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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 3 (1983), S. 431-438 
    ISSN: 0886-1544
    Keywords: myotendinous junction ; laminin ; type IV collagen ; heparan sulfate proteoglycan ; alpha actinin ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The muscle-tendon junction of murine skeletal muscles has been analyzed by a variety of extraction techniques, by myosin subfragment-1 binding experiments, and by ultrastructural immunocytochemistry. The results indicate that the muscle-tendon junction is composed of four distinct domains: an intracellular domain, the internal lamina; a domain connecting the internal lamina with the lamina densa of the external lamina, the connecting domain; the lamina densa; and a domain which attaches the lamina densa to the collagen fibers, the matrix. Each of these domains is distinct with respect to position, three-dimensional organization, and molecular composition, and is therefore considered to have a unique role in the transmission of contractile force.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 207 (1983), S. 573-591 
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The force generated within skeletal muscle fibers of vertebrates is transmitted to the tendon at the muscle-tendon junction. Ultrastructural analysis of the murine muscle-tendon junction following a variety of experimental manipulations has produced evidence that the muscle-tendon junction can be described in terms of four principal domains (Trotter and Eberhard, 1983), two of which are discussed in the present report. Each domain is defined by the shape and orientation of its principal components, and by its position with respect to the plasma membrane. The internal lamina is composed of actin filaments, with a center to center spacing of approximately 12 nm, oriented mainly parallel to the principal vector of contractile force, and to the plasma membrane. These filaments are cross-linked into a structural unit, perhaps by the electron-dense structures which are associated with them. The internal lamina is morphologically connected to the external lamina (lamina densa) by a population of fine filaments oriented approximately perpendicular to the principal vector of contractile force. These filaments which constitute the connecting domain, are approximately 2-8 nm in diameter and are at least 50 nm long. They pass through three separate regions: the sarcoplasm between the internal lamina and the plasma membrane; the plasma membrane proper; and the extracellular space between the plasma membrane and the lamina densa. This third region is often referred to as the lamina lucida. These filaments are composed of at least three separate components in series, linked together by noncovalent interactions. The existence of these discrete structural domains implies that each has a different molecular composition and different mechanical properties.
    Additional Material: 15 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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