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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 588 (1990), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-119X
    Keywords: Cytoskeleton Desmin knock-out mice Intermediate filament-associated proteins Myotendinous junctions Neuromuscular junctions
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Mice lacking the gene encoding for the intermediate filament protein desmin have a surprisingly normal myofibrillar organization in skeletal muscle fibers, although myopathy develops in highly used muscles. In the present study we examined how synemin, paranemin, and plectin, three key cytoskeletal proteins related to desmin, are organized in normal and desmin knock-out (K/O) mice. We show that in wild-type mice, synemin, paranemin, and plectin were colocalized with desmin in Z-disc-associated striations and at the sarcolemma. All three proteins were also present at the myotendinous junctions and in the postsynaptic area of motor endplates. In the desmin K/O mice the distribution of plectin was unaffected, whereas synemin and paranemin were partly affected. The Z-disc-associated striations were in general no longer present in between the myofibrils. In contrast, at the myotendinous and neuromuscular junctions synemin and paranemin were still present. Our study shows that plectin differs from synemin and paranemin in its binding properties to the myofibrillar Z-discs and that the cytoskeleton in junctional areas is particularly complex in its organization.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 29 (1994), S. 312-320 
    ISSN: 0886-1544
    Keywords: contractile ring ; cleavage furrow ; mitosis ; unconventional myosin ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: During cytokinesis, daughter cells are cleaved in two by the constriction of an actin-rich contractile ring which encircles the equator of the dividing cell. Filamentous myosin II is present in the contractile ring and necessary for constriction of the furrow, as shown in several cell types [Satterwhite and Pollard, 1992: Curr. Opin. Cell Biol. 4:43-52]. However, no functional role nor distinctive localization has been previously identified for non-filamentous “unconventional” myosins, such as myosin I, during cytokinesis. Using antibodies to adrenal medullary myosin I, we report that myosin I is localized in 3T3 fibroblasts to the mid-equatorial plane during late-cytokinesis, as well as to the polar edges as previously described in ameboid cells [Fukui et al., 1989: Nature 341:328-331]. Confocal microscopy revealed that myosin I is concentrated at the midbody region in a nearly continuous transverse disk, extending from the cortical region of the furrow through the midbody itself. These findings suggest that, in addition to the accepted role of filamentous myosin II in constriction of the contractile ring, non-filamentous myosin I might contribute to motile events occurring late in cytokinesis. © 1994 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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