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• W179637409 abstract "Rat cardiac ventricular myosins were obtained from fetuses, from young, adult, and old normal animals, from hypophysectomised adults and from rats submitted to a chronic mechanical overload of the heart. The different proteins were compared by electrophoresis in non-denaturing conditions and by competitive enzymelinked immunosorbent assay (EL.ISA). For the latter purpose, antibodies specific of the rat cardiac V3 isomyosin were used. It was found that the V3 isomyosin of fetuses is indistinguishable from that of adult hypertrophied heart. This result strongly suggests that adaptation to chronic increase in cardiac work is mediated through the synthesis of the fetal form of myosin. Double immunolabeling of isolated myocytes with antibodies specific of the rat V1 or the rat V3 isomyosins showed that this isoenzymic redistribution occurs throughout the whole length of the myocytes, without any preferential localization of the newly synthesized V3 isoform. The existence of such a mechanism of adaptation was also searched for in human hearts. Competitive ELISA performed with antibodies against human cardiac heavy meromyosin indicated no differences in apparent affinities with the myosins of two “control” subjects and of three patients with noticeable cardiac hypertrophy." @default.
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• W179637409 date "1983-01-01" @default.
• W179637409 modified "2023-09-27" @default.
• W179637409 title "Myosin isoenzymic distribution in hyperthrophied rat and human hearts" @default.
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• W179637409 doi "https://doi.org/10.1007/978-3-642-85326-5_15" @default.
• W179637409 hasPublicationYear "1983" @default.
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