PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “Muscle Development”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 343 records · Page 19Linked to original sources

Chick and quail limb bud myoblasts, isolated at different times during muscle development, express stage-specific phenotypes when differentiated in culture.

Evidence is presented which shows that myoblasts, isolated at different stages during chick and quail limb bud development, will form, in culture, myotubes which can be distinguished with a combination of morphological as well as biochemical criteria. Hind limb bud myoblasts isolated from 5-day-old embryos form very short myotubes which synthesize a myosin, the light chains of which are predominantly LC1F and LC2S. Myoblasts isolated from the limb buds of 7-8-day-old embryos form large myotubes which synthesize a myosin the light chains of which are predominantly LC1F, LC2S and LC2F. Myoblasts isolated from the thigh muscle of embryos older than 10 days form large myotubes which synthesize a myosin the light chains of which are predominantly LC1F and LC2F. These results have been confirmed by hybridization of the cellular mRNA with a molecular probe specific for LC2F. These results lead us to suggest the existence of at least two classes of myoblasts which appear at different times during limb bud development. The first class, or 'early' myoblasts, is present in the limb buds of 5-day-old embryos, whereas the second class, or 'late' myoblasts, is present in the muscles of embryos older than 8 days. This result, however, is also compatible with the hypothesis that all muscle cells are the same at all times during development, and that the different phenotypes simply reflect differences in the environmental conditions.

Animals↗

Scanning electron microscopy of human prenatal muscle development.

A scanning electron microscopic study of the development of the human quadriceps was performed in 30 fetuses ranging from 6 to 40 weeks gestation. The results clearly illustrate the hyperplastic phase of myogenesis, showing the differentiation, multiplication and fusion of the myoblasts and the subsequent formation of different generations of myotubes. The myoblasts decrease relatively in number within the developing quadriceps until the 19th week of gestation, and remain afterwards as quiescent satellite cells. The maturation of the myotubes to myofibers and the metabolic differentiation of the fibers are not accompanied by significant changes in their external form in terms of scanning electron microscopy. The hypertrophic phase of myogenesis and general fetal growth can be followed with scanning electron microscopy by the increase in size of the fibers or bundles of fibers, as well as by the differentiation of the connective tissue components of the muscle.

Embryonic and Fetal Development↗

Ultrastructure of developing muscle in the upper limbs of the human embryo and fetus.

BACKGROUND: The ultrastructure of the myogenesis, which proceeds along with the appearance of muscle-specific proteins and isozymes, has not been fully described in the upper limb of staged human embryos. METHODS: Eight human embryos (Carnegie stage 14-22) and two fetuses (11 and 12 weeks of gestation) were fixed with 5% glutaraldehyde, 4% paraformaldehyde, and 0.2% picric acid in 0.1 M phosphate buffer, pH 7.2. The upper limbs were dissected out and processed for transmission electron microscopy, and sections of the biceps brachii muscle were cut and examined. RESULTS: At stage 14, the myoblasts were loosely scattered in the ventral proximal region of the upper limb bud and had a small amount of cytoplasm with a few intracellular organelles. At stage 16, the myoblasts were spindle shaped and oriented parallel to the axis of the upper limb bud. These cells had irregularly shaped nuclei with prominent nucleoli, rough endoplasmic reticulum (ER), and mitochondria, but no myofilaments were observed. At stages 17-19, rough ER, free ribosomes, and mitochondria increased in number and thick and thin filaments with faint Z-lines appeared in the peripheral cytoplasm of the myotube. The plasma membranes of some neighboring myotubes were continuous, suggesting that these cells were in the initial stages of the fusion process. At stage 22, the striated pattern of the myofilaments became evident and tubular structures appeared around them and near the plasma membrane. In the fetus at the 11th week, the basal lamina began to surround the myotubes, and T-tubules with sarcoplasmic reticulum were observed. Dyads and triads were observed in the myotube of the 12th week fetus. CONCLUSION: These findings suggest that rapid myogenesis occurs during the late embryonic period in human upper limbs and that the ultrastructural characteristics of mature myotubes are established during the early fetal period.

Arm↗

[Changes in creatine kinase activity and protein spectrum of the developing muscle culture treated with creatine phosphate].

A study was made of the influence of creatine phosphate (CP) on creatine kinase activity and the total protein status of the primary chicken myoblast culture. It has been established that the two-hour exposure of the developing culture in the presence of 2 and 4 mM CP is accompanied by the lowering of the content of water extractable protein and a considerable increase of creatine kinase activity. Meanwhile the total activity of the enzyme rises in the non-differentiated and falls in the differentiated one. Electrophoretic analysis has shown CP to produce not only quantitative but also deep qualitative changes in the myoblast protein spectrum. It is assumed that the changes revealed are nonspecific.

Animals↗

A C. elegans E/Daughterless bHLH protein marks neuronal but not striated muscle development.

The E proteins of mammals, and the related Daughterless (DA) protein of Drosophila, are ubiquitously expressed helix-loop-helix (HLH) transcription factors that play a role in many developmental processes. We report here the characterization of a related C. elegans protein, CeE/DA, which has a dynamic and restricted distribution during development. CeE/DA is present embryonically in neuronal precursors, some of which are marked by promoter activity of a newly described Achaete-scute-like gene hlh-3. In contrast, we have been unable to detect CeE/DA in CeMyoD-positive striated muscle cells. In vitro gel mobility shift analysis detects dimerization of CeE/DA with HLH-3 while efficient interaction of CeE/DA with CeMyoD is not seen. These studies suggest multiple roles for CeE/DA in C. elegans development and provide evidence that both common and alternative strategies have evolved for the use of related HLH proteins in controlling cell fates in different species.

Amino Acid Sequence↗

GLUT4 heterozygous knockout mice develop muscle insulin resistance and diabetes.

GLUT4, the insulin-responsive glucose transporter, plays an important role in postprandial glucose disposal. Altered GLUT4 activity is suggested to be one of the factors responsible for decreased glucose uptake in muscle and adipose tissue in obesity and diabetes. To assess the effect of GLUT4 expression on whole-body glucose homeostasis, we disrupted the murine GLUT4 gene by homologous recombination. Male mice heterozygous for the mutation (GLUT4 +/-) exhibited a decrease in GLUT4 expression in adipose tissue and skeletal muscle. This decrease in GLUT4 expression did not result in obesity but led to increased serum glucose and insulin, reduced muscle glucose uptake, hypertension, and diabetic histopathologies in the heart and liver similar to those of humans with non-insulin-dependent diabetes mellitus (NIDDM). The male GLUT4 +/- mice represent a good model for studying the development of NIDDM without the complications associated with obesity.

Animals↗

A myogenic switch. Muscle development.

Experiments manipulating the level of the basic helix-loop-helix transcription factor Twist in the Drosophila embryo have revealed a novel role for this protein in a 'myogenic switch' during early development.

Amino Acid Sequence↗

Insulin-like growth factors (IGF) in muscle development. Expression of IGF-I, the IGF-I receptor, and an IGF binding protein during myoblast differentiation.

The insulin-like growth factors (IGFs) I and II exert pleiotropic effects on diverse cell types through interaction with specific high affinity cell surface receptors and with locally produced binding proteins. In skeletal muscle and in myoblast cell lines, the functions of IGF-I and -II are complex. Both growth factors appear capable of stimulating cellular proliferation and differentiation, as well as exerting insulin-like effects on intermediary metabolism. We have demonstrated recently that the expression of IGF-II and its receptor is induced during the terminal differentiation of the myoblast cell line, C2, and have suggested that IGF-II may be an autocrine growth factor in these cells (Tollefsen, S.E., Sadow, J.L., and Rotwein, P. (1989) Proc. Natl. Acad. Sci. U.S.A. 86, 1543-1547). We now have examined this cell line for expression of other components involved in IGF signaling. The synthesis of IGF-I is low during myoblast proliferation; IGF-I mRNA can be detected only through use of a sensitive solution hybridization assay. Typical IGF-I receptors can be measured in myoblasts, whereas IGF binding proteins cannot be detected in proliferating cells or in conditioned culture medium. During myogenic differentiation, IGF-I mRNA levels increase transiently by 6-10-fold within 48-72 h. The expression of IGF-I mRNA is accompanied by a 2.5-fold accumulation of IGF-I in the culture medium. IGF-I receptors also increase transiently, doubling by 48 h after the onset of differentiation. By contrast, secretion of a Mr 29,000 IGF binding protein is induced 30-fold to 100 ng/ml within 16 h and continues to increase throughout differentiation. These studies demonstrate that several components critical to IGF action are produced in a fusing skeletal muscle cell line in a differentiation-dependent manner and suggest that both IGF-I and IGF-II may be autocrine factors for muscle.

Amino Acid Sequence↗