Regulation of an antisense RNA with the transition of neonatal to IIb myosin heavy chain during postnatal development and hypothyroidism in rat skeletal muscle

Pandorf, Clay E.; Jiang, Weihua; Qin, Anqi X.; Bodell, P. W.; Baldwin, Kenneth M.; Haddad, Fadia

doi:10.1152/ajpregu.00591.2011

Cited by 13 publications

(14 citation statements)

References 68 publications

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“…In addition, MYH3 coding the embryonic isoform locates 5' to MYH2 while MYH8 coding the neonatal isoform locates 3' to MYH4. According to Pandorf et al (2012), the expression of MYH4 mRNA (coding MHC 2b) increased until day 20 of the postnatal life in Plantaris muscle of the rat, whereas MYH8 mRNA (coding the neonatal isoform) disappeared in the same period. When the new born rats were given PTU in order to induce hypothyroidism, the expression of MYH4 mRNA in the Plantaris muscle remained low, while that of MYH8 mRNA was observed even on day 40 of postnatal life (Pandorf et al 2012).…”

Section: Discussionmentioning

confidence: 99%

“…According to Pandorf et al (2012), the expression of MYH4 mRNA (coding MHC 2b) increased until day 20 of the postnatal life in Plantaris muscle of the rat, whereas MYH8 mRNA (coding the neonatal isoform) disappeared in the same period. When the new born rats were given PTU in order to induce hypothyroidism, the expression of MYH4 mRNA in the Plantaris muscle remained low, while that of MYH8 mRNA was observed even on day 40 of postnatal life (Pandorf et al 2012). The results indicate that the transition from the neonatal isoform to MHC 2b, two isoforms located in the vicinity of the same chromosome, might have been delayed by the hypothyroidism.…”

Section: Discussionmentioning

confidence: 99%

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Changes in muscle fiber type and expression of mRNA of myosin heavy chain isoforms in porcine muscle during pre‐ and postnatal development

Katsumata

Yamaguchi

Ishida

et al. 2016

Animal Science Journal

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The purpose of this study is to elucidate developmental changes in muscle fiber type in the pig during pre- and postnatal development. For this purpose, we performed a histochemical analysis for myosin adenosine triphosphatase activity to assess muscle fiber type and determined abundances of messenger RNA (mRNA) of myosin heavy chain (MHC) isoforms. Samples of Longissimus dorsi (LD) muscle were taken from fetuses on day 90 of the fetal stage. Further, samples of LD, Rhomboideus and Biceps femoris (B. femoris) muscles were taken from pigs when they were 1, 12, 26, 45 or 75 days old. Expression of MHC 2b mRNA in the LD and the B. femoris muscles rapidly and considerably increased from the late fetal stage to the early postnatal stage and this increase was associated with the development of type 2b fibers at least in the LD muscle. As shown by the rapid and considerable changes in expression of MHC 2b mRNA, it seems that a certain plasticity of muscle fiber type still remains in this developmental stage.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Changes in muscle fiber type and expression of mRNA of myosin heavy chain isoforms in porcine muscle during pre‐ and postnatal development

Katsumata

Yamaguchi

Ishida

et al. 2016

Animal Science Journal

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“…The molecular mechanisms controlling the myosin switch during development remain to be established and probably involve specific regulatory sequences associated with the MYH gene cluster, where MYH genes are arranged in the order: MYH3 - MYH2 - MYH1 - MYH4 - MYH8 - MYH13 . It has been reported that thyroid hormone controls the transition between neonatal and adult fast 2B MyHC by a long non-coding antisense RNA which is transcriptionally regulated during postnatal development and in response to hypothyroidism: this antisense RNA is transcribed from a site within the intergenic region between MYH8 (MyHC-neo) and the closely associated MYH4 (MyHC-2B) gene and appears to mediate the transcriptional repression of the MYH8 gene [ 40 ]. A central enhancer located between the MYH3 and MYH2 genes has been recently identified [ 41 ].…”

Section: Reviewmentioning

confidence: 99%

Developmental myosins: expression patterns and functional significance

et al. 2015

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Developing skeletal muscles express unique myosin isoforms, including embryonic and neonatal myosin heavy chains, coded by the myosin heavy chain 3 (MYH3) and MYH8 genes, respectively, and myosin light chain 1 embryonic/atrial, encoded by the myosin light chain 4 (MYL4) gene. These myosin isoforms are transiently expressed during embryonic and fetal development and disappear shortly after birth when adult fast and slow myosins become prevalent. However, developmental myosins persist throughout adult stages in specialized muscles, such as the extraocular and jaw-closing muscles, and in the intrafusal fibers of the muscle spindles. These myosins are re-expressed during muscle regeneration and provide a specific marker of regenerating fibers in the pathologic skeletal muscle. Mutations in MYH3 or MYH8 are responsible for distal arthrogryposis syndromes, characterized by congenital joint contractures and orofacial dysmorphisms, supporting the importance of muscle contractile activity and body movements in joint development and in shaping the form of the face during fetal development. The biochemical and biophysical properties of developmental myosins have only partially been defined, and their functional significance is not yet clear. One possibility is that these myosins are specialized in contracting against low loads, and thus, they may be adapted to the prenatal environment, when fetal muscles contract against a very low load compared to postnatal muscles.

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“…Recently, postnatal changes in MyHC isoform mRNA transcription were found to be regulated by a natural antisense transcript (bII NAT) such that expression of MyHC Neo is positively correlated with expression of bII NAT whereas expression of MyHC 2B is negatively correlated. Thus, postnatally expression of bII NAT can play a critical role in coordinating the transition from MyHC Neo to adult MyHC 2B (and possibly MyHC 2X ) isoforms (315). Recently, it was shown that postnatal changes in MyHC isoform mRNA expression in the rat diaphragm muscle do not match the changes in MyHC protein expression, suggesting that changes in MyHC isoform expression in the developing rat diaphragm muscle are not driven solely by changes in mRNA expression (136).…”

Section: Respiratory Muscle Structurementioning

confidence: 99%

Mechanical Properties of Respiratory Muscles

Sieck

Ferreira

Reid

et al. 2013

Comprehensive Physiology

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Striated respiratory muscles are necessary for lung ventilation and to maintain the patency of the upper airway. The basic structural and functional properties of respiratory muscles are similar to those of other striated muscles (both skeletal and cardiac). The sarcomere is the fundamental organizational unit of striated muscles and sarcomeric proteins underlie the passive and active mechanical properties of muscle fibers. In this respect, the functional categorization of different fiber types provides a conceptual framework to understand the physiological properties of respiratory muscles. Within the sarcomere, the interaction between the thick and thin filaments at the level of cross-bridges provides the elementary unit of force generation and contraction. Key to an understanding of the unique functional differences across muscle fiber types are differences in cross-bridge recruitment and cycling that relate to the expression of different myosin heavy chain isoforms in the thick filament. The active mechanical properties of muscle fibers are characterized by the relationship between myoplasmic Ca2+ and cross-bridge recruitment, force generation and sarcomere length (also cross-bridge recruitment), external load and shortening velocity (cross-bridge cycling rate), and cross-bridge cycling rate and ATP consumption. Passive mechanical properties are also important reflecting viscoelastic elements within sarcomeres as well as the extracellular matrix. Conditions that affect respiratory muscle performance may have a range of underlying pathophysiological causes, but their manifestations will depend on their impact on these basic elemental structures.

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Regulation of an antisense RNA with the transition of neonatal to IIb myosin heavy chain during postnatal development and hypothyroidism in rat skeletal muscle

Cited by 13 publications

References 68 publications

Changes in muscle fiber type and expression of mRNA of myosin heavy chain isoforms in porcine muscle during pre‐ and postnatal development

Changes in muscle fiber type and expression of mRNA of myosin heavy chain isoforms in porcine muscle during pre‐ and postnatal development

Developmental myosins: expression patterns and functional significance

Mechanical Properties of Respiratory Muscles

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