Uncoupling of muscle-specific protein expression in myocyte X myoblast heterokaryons

Woodring E. Wright; Victor K. Lin

doi:10.1016/0922-3371(90)90029-V

Uncoupling of muscle-specific protein expression in myocyte X myoblast heterokaryons

Woodring E. Wright, Victor K. Lin

Research output: Contribution to journal › Article › peer-review

1 Scopus citations

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)
Pages (from-to)	113-122
Number of pages	10
Journal	Cell Differentiation and Development
Volume	29
Issue number	2
DOIs	https://doi.org/10.1016/0922-3371(90)90029-V
State	Published - Feb 1990

Keywords

Acetylcholine receptor
Creatine kinase
Gene activation
Gene expression
Heterokaryon
Muscle

ASJC Scopus subject areas

Developmental Biology

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10.1016/0922-3371(90)90029-V

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title = "Uncoupling of muscle-specific protein expression in myocyte X myoblast heterokaryons",

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.",

keywords = "Acetylcholine receptor, Creatine kinase, Gene activation, Gene expression, Heterokaryon, Muscle",

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note = "Funding Information: This work was supported by grants from the National Institutes of Health (AGO 1228) and the Muscular Dystrophy Association of America.",

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T1 - Uncoupling of muscle-specific protein expression in myocyte X myoblast heterokaryons

AU - Wright, Woodring E.

AU - Lin, Victor K.

N1 - Funding Information: This work was supported by grants from the National Institutes of Health (AGO 1228) and the Muscular Dystrophy Association of America.

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Y1 - 1990/2

N2 - 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.

AB - 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.

KW - Acetylcholine receptor

KW - Creatine kinase

KW - Gene activation

KW - Gene expression

KW - Heterokaryon

KW - Muscle

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Uncoupling of muscle-specific protein expression in myocyte X myoblast heterokaryons

Abstract

Keywords

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