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Vol. 10, Issue 11, 3801-3813, November 1999
and
*Department of Biochemistry, The Cancer Institute of the Japanese
Foundation for Cancer Research and Research for the Future Program,
Japan Society for the Promotion of Science, Tokyo 170-8455, Japan;
The biological effects of type I serine/threonine kinase receptors
and Smad proteins were examined using an adenovirus-based vector
system. Constitutively active forms of bone morphogenetic protein (BMP)
type I receptors (BMPR-IA and BMPR-IB; BMPR-I group) and those of
activin receptor-like kinase (ALK)-1 and ALK-2 (ALK-1 group) induced
alkaline phosphatase activity in C2C12 cells. Receptor-regulated Smads (R-Smads) that act in the BMP pathways, such as Smad1 and Smad5,
also induced the alkaline phosphatase activity in C2C12 cells. BMP-6
dramatically enhanced alkaline phosphatase activity induced by Smad1 or
Smad5, probably because of the nuclear translocation of R-Smads
triggered by the ligand. Inhibitory Smads, i.e., Smad6 and Smad7,
repressed the alkaline phosphatase activity induced by BMP-6 or the
type I receptors. Chondrogenic differentiation of ATDC5 cells
was induced by the receptors of the BMPR-I group but not by those of
the ALK-1 group. However, kinase-inactive forms of the receptors of the
ALK-1 and BMPR-I groups blocked chondrogenic differentiation. Although
R-Smads failed to induce cartilage nodule formation, inhibitory Smads
blocked it. Osteoblast differentiation induced by BMPs is thus mediated
mainly via the Smad-signaling pathway, whereas chondrogenic
differentiation may be transmitted by Smad-dependent and independent pathways.
Department of Biomaterials Science and
Second Department of Oral Surgery, Faculty of Dentistry,
Tokyo Medical and Dental University, Tokyo 113-8549, Japan; and
§Creative BioMolecules, Hopkinton, Massachusetts 01748
Corresponding author. E-mail address:
fjios2{at}dent.tmd.ac.jp.
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