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  • 1
    Electronic Resource
    Electronic Resource
    Vital labelling of somite-derived myogenic cells in the chicken limb bud (1991)
    Springer
    Development genes and evolution 200 (1991), S. 188-192 
    Details
    ISSN: 1432-041X
    Keywords: Myogenesis ; Migration ; Muscle ; Vital staining ; Limb morphogenesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary In order to understand how myogenic cells migrate in the limb bud, it is indispensable to distinguish undifferentiated myogenic cells from other mesenchymal cells. Thus, a suitable method for this purpose has been sought. A method to exchange the somites of a chicken and a quail microsurgically has widely been used, since the nuclei of the two species are morphologically distinguishable. However, microsurgery is accompanied by disturbances at the operated locus, and introducing cells of different species might induce unexpected effects. We report a new method for labelling chicken myogenic cells without transplantational operations, and describe their migration pattern in limb buds. Injection of a fluorescent carbocyanine dye into the somite lumen intensely labelled the somitic cells. Myogenic cells derived from the somite were clearly detected in limb buds. Before stage 20, the labelled cells were diffusely distributed in the proximal region of the limb bud. At about stage 21 in both wing and leg buds, labelled cells began to form dorsal and ventral masses. The label was followed until the cells differentiated and expressed myosin. This vital labelling method has advantages over the somite transplantation method: it does not include surgical operations that may disturb the normal development, and the cells are labelled intensely enough to be detected in a whole mount preparation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00361336
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  • 2
    Electronic Resource
    Electronic Resource
    Mutations in the integrin α7 gene cause congenital myopathy (1998)
    [s.l.] : Nature Publishing Group
    Nature genetics 19 (1998), S. 94-97 
    Details
    ISSN: 1546-1718
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] The basal lamina of muscle fibers plays a crucial role in the development and function of skeletal muscle. An important laminin receptor in muscle is integrin α7β1D. Integrin β1 is expressed throughout the body, while integrin α7 is more muscle-specific1–5. To address ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/ng0598-94
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  • 3
    Electronic Resource
    Electronic Resource
    β–sarcoglycan (A3b) mutations cause autosomal recessive muscular dystrophy with loss of the sarcoglycan complex (1995)
    [s.l.] : Nature Publishing Group
    Nature genetics 11 (1995), S. 266-273 
    Details
    ISSN: 1546-1718
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] The dystrophin associated proteins (DAPs) are good candidates for harboring primary mutations in the genetically heterogeneous autosomal recessive muscular dystrophies (ARMD). The transmembrane components of the DAPs can be separated into the dystroglycan and the sarcoglycan complexes. Here we ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/ng1195-266
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  • 4
    Electronic Resource
    Electronic Resource
    Creatine kinase, cell membrane and Duchenne muscular dystrophy (1999)
    Springer
    Molecular and cellular biochemistry 190 (1999), S. 143-151 
    Details
    ISSN: 1573-4919
    Keywords: dystrophin ; dystroglycans ; sarcoglycans
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract In 1958 Professor Setsuro Ebashi found that serum creatine kinase activity is increased in patients suffering from various muscular dystrophies, especially Duchenne muscular dystrophy (DMD). He and others proposed that creatine kinase passes through the cell membrane as it is released from DMD muscle fibers. Since then, it has been found that dystrophin and dystrophin-associated proteins are connected to several other components, including the basal lamina and subsarcolemmal cytoskeletal networks on the cell membrane, while dystrophin anchors these dystrophin-associated proteins to the actin filaments inside the muscle cell. In DMD muscle, dystrophin has been found to be absent and dystroglycans and sarcoglycans decreased. However, how creatine kinase molecules can pass through the DMD muscle cell membrane still remains unanswered. On the basis of recent findings on the structure of the protein layers which sandwich the lipid bilayer of muscle cell membranes, this essay stresses the importance of these lipid bilayers in protecting creatine kinase release from protoplasma in normal muscle. It further indicates the possibility that the absence of dystrophin in DMD muscle during muscle contraction may result in temporal damage to the lipid bilayer.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006974613418
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  • 5
    Electronic Resource
    Electronic Resource
    Immunostaining of skeletal and cardiac muscle surface membrane with antibody against Duchenne muscular dystrophy peptide (1988)
    [s.l.] : Nature Publishing Group
    Nature 333 (1988), S. 861-863 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The sequence of the synthetic peptide (DMDP) used to raise the antiserum we describe is derived from the DMD complementary DNA (cDNA) clone, position 1,526 to 1,675. Our preliminary results with this antiserum suggested that the protein encoded by the DMD gene is localized at the surface membrane ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/333861a0
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  • 6
    Electronic Resource
    Electronic Resource
    Developmental expression of dystrophin on the plasma membrane of rat muscle cells (1989)
    Springer
    Protoplasma 151 (1989), S. 11-18 
    Details
    ISSN: 1615-6102
    Keywords: Duchenne muscular dystrophy ; Dystrophin ; Muscle cell differentiation ; Muscle cell growth ; Primary myotubes ; Secondary myotubes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The Duchenne muscular dystrophy gene product dystrophin has been shown to be located on the inside of the plasma membrane. We investigated the developmental expression of dystrophin on rat skeletal muscle plasma membrane with the antiserum raised against a fragment of the polypeptide predicted from the human dystrophin cDNA map [Koenig et al. (1987) Cell 50: 509–517]. Plasma membrane of primary myotubes of the extensor digitorum longus (EDL) muscle was not initially stained by the antiserum; staining began at day 19 of embryonic life, and plasma membrane of all polynuclear muscle cells including secondary myotubes was uniformly stained by day 5 after birth. These immunohistochemical findings were supported by immunoblot analysis. These results indicate that plasma membrane of myotubes at their first appearance is not lined with dystrophin at the detectable level but becomes lined as their development proceeds.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01403297
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  • 7
    Electronic Resource
    Electronic Resource
    Expression of dystrophin on the cell surface membrane of intrafusal fibers of human skeletal muscle (1989)
    Springer
    Protoplasma 152 (1989), S. 109-111 
    Details
    ISSN: 1615-6102
    Keywords: Duchenne muscular dystrophy ; Dystrophin ; Muscle spindle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We examined the morphological expression of dystrophin in the intrafusal muscle fibers in skeletal muscle from normal human and Duchenne muscular dystrophy (DMD) patients, using antisera against the N-terminal and C-terminal regions of dystrophin. The intrafusal fibers of normal muscle express dystrophin on their cell surface membrane, but those of DMD muscle do not.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01323069
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  • 8
    Electronic Resource
    Electronic Resource
    Class specificity of transferrin as a muscle trophic factor (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 126 (1986), S. 341-351 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The specificity of transferrin (Tf) in its exertion of a growth-promoting effect on myogenic cells was examined using serum Tfs from chick, dove, goose, turkey, bovine, horse, rabbit, rat, and swine and primary myogenic cells from chick, duck, quail, rabbit, and rat, and rat L6 cells. Avian Tfs were effective on avian cells but not on mammalian cells, while mammalian Tfs were effective on mammalian cells but not on avian cells. Dove and bovine Tfs were exceptional in that they were effective on some class-heterologous cells at higher concentrations and less so or completely ineffective on some class-homologous cells. Despite these exceptions, however, the relationship between Tfs and cells can be summarized as a class specificity.To exert the growth-promoting effect, it is prerequisite for Tf to bind its specific receptor on the cell surface. Using quail and L6 cells, we found that the binding of 125I-labeled chick and rat Tfs to the respective receptors of quail and L6 myoblasts was competitively inhibited by other kinds of effective Tfs, but not by ineffective ones.We conclude that the class specificity in myotrophic activity of Tf is due to the affinity between Tf and Tf receptor.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041260304
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  • 9
    Electronic Resource
    Electronic Resource
    Necessity of transferrin for RNA synthesis in chick myotubes (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 127 (1986), S. 349-356 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Chick transferrin (Tf) is essential not only for growth and differentiation but also for the maintenance of chick myotubes in culture. Its removal from the culture medium gives rise to degeneration of the myotubes. The analysis of this process revealed that the removal resulted in decrease in total and messenger RNA content in the myotubes; this was mainly due to a decrease in RNA synthesis. Activity of in vitro RNA synthesis in isolated nuclei from myotubes cultured without Tf was lower than the activity in nuclei from myotubes cultured with Tf and increased with the addition of FeCl3. Although RNA degradation in myotubes was also enhanced following Tf removal, the degree was small. The synthesis of most proteins was reduced. In contrast to this, a few new proteins of unknown nature were synthesised in myotubes cultured in Tf-free medium.The role of Fe ion carried into the cells by Tf in promoting myogenic cell growth and differentiation and in preventing the myotubes from degeneration can be explained, at least in part, on the basis of its effect on RNA synthesis.Since we have found that Fe is required for activation of RNA polymerase purified from embryonic muscles (Shoji and Ozawa, 1985b), these effects may be ascribed to this activating effect.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041270302
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  • 10
    Electronic Resource
    Electronic Resource
    Caffeine contracture in the cultured chick myotube (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 129 (1986), S. 289-294 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A possible function of Ca store site in cultured chick myotubes was examined by recording contraction of the myotube with special reference to the effect of caffeine. Caffeine at low concentrations (below 1 mM), applied focally on the myotube through a micropipette with a pressure pulse, elicited focal contraction without membrane potential changes. Procaine inhibited the caffeine contracture. Deuterium oxide also inhibited the caffeine contracture at low concentrations, but enhanced the maximal contracture. These observations are Similar to those in the mature frog muscle fiber in which the sarcoplasmic reticulum (SR) is a main site of caffeine action. On the basis of these similarities, it was considered that caffeine acts on SR to elicit contracture in the myotube. The ability of SR to accumulate and release Ca ion seemed to be low, because caffeine contracture decreased or disappeared in a Ca-free solution in many myotubes.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041290304
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