Nerve-dependent changes in clonable myoblast populations

Bonner, Philip H.

doi:10.1016/0012-1606(78)90285-3

Cited by 49 publications

(17 citation statements)

References 15 publications

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“…Therefore, both slow and fast myosin light chains are synthesized and assembled as part of the myofibrillar apparatus at these ages. Synthesis of slow myosin light chains in pectoral muscle begins to decline at approximately 12 days of development; by 14 days of development, only trace amounts of one slow myosin light chain, (27)(28)(29), there is abundant evidence that individual fibers can synthesize both slow and fast myosin and that the synthesis of myosin type is able to be regulated within an individual fiber (12,(30)(31)(32)(33)(34). For example, in cross-innervation or chronic stimulation of fast muscle there is a change in myosin isozyme type in existing fibers as a response to these changing environmental stimuli (30)(31)(32)(33).…”

Section: Resultsmentioning

confidence: 99%

Myosin light chains and the developmental origin of fast muscle.

Stockdale¹,

Raman²,

Baden³

1981

Proc. Natl. Acad. Sci. U.S.A.

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Physiological characteristics of embryonic and fetal fast muscle function are similar to those ofadult slow muscles, whereas most biochemical data suggest that embryonic and fetal fast muscles contain only fast muscle myosin. In the studies reported here, myofibrillar preparations from developing avian pectoral muscle (fast muscle) were isolated and analyzed for myosin light-chain type and synthesis. These Developing fast muscle has physiological characteristics similar to those of slow muscle of the adult (1, 2); however, most biochemical analyses of fetal fast muscle indicate the presence of only fast myosin (3-6). The basis for the discrepancy between physiological and biochemical measurements is complex, because of the varied developmental ages that have been studied and the age-related differences in stoichiometry of the proteins comprising the myofibrillar apparatus during embryonic development (7, 8). Furthermore, recent observations indicate that there are embryonic forms ofboth myosin heavy chain and light chain not found in the adult (9-11).Gauthier et aL (12) report that development of a mammalian fast muscle (the diaphragm) is characterized by the presence of immunologically reactive slow and fast myosin within every muscle fiber, whereas, after birth, nearly every fiber contains only fast myosin. However, in analyzing a different fast muscle (avian pectoral muscle), Hoh (7) and Rubinstein and coworkers (4, 5) report that only fast myosin and no slow myosin is found in embryonic or fetal stages of pectoral muscle development. The latter investigators propose that the more developmentally primitive muscle synthesizes fast myosin and that the initiation of slow myosin synthesis is a consequence of developmental events imposed upon the muscle, such as innervation. However, the recent work of Keller and Emerson (13) and of Stockdale et al. (14) demonstrates that innervation is not required for initiation of slow myosin synthesis; myoblasts from embryonic muscle differentiating in cell culture in the complete absence of nerves synthesize slow myosin light chains. This paper extends these observations to show that early in development avian fast muscle synthesizes and assembles myofibrils with both slow and fast myosin light chains. Later in development, fast muscle no longer assembles myofibrils containing slow myosin light chains due to the cessation of synthesis of slow myosin light chains in mid-development. MATERIALS AND METHODSMuscle Tissue. Muscle was prepared from White Leghorn chickens or White Leghorn chicken embryos. Fast muscle (pectoral muscle) or slow muscle (lateral adductor of the thigh or anterior latissimus dorsi) was dissected from embryonic or adult birds and cleaned, and myosin was extracted. Fast muscle development was studied from day 9 of incubation through day 1 after hatching and in the adult; slow muscle was studied in 13-day embryos through hatching and in the adult.Tissue Culture. For explant cultures, muscles were dissected from chicken embryos ofthe required age, ...

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Section: Resultsmentioning

confidence: 99%

Myosin light chains and the developmental origin of fast muscle.

Stockdale¹,

Raman²,

Baden³

1981

Proc. Natl. Acad. Sci. U.S.A.

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“…Also, the influence of innervation on satellite cell activity is not well understood. Denervation of immature chicken muscles blocks proliferation of myoblasts 9,10 ; satellite cells vanish in neonatally denervated rat muscles. 19,35,36 Denervation of adult muscles of rats and mice initially causes proliferation of connective tissue and satellite cells.…”

Section: Accepted 16 November 1999mentioning

confidence: 98%

Dynamics of nuclei of muscle fibers and connective tissue cells in normal and denervated rat muscles

2000

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“…For example, it has been shown in chick muscle, using the clonal analysis that both the ability of myoblasts to fuse in vitro, and the morphology of myotubes, appear to be regulated by neural contact within the limb bud (11,12). Similarly, Koenig and Vigny (70) observed that myotubes in primary rat muscle cultures could make 16S acetylcholinesterase (AChE) in the absence of nerves only if derived from embryonic muscles that had already been innervated; myotubes formed by cells from uninnervated muscles could make 16S AChE only if co-cultured with nerves.…”

Section: IImentioning

confidence: 99%

Differentiation of skeletal muscle cells in culture.

Inestrosa

1982

Cell Struct. Funct.

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Nerve-dependent changes in clonable myoblast populations

Cited by 49 publications

References 15 publications

Myosin light chains and the developmental origin of fast muscle.

Myosin light chains and the developmental origin of fast muscle.

Dynamics of nuclei of muscle fibers and connective tissue cells in normal and denervated rat muscles

Differentiation of skeletal muscle cells in culture.

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