Myosin heavy chain isoforms in postnatal muscle development of mice

Agbulut, Onnik; Noirez, Philippe; Beaumont, Françoise; Butler-Browne, Gillian

doi:10.1016/s0248-4900(03)00087-x

Cited by 230 publications

(260 citation statements)

References 51 publications

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“…2 We performed immunolabeling with anti-NCAM and anti-neonatal/perinatal/fetal MHC (MHCn), both of which are neurally and developmentally regulated. 1,11,12,20,21,25 The multigene family that encodes MHC is expressed in a developmentally regulated sequence. Developmental isoforms that have been characterized include MHCemb and MHCn.…”

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confidence: 99%

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Myogenesis in human denervated muscle biopsies

2007

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Electron microscopic studies of long-term denervated rat muscles have identified very small, immature myofibers that are believed to arise from detached satellite cells that have fused to form new fibers within the interstitial space. At present, it is unknown whether and to what extent equivalent fibers exist in denervated human muscle. Serial sections of muscle biopsies from 66 patients diagnosed with polyneuropathy or amyotrophic lateral sclerosis were immunolabeled with anti-NCAM and antineonatal myosin heavy chain monoclonal antibodies that are both neurally and developmentally regulated. We evaluated 200 myofibers in each section. Of the biopsy specimens, 75% contained small myofibers that showed a thin perinuclear cytoplasmic rim. Small fibers expressing neonatal myosin heavy chain (MHCnϩ) were found in all of these biopsies (100%) and NCAMϩ fibers in 98%. The percentage of MHCnϩ small fibers averaged 82% and NCAMϩ small myofibers averaged 40%. The percentage of NCAMϩ small fibers was significantly lower than that of MHCnϩ fibers. In contrast, the percentage of MHCnϩ vs. NCAMϩ angular atrophic fibers did not show a significant difference. A substantial subset of neurogenic biopsies showed small fibers that differ from angular atrophic fibers both in size and expression pattern of MHCn and NCAM. Myogenesis appears to be a frequent finding in neurogenic atrophy.

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confidence: 99%

“…Newly formed myofibers display a highly regulated, sequential transition from embryonic to neonatal and finally to adult myosin heavy chain isoforms. 1,20 The different forms of NCAM are a result of alternative splicing of a single gene and post-translational modifications. 9,18 NCAM is also upregulated in newly formed myofibers.…”

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confidence: 99%

Myogenesis in human denervated muscle biopsies

2007

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“…Since it was first shown that the muscle fibers of mouse tongue consisted entirely of fast isoforms of MyHC (Dalrymple et al, 1999(Dalrymple et al, , 2000Shuler and Dalrymple, 2001), the composition ratio for each isoform has been studied in detail using gel electrophoresis (Agbulut et al, 2003). These studies have indicated that although MyHC-2b continues to increase after birth, MyHC-2a is expressed only transiently for several weeks postpartum.…”

Section: Discussionmentioning

confidence: 99%

“…Agbulut et al determined MyHC composition ratios in mouse tongue muscle and reported that while MyHC-2b increases from birth onward, MyHC-2a is expressed transiently, for only a few weeks postpartum (Agbulut et al, 2003). Moreover, tongue consists of both intrinsic and extrinsic muscles, and differences have been reported in the properties of fibers among the intrinsic muscles .…”

Section: Introductionmentioning

confidence: 99%

Myosin heavy chain composition of tongue muscle in microphthalmic (mi/mi) mice before and after weaning

Yanagisawa

Abe

Agematsu

et al. 2006

Annals of Anatomy - Anatomischer Anzeiger

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running title: MyHC in tongue muscle of mi/mi mice 2 SummaryTo elucidate the effects of teeth on muscle fibers in tongue during the development process, we examined the expression of muscle contractile proteins and the genes for those proteins in normal mice and microphthalmic (mi/mi) mice with impaired tooth eruption. The mice were observed during the growth period, including weaning, which is when feeding movements undergo major changes.Expression of the myosin heavy chain (MyHC)-2a protein, whose contraction speed is relatively slow, disappeared after weaning in normal mice, while it remained in high concentrations even after weaning in mi/mi mice. The presence of MyHC-2a after weaning in mice with no tooth eruption was attributed to a compensation for lack of proper masticatory function and sucking-like movements, as MyHC-2a is necessary for these movements.

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“…Mouse muscle is composed of four major fiber types, defined by their myosin heavy chain (MyHC) content as slow type I and fast type IIa, IIx, and IIb (Kelly and Rubinstein, 1994). To determine whether fiber type was a factor in the level of expression driven by A17, we examined the soleus muscle, because in mouse it contains approximately 50% slow type I and fast type IIa/IIx fibers (Agbulut et al, 2003). Immunostaining with MyHC-specific antibodies showed clearly that myonuclei with ␤-galactosidase activity were located in both fiber types (Fig.…”

Section: A17 Drives the Mrf4 Promoter In Both Fast And Slow Fiber Typesmentioning

confidence: 99%

The A17 enhancer directs expression of Myf5 to muscle satellite cells but Mrf4 to myonuclei

Chang

Vincent

Buckingham

et al. 2007

Developmental Dynamics

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The myogenic regulatory factors, Myf5 and Mrf4, play key roles in the specification and differentiation of skeletal muscle, respectively. Many cis-acting regulatory elements at the Mrf4/Myf5 locus have been identified, including the A17 enhancer. During development, A17 in conjunction with the Mrf4 or Myf5 promoter, directs transgene expression either to embryonic or fetal muscles. We now show that this enhancer also regulates Mrf4/Myf5 transcription in the adult. A17 linked to the Myf5 promoter drives expression in muscle satellite cells, whereas with the Mrf4 promoter, A17 directs transgene expression to myonuclei. Interestingly, expression of A17-Mrf4-nlacZ transgenes in myonuclei varies between muscles, revealing muscle autonomous transcriptional regulation. During muscle repair, satellite cells are induced to proliferate and differentiate to provide new myonuclei. A17 directs Myf5 expression in satellite cell progeny while it only drives the Mrf4 promoter after differentiation. Importantly, therefore, this promoterspecific activity directed by A17 reflects aspects of the expression profiles of the endogenous Myf5 and Mrf4 genes. Developmental Dynamics 236:3419 -3426, 2007.

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Myosin heavy chain isoforms in postnatal muscle development of mice

Cited by 230 publications

References 51 publications

Myogenesis in human denervated muscle biopsies

Myogenesis in human denervated muscle biopsies

Myosin heavy chain composition of tongue muscle in microphthalmic (mi/mi) mice before and after weaning

The A17 enhancer directs expression of Myf5 to muscle satellite cells but Mrf4 to myonuclei

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