Fast myosin heavy chain expression during the early and late embryonic stages of chicken skeletal muscle development

Horn, Robert Van; Crow, Michael T.

doi:10.1016/0012-1606(89)90100-0

Cited by 33 publications

(11 citation statements)

References 40 publications

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“…These Pax7 + myogenic precursors fuse among themselves or to the primary fibers and give rise to secondary or fetal fibers that express specific markers such as β-enolase, Nfix or MyLC3 (Myl3) (Fougerousse et al, 2001;Keller et al, 1992;Kelly et al, 1997;Messina et al, 2010). At this time, the fibers also start to express fast MyHC isoforms (Van Horn and Crow, 1989). During secondary myogenesis, muscle growth is sustained essentially by cell fusion and the addition of myonuclei from proliferating Pax7 + progenitors (White et al, 2010).…”

Section: Primary and Secondary Myogenesismentioning

confidence: 99%

Making muscle: skeletal myogenesisin vivoandin vitro

2017

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Skeletal muscle is the largest tissue in the body and loss of its function or its regenerative properties results in debilitating musculoskeletal disorders. Understanding the mechanisms that drive skeletal muscle formation will not only help to unravel the molecular basis of skeletal muscle diseases, but also provide a roadmap for recapitulating skeletal myogenesis in vitro from pluripotent stem cells (PSCs). PSCs have become an important tool for probing developmental questions, while differentiated cell types allow the development of novel therapeutic strategies. In this Review, we provide a comprehensive overview of skeletal myogenesis from the earliest premyogenic progenitor stage to terminally differentiated myofibers, and discuss how this knowledge has been applied to differentiate PSCs into muscle fibers and their progenitors in vitro.

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Section: Primary and Secondary Myogenesismentioning

confidence: 99%

Making muscle: skeletal myogenesisin vivoandin vitro

2017

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“…in several instances, antibodies selectively reactive with developmental heavy chain forms were found fo stain all fibres in a given muscle (Bandman & Bennett, 1988;Van Horn & Crow, 1989). Of particular interest, however, would be examination of fibres with such antibodies during periods of rapid transition.…”

Section: Discussionmentioning

confidence: 95%

“…Another is presumably the remnants of the early embryonic fast-type species identified by Hofmann and colleagues. (1988) and Van Horn and Crow (1989). The structural characteristics distinguishing these four forms are under investigation.…”

Section: Discussionmentioning

confidence: 98%

“…Subsequently, shallow gradient SDS-gel electrophoresis permitted resolution of a major heavy chain band af 19 days in ovo and I day post-hatch which was immunochemically distinct from a major heavy chain species present af 12 days in ovo (Hofmann et ai., 1988). Recently, Van Horn and Crow (1989) distinguished immunochemically early-and late-embryonic fast-type heavy chains. They showed that the late form failed fo appear in curarized embryos suggesting that is appearance was related to innervation.…”

Section: Discussionmentioning

confidence: 98%

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Developmental myosin heavy chain progression in avian type IIB muscle fibres

Rushbrook

Weiss

Yao

1991

J Muscle Res Cell Motil

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Myosin heavy chain species were investigated during development in avian pectoralis major muscles (type IIB fibres) by high resolution anion-exchange chromatography of the myosin head region, subfragment-1. At 15 days in ovo four distinct fast-type heavy chain species, I, II, III and IV, in order of elution, were identified. By 19 days in ovo, form IV had become predominant and remained the major species through 3-days post-hatch. This form has been named the peri-hatch form. Between 3 and 5 days post-hatch, a second massive change occurred such that by 5 days post-hatch a new species, V, apparent at 19 days in ovo in small amounts, dominated and at 8 days post-hatch was the only heavy chain species present. Form V, which corresponds to that previously identified as the post-hatch form, continued as the major species through 20 days post-hatch and was replaced slowly by the adult form. N-terminal sequencing of CNBr peptides from three subfragment-1 heavy chain species, the peri-hatch (form IV), the post-hatch (form V) and adult, revealed differences in amino acid sequence consistent with the three being products of different genes. These results confirm and extend recent reports of complexity in fast heavy chain expression prior to hatching in the chicken (Hofmann et al., 1988; Van Horn & Crow, 1989).

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“…There are, moreover, two different embryonic ('early' and 'late') fast-type myosins in this muscle (Lowey et al, 1986;Gauthier, 1987;Hofmann ef al., 1988). Early and late embryonic fast myosins have also been identified in hindlimb muscles (Crow, 1987;van Horn & Crow, 1989), and slow-type embryonic myosins have also been described in these muscles (Benfield ef al., 1983;Hofmann et al, 1988;Dhoot, 1989).…”

Section: Introductionmentioning

confidence: 99%

Developmental transitions in the myosin patterns of two fast muscles

Gauthier

Orfanos

1993

J Muscle Res Cell Motil

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Transitions in myosin patterns were examined in situ by immunofluorescence in two fast muscles of the developing chicken, the pectoralis and the posterior latissimus dorsi. Myosin isoforms were localized using stage-specific monoclonal antibodies against the heavy chain of pectoralis myosin. Two antibodies (12C5 and 10H10) recognize adult and late embryonic myosin. They reacted weakly with both the pectoralis and posterior latissimus dorsi at 10 days in ovo, but intensely at 18 days in ovo. Both muscles were completely unreactive with an adult-specific antibody (5C3), indicating that the staining with 12C5 and 10H10 at 18 days in ovo reflects embryonic myosin. Thus two different embryonic isoforms are expressed sequentially in each muscle. Both 12C5 and 10H10 reacted weakly again with these muscles after hatching. The reappearance of a strong positive response to both antibodies, at 28 days in the pectoralis and after 60 days in the posterior latissimus dorsi, correlated well with the first appearance of a response to the adult-specific antibody, 5C3, signalling the beginning of the adult pattern. Both muscles reacted strongly with an antibody (5B4) specific for 'neonatal' myosin between 18 days in ovo and 60 days after hatching. In the pectoralis, embryonic was replaced by neonatal myosin in most fibres by 14 days after hatching; by 28 days, both adult and neonatal myosin were expressed in most fibres; and in the adult, neonatal myosin was replaced entirely by the adult isoform. In contrast, many fibres in the posterior latissimus dorsi still expressed both embryonic and neonatal myosins up to at least 60 days post-hatch, and the remaining fibres expressed the neonatal isoform; the neonatal isoform was present in some fibres even in the adult posterior latissimus dorsi. We have therefore demonstrated in situ four different heavy chain isoforms in two different fast muscles. 'Early embryonic', 'late embryonic', 'neonatal' and eventually 'adult' isoforms are expressed in each muscle and more than one isoform often coexists in the same fibre.

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Fast myosin heavy chain expression during the early and late embryonic stages of chicken skeletal muscle development

Cited by 33 publications

References 40 publications

Making muscle: skeletal myogenesisin vivoandin vitro

Making muscle: skeletal myogenesisin vivoandin vitro

Developmental myosin heavy chain progression in avian type IIB muscle fibres

Developmental transitions in the myosin patterns of two fast muscles

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