MyoR is expressed in nonmyogenic cells and can inhibit their differentiation

Yu, Liming; Mikloucich, Jerome; Sangster, Niquiche; Perez, Ana V.; McCormick, Paulette J.

doi:10.1016/s0014-4827(03)00252-0

Cited by 23 publications

(34 citation statements)

References 42 publications

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“…However, these signaling changes did not lead to alterations in gene expression in MAs after a liquid diet, even though muscle fiber size was affected. Masticatory muscles are morphologically and physiologically distinct from axial muscles, and, unlike the latter, masticatory muscles might be slow to remodel (19,35,51,52). They also have reduced ability to hypertrophy and an increased propensity to undergo apoptosis (19).…”

Section: Discussionmentioning

confidence: 99%

Masticatory muscles of mouse do not undergo atrophy in space

et al. 2015

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Muscle loading is important for maintaining muscle mass; when load is removed, atrophy is inevitable. However, in clinical situations such as critical care myopathy, masticatory muscles do not lose mass. Thus, their properties may be harnessed to preserve mass. We compared masticatory and appendicular muscles responses to microgravity, using mice aboard the space shuttle Space Transportation System-135. Age-and sex-matched controls remained on the ground. After 13 days of space flight, 1 masseter (MA) and tibialis anterior (TA) were frozen rapidly for biochemical and functional measurements, and the contralateral MA was processed for morphologic measurements. Flight TA muscles exhibited 20 6 3% decreased muscle mass, 2-fold decreased phosphorylated (P)-Akt, and 4-to 12-fold increased atrogene expression. In contrast, MAs had no significant change in mass but a 3-fold increase in P-focal adhesion kinase, 1.5-fold increase in P-Akt, and 50-90% lower atrogene expression compared with limb muscles, which were unaltered in microgravity. Myofibril force measurements revealed that microgravity caused a 3-fold decrease in specific force and maximal shortening velocity in TA muscles. It is surprising that myofibril-specific force from both control and flight MAs were similar to flight TA muscles, yet power was compromised by 40% following flight. Continued loading in microgravity prevents atrophy, but masticatory muscles have a different set point that mimics disuse atrophy in the appendicular

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Section: Discussionmentioning

confidence: 99%

Masticatory muscles of mouse do not undergo atrophy in space

et al. 2015

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“…In mice, although Musculin (Myod repressor, MyoR) is known to block myogenesis and activate E-box-dependent muscle genes [32], it can also inhibit differentiation of nonmyogenic cells and regulate functions of kidney side population cells [33,34]. These observations indicate that Musculin might have multiple functions.…”

Section: Discussionmentioning

confidence: 99%

Essential roles of basic helix-loop-helix transcription factors, Capsulin and Musculin, during craniofacial myogenesis of zebrafish

Lee

Chang

Hsu

et al. 2011

Cell. Mol. Life Sci.

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Capsulin and Musculin are basic helix-loop-helix transcription factors, but their biophysiological roles in zebrafish cranial myogenesis are unclear. Expressions of endogenous capsulin transcripts are detected at the central- (~24-hpf) and at dorsal- and ventral-mesoderm cores (~30-72 hpf) of branchial arches. In contrast, musculin transcripts are expressed as a two-phase manner: early phase (20-22 hpf) expressions of musculin are detected at the head mesoderm, whereas late-phase (36-72 hpf) are detected at all presumptive head-muscle precursors. Knockdown of either capsulin or musculin leads to loss of all cranial muscles without affecting trunk muscle development. The defective phenotypes of Capsulin- and Musculin-morphant can be rescued by co-injection of mRNA of each other. Both myf5 and myod transcripts are down-regulated in the Capsulin-morphant while myod transcripts are up-regulated in the Musculin-morphant. Therefore, we propose a putative regulatory network to understand how capsulin/musculin regulate distinctly either myf5 or myod during zebrafish craniofacial myogenesis.

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“…Vertebrates have four MRFs: Myf5 (Braun et al, 1989) and Myod (Sassoon et al, 1989), which play redundant roles in myoblast specification in the dorsal or ventral dermomyotome, respectively, and MRF4 (Braun et al, 1990) and Myogenin (Edmondson and Olson, 1989), which instruct myoblasts for terminal differentiation. The bHLH factor MyoR (myogenic repressor) or musculin is expressed at high levels in proliferating skeletal myoblasts where it antagonizes the action of Myod and is downregulated during muscle differentiation (Lu et al, 1999;Yu et al, 2003). MyoR is paralogous to the bHLH protein capsulin, which is expressed in smooth muscle cell precursors (Lu et al, 1998).…”

Section: Molecular Patterning Of Musclesmentioning

confidence: 99%

“…Twist is essential for mesoderm specification and its subsequent subdivision into different myogenic domains (Baylies and Bate, 1996;Leptin, 1991) and is activated via a Wg (Drosophila Wnt) signaling (Bate and Rushton, 1993) whilst being negatively regulated by a Notch signaling pathway (TapanesCastillo and Baylies, 2004). The further subdivision of myogenic domains and the specification of different types of muscles involve Kume, 2009;Potthoff and Olson, 2007;Schmidt et al, 2003;Wilm et al, 2004;Yu et al, 2003).…”

Section: Molecular Patterning Of Musclesmentioning

confidence: 99%