Functional receptors for transforming growth factor-β are retained by biochemically differentiated C2 myocytes in growth factor-deficient medium containing EGTA but down-regulated during terminal differentiation

Jing Shan Hu, Eric N. Olson

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30 Citations (Scopus)

Abstract

Transforming growth factor-β (TGF-β) has been shown to block the morphological and molecular events associated with myoblast differentiation. During fusion of C2 myoblasts, TGF-β receptors are down-regulated, and muscle-specific genes become refractory to the inhibitory effects of TGF-β. To define further the mechanisms that modulate TGF-β receptor expression during myogenesis, we have developed culture conditions that support the differentiation of C2 cells in the absence of fusion and have examined the expression of functional TGF-β receptors in biochemically differentiated mononucleated myocytes. Exposure of C2 myoblasts to growth factor-deficient medium containing 1.4 mM [ethylenebis(oxyethylenenitrilo)]tetraacetic acid (EGTA) leads to withdrawal from the cell cycle and high level expression of muscle-specific mRNAs and proteins. Under these conditions, TGF-β receptors fail to be down-regulated, and the differentiation program remains sensitive to repression by TGF-β. These studies demonstrate that EGTA uncouples muscle-specific gene expression from fusion in C2 cells and that in the absence of fusion, C2 myocytes retain a functional TGF-β signaling system.

Original languageEnglish (US)
Pages (from-to)7914-7919
Number of pages6
JournalJournal of Biological Chemistry
Volume265
Issue number14
StatePublished - May 15 1990

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Egtazic Acid
Transforming Growth Factors
Muscle Cells
Intercellular Signaling Peptides and Proteins
Growth Factor Receptors
Myoblasts
Fusion reactions
Muscle
Muscles
Muscle Development
Gene Fusion
Gene expression
Refractory materials
Cell Differentiation
Cell Cycle
Genes
Cells
Gene Expression
Messenger RNA
Acids

ASJC Scopus subject areas

  • Biochemistry

Cite this

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abstract = "Transforming growth factor-β (TGF-β) has been shown to block the morphological and molecular events associated with myoblast differentiation. During fusion of C2 myoblasts, TGF-β receptors are down-regulated, and muscle-specific genes become refractory to the inhibitory effects of TGF-β. To define further the mechanisms that modulate TGF-β receptor expression during myogenesis, we have developed culture conditions that support the differentiation of C2 cells in the absence of fusion and have examined the expression of functional TGF-β receptors in biochemically differentiated mononucleated myocytes. Exposure of C2 myoblasts to growth factor-deficient medium containing 1.4 mM [ethylenebis(oxyethylenenitrilo)]tetraacetic acid (EGTA) leads to withdrawal from the cell cycle and high level expression of muscle-specific mRNAs and proteins. Under these conditions, TGF-β receptors fail to be down-regulated, and the differentiation program remains sensitive to repression by TGF-β. These studies demonstrate that EGTA uncouples muscle-specific gene expression from fusion in C2 cells and that in the absence of fusion, C2 myocytes retain a functional TGF-β signaling system.",
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AU - Olson, Eric N.

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N2 - Transforming growth factor-β (TGF-β) has been shown to block the morphological and molecular events associated with myoblast differentiation. During fusion of C2 myoblasts, TGF-β receptors are down-regulated, and muscle-specific genes become refractory to the inhibitory effects of TGF-β. To define further the mechanisms that modulate TGF-β receptor expression during myogenesis, we have developed culture conditions that support the differentiation of C2 cells in the absence of fusion and have examined the expression of functional TGF-β receptors in biochemically differentiated mononucleated myocytes. Exposure of C2 myoblasts to growth factor-deficient medium containing 1.4 mM [ethylenebis(oxyethylenenitrilo)]tetraacetic acid (EGTA) leads to withdrawal from the cell cycle and high level expression of muscle-specific mRNAs and proteins. Under these conditions, TGF-β receptors fail to be down-regulated, and the differentiation program remains sensitive to repression by TGF-β. These studies demonstrate that EGTA uncouples muscle-specific gene expression from fusion in C2 cells and that in the absence of fusion, C2 myocytes retain a functional TGF-β signaling system.

AB - Transforming growth factor-β (TGF-β) has been shown to block the morphological and molecular events associated with myoblast differentiation. During fusion of C2 myoblasts, TGF-β receptors are down-regulated, and muscle-specific genes become refractory to the inhibitory effects of TGF-β. To define further the mechanisms that modulate TGF-β receptor expression during myogenesis, we have developed culture conditions that support the differentiation of C2 cells in the absence of fusion and have examined the expression of functional TGF-β receptors in biochemically differentiated mononucleated myocytes. Exposure of C2 myoblasts to growth factor-deficient medium containing 1.4 mM [ethylenebis(oxyethylenenitrilo)]tetraacetic acid (EGTA) leads to withdrawal from the cell cycle and high level expression of muscle-specific mRNAs and proteins. Under these conditions, TGF-β receptors fail to be down-regulated, and the differentiation program remains sensitive to repression by TGF-β. These studies demonstrate that EGTA uncouples muscle-specific gene expression from fusion in C2 cells and that in the absence of fusion, C2 myocytes retain a functional TGF-β signaling system.

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