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(Received for publication, October 2, 1996, and in revised form, May 29, 1997)
From the Members of the transforming growth
factor (TGF)-
Volume 272, Number 35,
Issue of August 29, 1997
pp. 22046-22052
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
,
,
and
Department of Biochemistry, School of
Dentistry, Showa University, Tokyo 142, Japan, the § Faculty
of Pharmaceutical Sciences, Hokkaido University, Sapporo 060, Japan,
the ¶ Yamanouchi Pharmaceutical Co., Ltd., Tokyo 103, Japan,
and the Genetics Institute Inc.,
Cambridge, Massachusetts 02140
superfamily bind the transmembrane serine/threonine
kinase complex consisting of type I and type II receptors. Their
intracellular signals are propagated via respective type I receptors.
Bone morphogenetic protein (BMP)-2, a member of the TGF-
superfamily, induces ectopic bone formation when implanted into
muscular tissues. Two type I receptors (BMPR-IA and BMPR-IB) have been
identified for BMP-2. We have reported that BMP-2 inhibits the terminal
differentiation of C2C12 myoblasts and converts their differentiation
pathway into that of osteoblast lineage cells (Katagiri, T., Yamaguchi, A., Komaki, M., Abe, E., Takahashi, N., Ikeda, T., Rosen, V., Wozney,
J. M., Fujisawa-Sehara, A. and Suda, T. (1994) J. Cell Biol. 127, 1755-1766). In the present study, we examined the
involvement of functional BMP-2 type I receptors in signal transduction
in C2C12 cells, which expressed mRNA for BMPR-IA, but not for
BMPR-IB in Northern blotting. TGF- type I receptor (TR-I)
mRNA was also expressed in C2C12 cells. Subclonal cell lines of
C2C12 that stably expressed a kinase domain-truncated BMPR-IA
(
BMPR-IA) differentiated into myosin heavy chain-expressing myotubes
but not into alkaline phosphatase (ALP)-positive cells, even in the
presence of BMP-2. In contrast, the differentiation of the
BMPR-IA-transfected C2C12 cells into myotubes was suppressed by
TGF-1, as in the parental C2C12 cells. BMP-2 did not efficiently
suppress the mRNA expression of muscle-specific genes such as
muscle creatine kinase, MyoD, and myogenin, nor did it induce the
expression of ALP mRNA in the BMPR-IA-transfected C2C12 cells.
In contrast, TGF-1 inhibited mRNA expression of the
muscle-specific genes in those cells. When wild-type BMPR-IA was
transiently transfected into the BMPR-IA-transfected C2C12 cells, a
number of ALP-positive cells appeared in the presence of BMP-2.
Transfection of wild-type BMPR-IB or TR-I failed to increase the
number of ALP-positive cells. These results suggest that the
BMP-2-induced signals, which inhibit myogenic differentiation and
induce osteoblast differentiation, are transduced via BMPR-IA in C2C12
myoblasts.
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