Chicken cardiac myofibrillogenesis studied with antibodies specific for titin and the muscle and nonmuscle isoforms of actin and tropomyosin |
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Authors: | Susan E Handel Marion L Greaser Edward Schultz Seu-Mei Wang Jeannette C Bulinski Jim J -C Lin James L Lessard |
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Institution: | (1) Muscle Biology Laboratory, University of Wisconsin-Madison, 53706 Madison, WI, USA;(2) Department of Anatomy, University of Wisconsin-Madison, 53706 Madison, WI, USA;(3) Department of Anatomy and Cell Biology, Columbia University, 10032 New York, NY, USA;(4) Department of Biology, University of Iowa, 52242 Iowa City, IA, USA;(5) Division of Basic Research, Childrens Hospital Research Foundation, 45229 Cincinnati, OH, USA;(6) Present address: Department of Human Anatomy and Cell Biology, University of Liverpool, Liverpool, UK;(7) Present address: Department of Anatomy, National Taiwan University, Taipei, Taiwan;(8) University of Wisconsin, 1805 Linden Drive West, 53706 Madison, WI, USA |
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Abstract: | Summary Myofibrillogenesis was studied in cultured chick cardiomyocytes using indirect immunofluorescence microscopy and antibodies against - and -actin, muscle and nonmuscle tropomyosin, muscle myosin, and titin. Initially, cardiomyocytes, devoid of myofibrils, developed variable numbers of stress fiber-like structures with uniform staining for anti-muscle and nonmuscle actin and tropomyosin, and diffuse, weak staining with anti-titin. Anti-myosin labeled bundles of filaments that exhibited variable degrees of association with the stress fiber-like structures. Myofibrillogenesis occurred with a progressive, and generally simultaneous, longitudinal reorganization of stress fiber-like structures to form primitive sarcomeric units. Titin appeared to attain its mature pattern before the other major contractile proteins. Changes in the staining patterns of actin, tropomyosin, and myosin as myofibrils matured were interpreted as due to longitudinal filament alignment occurring before ordering in the axial direction. Non-muscle actin and tropomyosin were found with sarcomeric periodicity in the initial stages of sarcomere myofibrillogenesis, although their staining patterns were not identical. The localization of the sarcomeric proteins -actin and muscle tropomyosin in stress fiber-like structures and the incorporation of non-muscle proteins in the initial stages of sarcomere organization bring into question the meaning of sarcomeric proteins in regard to myofibrillogenesis. |
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Keywords: | Fibrillogenesis Muscle cardiac Myosin Actin Immunofluorescence microscopy Myofibrils Domestic fowl |
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