Abstract
The inducibility of several rat skeletal muscle proteins was examined in heterokaryons formed by fusing differentiated chick myocytes to undifferentiated rat myoblasts. Chicken and rat proteins were distinguished using species-specific antibodies or by their different migrations in polyacrylamide or agarose gels. Both rat skeletal myosin light chain 1 and rat α-tropomyosin were induced in the heterokaryons. In contrast, neither rat acetylcholine receptors nor creatine kinase could be detected. These results suggest that chick myocytes may contain quantities of regulatory factors that are sufficient for the activation of some but not all of these rat muscle-specific proteins within the cellular context of the heterokaryon.
Original language | English (US) |
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Pages (from-to) | 113-122 |
Number of pages | 10 |
Journal | Cell Differentiation and Development |
Volume | 29 |
Issue number | 2 |
DOIs | |
State | Published - Feb 1990 |
Keywords
- Acetylcholine receptor
- Creatine kinase
- Gene activation
- Gene expression
- Heterokaryon
- Muscle
ASJC Scopus subject areas
- Developmental Biology