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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Anatomy and embryology 176 (1987), S. 183-189 
    ISSN: 1432-0568
    Keywords: Epicardium ; Development ; Heart ; Mouse embryo ; Scanning electron microscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The formation of the epicardium was investigated in the mouse embryo using scanning electron microscopy (SEM) in order to establish a three-dimensional perspective concerning epicardial development in mammals. The epicardium first appears as aggregates of cells scattered on the caudal surface of the ventricle and atria where these regions face the septum transversum in a 9-day-old embryo. These aggregated cells seem to have originated from the mesothelial projections extending from the surface of the septum transversum. Then, the cells of each aggregate flatten, subsequently fusing with each other to form a continuous sheet of epicardium. The fusion of aggregates proceeds in a cranial direction. Finally, the bulbus cordis and truncus arteriosus become invested by migrating cells at the cranial end of the epicardial sheet about 11 days after fertilization. The present observations are discussed in comparison with those made previously in avian embryos.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-0878
    Keywords: Key words Myofibrillar proteins ; Myotome ; Nerve ; Acetylcholine receptor ; Chicken embryo
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  Fluorescence microscopy of chicken cervical somites revealed that muscle-specific proteins began to appear at stage 11 (Hamburger and Hamilton numbering), and the onset of the expression of all the proteins examined in the present study had occurred by stage 17. Muscle proteins were classified into six groups according to the stage of their appearance. Since all these proteins were expressed before emergence of nerve fibers in myotomes, switching-on of their synthesis does not seem to require neuronal influence. However, since isoproteins other than adult muscle types disappeared and diversification of muscle fiber types occurred coordinately with the clustering of acetylcholine receptors in cervical muscles, switching-off of the synthesis of the nonadult isoforms might have been accelerated by the formation of functional neuromuscular junctions. The absence of nebulin and C-protein in early stages seems to indicate that these proteins are not required for the initial assembly of myofilaments and/or myofibrils. Further, this absence might be considered to facilitate exchangeabilities of proteins in nascent myofibrils, thereby changing the isoforms to adult types.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1058-8388
    Keywords: Cardiac myocyte ; Development ; Myofibril ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Immunogold electron microscopy of cardiac myocytes microinjected with biotin-labeled actin showed that gold labeling was first found around the A band level of myofibrils at their proximal parts. This observation suggests that polymerization of actin and/or the addition of newly formed actin filaments occurs preferentially in association with myosin filaments to increase the myofibrillar girth. At the distal portions of developing myofibrils, their terminal ends were initially labeled, suggesting that continued reorganization and/or de novo formation of myofibrils occurs at these locations. Soon, gold particles were seen along the termini of growing myofibrils. This appears to indicate that actin subunits are added at the membrane-associated ends of preexisting actin filaments to increase the length of myofibrils. Adhesion plaque proteins, e.g., vinculin, do not appear to play any role in assembling actin monomers at these sites on the inner surface of the sarcolemma.Immunofluorescence and immunoelectron microscopy of cardiomyocytes double-stained with antibodies against two distant domains of connecttin (titin) filaments and other sarcomeric proteins showed that these domains of connectin filaments and myosin were synthesized almost simultaneously on large polyribosomes and/or associated immediately after the synthesis of these molecules. Connectin and myosin bands were formed after α-actinin striations (Z bands) were seen on preformed I-Z-I-like structures. The observation that the development and distribution of connectin were tightly linked with those of myosin suggests the possible role of connectin for integrating myosin filaments with the early formed I-Z-I complexes of myofibrils. © 1993 wiley-Liss, Inc.
    Additional Material: 15 Ill.
    Type of Medium: Electronic Resource
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