Functional receptors for transforming growth factor-β are retained by biochemically differentiated G2 myocytes in growth factor-deficient medium containing EGTA but down-regulated during terminal differentiation

Jing Shan Hu, Eric N. Olson

Research output: Contribution to journalArticle

30 Scopus citations


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 ctional 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
Issue number14
StatePublished - Jun 1 1990


ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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