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J. Biol. Chem., Vol. 265, Issue 14, 7914-7919, May, 1990

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

JS Hu and EN Olson
Department of Biochemistry and Molecular Biology, University of Texas M. D. Anderson Cancer Center, Houston 77030.

Transforming growth factor-beta (TGF-beta) has been shown to block the morphological and molecular events associated with myoblast differentiation. During fusion of C2 myoblasts, TGF-beta receptors are down-regulated, and muscle-specific genes become refractory to the inhibitory effects of TGF-beta. To define further the mechanisms that modulate TGF-beta 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-beta 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-beta receptors fail to be down-regulated, and the differentiation program remains sensitive to repression by TGF-beta. 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- beta signaling system.
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