ajpregu.00690.2003.-The rev-erbA␣ orphan protein belongs to the steroid nuclear receptor superfamily. No ligand has been identified for this protein, and little is known of its function in development or physiology. In this study, we focus on 1) the distribution of the rev-erbA␣ protein in adult fast-and slow-twitch skeletal muscles and muscle fibers and 2) how the rev-erbA␣ protein influences myosin heavy chain (MyHC) isoform expression in mice heterozygous (ϩ/Ϫ) and homozygous (Ϫ/Ϫ) for a rev-erbA␣ protein null allele. In the fast-twitch extensor digitorum longus muscle, rev-erbA␣ protein expression was linked to muscle fiber type; however, MyHC isoform expression did not differ between wild-type, ϩ/Ϫ, or Ϫ/Ϫ mice. In the slow-twitch soleus muscle, the link between rev-erbA␣ protein and MyHC isoform expression was more complex than in the extensor digitorum longus. Here, a significantly higher relative amount of the ␤/slow (type I) MyHC isoform was observed in both rev-erbA␣ Ϫ/Ϫ and ϩ/Ϫ mice vs. that shown in wild-type controls. A role for the ratio of thyroid hormone receptor proteins ␣ 1 to ␣2 in modulating MyHC isoform expression can be ruled out because no differences were seen in MyHC isoform expression between thyroid hormone receptor ␣ 2-deficient mice (heterozygous and homozygous) and wild-type mice. Therefore, our data are compatible with the rev-erbA␣ protein playing an important role in the regulation of skeletal muscle MyHC isoform expression. orphan nuclear receptors; thyroid hormone; fast-and slow-twitch muscle THE VARIABLE EXPRESSION OF myofibrillar protein isoforms is a major determinant of the contractile properties and ATPase activities of skeletal and myocardial fibers (3, 50). The myosin heavy chain (MyHC) molecule is the most abundant myofibrillar protein and is encoded by a multigene family consisting of several members (35). Several isoforms have now been described in rodent skeletal muscles, including one slow isoform (type I or ␤/slow), three fast (IIa, IIx/d, and IIb), and two developmental (embryonic and neonatal/perinatal/fetal) isoforms, which are all coded by distinct genes (50). Four other MyHC isoforms, slow tonic, superfast IIm, ␣-cardiac-like, and extraocular myosin, are expressed in a few specialized muscles (7, 50). Despite their similarity in primary structure, the expression of different MyHC isoforms is precisely regulated in a tissue-specific and developmental stage-specific manner (50, 52). In addition, innervation patterns (33, 45, 46), altered physiological stimuli (34, 46), and various hormones (19) are known to have a significant impact on MyHC isoform expression.Skeletal muscle is a major target for hormone action. Thyroid hormone is one of the most potent regulators of skeletal muscle MyHC isoform expression in mammals, and it has been suggested...

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“…We also thank the very dedicated group of subjects who made this project possible. The monoclonal antibody A4.951 for MyHC I, developed by Dr. H. M. Blau (18), was obtained from the Developmental Studies Hybridoma Bank developed under the auspices of the National Institute of Child Health and Human Development and maintained by the Univ. of Iowa, Dept.…”

Section: Acknowledgmentsmentioning

confidence: 99%

Resistance exercise with whey protein ingestion affects mTOR signaling pathway and myostatin in men

Hulmi¹,

Tannerstedt²,

Selänne³

et al. 2009

Journal of Applied Physiology

120

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Hulmi JJ, Tannerstedt J, Selä nne H, Kainulainen H, Kovanen V, Mero AA. Resistance exercise with whey protein ingestion affects mTOR signaling pathway and myostatin in men. J Appl Physiol 106: 1720 -1729. First published March 19, 2009 doi:10.1152/japplphysiol.00087.2009.-Signaling pathways sense local and systemic signals and regulate muscle hypertrophy. The effects of whey protein ingestion on acute and long-term signaling responses of resistance exercise are not well known. Previously untrained young men were randomized into protein (n ϭ 9), placebo (n ϭ 9), and control (n ϭ 11) groups. Vastus lateralis (VL) muscle biopsies were taken before and 1 h and 48 h after a leg press of 5 ϫ 10 repetitions [resistance exercise (RE)] and after 21 wk (2 times per week) of resistance training (RT). Protein (15 g of whey) or nonenergetic placebo was ingested before and after a single RE bout and each RE workout throughout the RT. The protein group increased its body mass and VL muscle thickness (measured by ultrasonography) already at week 10.5 (P Ͻ 0.05). At week 21, the protein and placebo groups had similarly increased their myofiber size. No changes were observed in the nonexercised controls. However, the phosphorylation of p70 S6K and ribosomal protein S6 (rpS6) were increased at 1 h post-RE measured by Western blotting, the former being the greatest with protein ingestion. Mammalian target of rapamycin (mTOR) phosphorylation was increased after the RE bout and RT only in the protein group, whereas the protein ingestion prevented the post-RE decrease in phosphorylated eukaryotic initiation factor 4E binding protein 1 (p-4E-BP1). Akt phosphorylation decreased after RT, whereas no change was observed in phosphorylated eukaryotic elongation factor 2. A post-RE decrease in muscle myostatin protein occurred only in the placebo group. The results indicate that resistance exercise rapidly increases mTOR signaling and may decrease myostatin protein expression in muscle and that whey protein increases and prolongs the mTOR signaling response.hypertrophy; training; nutrition; S6K1; skeletal muscle ADEQUATE MUSCLE MASS is crucial for human well-being. It is, therefore, important to identify the mechanisms that stimulate muscle hypertrophy or prevent atrophy. The most efficient way to increase the size of a skeletal muscle is by resistance training (RT) in combination with protein-containing nutrition. Muscle hypertrophy due to RT and protein nutrition seems largely to result from cumulative acute increases in muscle protein synthesis. One resistance exercise (RE) bout can within 1 h increase muscle protein synthesis (9), which can last up to 72 h after exercise (39). Protein ingestion before or after a bout of RE has been shown to significantly enhance this response (52) and be possibly more beneficial in terms of muscle hypertrophy than nutrient ingestion at other times of day (7, 11). It would thus be important to understand how protein ingestion affects pathways regulating intracellular hypertrophy of muscle in the context ...

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Three Slow Myosin Heavy Chains Sequentially Expressed in Developing Mammalian Skeletal Muscle

Cited by 198 publications

References 0 publications

Targeted mutation of mouse skeletal muscle sodium channel produces myotonia and potassium-sensitive weakness

Targeted mutation of mouse skeletal muscle sodium channel produces myotonia and potassium-sensitive weakness

Aberrant expression of myosin isoforms in skeletal muscles from mice lacking therev-erbAαorphan receptor gene

Resistance exercise with whey protein ingestion affects mTOR signaling pathway and myostatin in men

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