Expression of myosin isoenzymes in cardiac-muscle cells in culture

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Expression of myosin isoenzymes in cardiac-muscle cells in culture.

Myosin isoenzyme profiles of rat and chicken embryonic cardiac myocytes were studied during differentiation and growth in vitro by native-gel electrophoresis and assay of Ca2+-activated ATPase. The electrophoretic pattern of myosin extracted from 18-day-embryonic-rat myocytes after 7 days in culture exhibits three isoenzyme bands, V1, V2 and V3, of which the slow-migrating V3 is predominant. Th...

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Cardiac Muscle Cells in Culture

The effect of amiodarone on the expression of myosin isoforms and the growth of neonatal rat cardiac muscle cells in culture was studied by native gel electrophoresis, assays of DNA and protein synthesis, and electron microscopy. Cardiac myocytes exposed to amiodarone in the absence of triiodothyronine (T3) showed predominant V1. When cardiac myocytes were exposed to amiodarone in the presence ...

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Fractional synthesis rates in vivo of skeletal-muscle myosin isoenzymes.

The synthesis rates of different myosin isoenzymes in a single muscle, and of the same isoenzymes in different muscles (soleus, masseter and plantaris), were measured. The rate of total protein synthesis was significantly higher in the soleus [greater than 95% slow myosin (SM)] than in the plantaris [greater than 95% fast myosin (FM)]. Two fast isoenzymes, FM2 and FM3, were synthesized at diffe...

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Developmental regulation of myosin gene expression in mouse cardiac muscle

Expression of the two isoforms of cardiac myosin heavy chain (MHC), MHC alpha and MHC beta, in mammals is regulated postnatally by a variety of stimuli, including serum hormone levels. Less is known about the factors that regulate myosin gene expression in rapidly growing cardiac muscle in embryos. Using isoform-specific 35S-labeled cRNA probes corresponding to the two MHC genes and the two myo...

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Changes in skeletal-muscle myosin isoenzymes with hypertrophy and exercise.

The patterns of myosin isoenzymes in fast- and slow-twitch muscles of the rat hindlimb were studied, by pyrophosphate/polyacrylamide-gel electrophoresis, with hypertrophy (induced by synergist removal) and with spontaneous running exercise of 4 and 11 weeks duration. At 11 weeks, changes with hypertrophy in the slow-twitch soleus, composed of greater than 95% SM2 (slow myosin 2) in normal muscl...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1984

ISSN: 0264-6021,1470-8728

DOI: 10.1042/bj2210021