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  • 1
    Digitale Medien
    Digitale Medien
    Springer
    Acta neuropathologica 80 (1990), S. 618-623 
    ISSN: 1432-0533
    Schlagwort(e): mdx and control mice muscles ; Dystrophin ; Quick-freeze, deep-etch, rotary-shadow replica ; Muscle plasma membrane-associated cytoskeletons
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Summary The Duchenne muscular dystrophy gene product “dystrophin” is a sarcolemma-associated cytoskeleton which is present just inside the sarcolemma. We investigated the ultrastructure and the relationship of this cytoskeleton to the muscle plasma membrane by immunoelectron microscopy and freeze-etch electron microscopy of liquid helium-frozen fresh muscles. The immunoelectron microscopy of the extensor digitorum longus muscles of six mdx mice and six control mice showed the location of anti-dystrophin antibody along the muscle plasma membrane undercoat of all the muscle samples from the control mice without any antibody reaction in the mdx mice muscles. Fresh extensor digitorum longus muscles of seven mdx and six control mice were quick-frozen in liquid helium in the rapid-freeze device. High-magnification electron microscopy of the deep-etch, rotary-shadow replicas of the frozen muscles showed the network formation and attachment of individual rod-shaped cytoskeletons of variable size to the cytoplasmic surface of the muscle plasma membrane in both mdx mice and control mice. The length of cytoskeletons attached to the muscle plasma membranes was measured and mean length±SE in mdx mice and control mice were 98±4 nm and 101±3 nm, respectively. Although these values were not statistically different (P〉0.1), the distribution frequency of 130–150 nm muscle plasma membrane-associated cytoskeletons was 7.9% in mdx mice versus 14.5% in control mice. Since the predicted length of dystrophin is 125–150 nm, the 130- to 150-nm plasma membrane-associated cytoskeletons of mdx control mice may include dystrophin.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    ISSN: 1432-0533
    Schlagwort(e): Key words Aciculin ; Dystrophin ; Binding site ; Normal and dystrophic muscles ; Ultrastructural ¶localization
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract Aciculin is a novel adherens junction antigen extracted from human uterine smooth muscle that is reported to associate biochemically with dystrophin. We attempted to determine (i) the immunostainability of anti-aciculin antibody for the 6 histochemically normal human muscles and seven muscles from boys with Duchenne muscular dystrophy(DMD) and 11 disease control muscles, (ii) the ultrastructural localization of aciculin in normal skeletal myofibers, (iii) aciculin’s spacial relationship with dystrophin and β-spectrin, and (iv) if the aciculin is ultrastructurally colocalized with dystrophin, the distance from the aciculin epitope to the epitope of the dystrophin N- or C-terminal domain. For this, rabbit anti-aciculin antibody was generated against the synthetic peptide of aciculin fragment D [4]. Immunohistochemical staining showed that the immunostainability of DMD muscles for anti-aciculin antibody was markedly decreased as compared with normal and disease control muscles. Single and double immunogold labeling electron microscopy of 6 histochemically normal human quadriceps femoris muscles revealed that aciculin was present along the inner surface of muscle plasma membrane and that aciculin formed doublets more frequently with dystrophin (23.5 ± 1.8%; group mean ± SE) than with β-spectrin (12.8 ± 1.1%; P 〈 0.01 two tailed t test). Rabbit anti-aciculin antibody frequently formed doublets with monoclonal antibodies against the N- or C-terminal domain of dystrophin at the muscle cell surface. These results suggest that aciculin is associated with dystrophin and may interact with both the N- and C-terminal domains of dystrophin.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    Springer
    Acta neuropathologica 82 (1991), S. 178-184 
    ISSN: 1432-0533
    Schlagwort(e): mdx and control mice muscles ; Quick-freeze, deep-etch, rotary-shadow replica ; Gold-labelled dystrophin ; Shape of dystrophin molecule
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Summary The Duchenne muscular dystrophy product ‘dystrophin’ has been shown to be located at the inner surface of normal muscle plasma membrane. This study was undertaken to visualize the shape of dystrophin molecules and their topographical distribution at the inner surface of murine skeletal muscle plasma membrane. The immunogold electron microscopy of plastic-embedded quadriceps femoris muscles of six mdx mice and six control mice showed the presence of gold particles along the muscle plasma membrane undercoat of all muscle samples from the control mice without any antibody reaction in the mdx mice muscles. The gold-labelled muscles of six mdx and six control mice were quickly frozen by liquid helium in a rapid-freeze apparatus. High magnification electron microscopy of the quick-freeze, deep-etch, rotary-shadow replicas of the gold-labelled muscles demonstrated the presence of dystrophin molecules associated with gold particles at the cytoplasmic surface of mdx control mice. The dystrophin molecules displayed a variety of shapes, such as rods with a reduction in diameter from one end to the other end and/or with the enlargement of their end(s). These dystrophin molecules were incorporated in the meshowork of muscle plasma membrane-associated cytoskeletons.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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