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J. Biol. Chem., Vol. 262, Issue 5, 1946-1949, 02, 1987
SM Seyedin, PR Segarini, DM Rosen, AY Thompson, H Bentz and J Graycar
Cartilage-inducing factors-A (CIF-A) and -B (CIF-B), purified from bovine
bone on the basis of their ability to induce the cartilage phenotype in
vitro, are proteins with molecular weights of 26,000 composed of two
apparently identical disulfide-linked chains. CIF-A is apparently identical
to TGF-beta from human platelets (Seyedin S. M., Thompson, A. Y., Bentz,
H., Rosen, D. M., McPherson, J. M., Conti, A., Siegel, N. R., Galluppi, G.
R., and Piez, K. A. (1986) J. Biol. Chem. 261, 5693-5695). We have now
found that, like CIF-A and TGF-beta, CIF-B induces anchorage-independent
proliferation of NRK-49F cells when these cells are simultaneously treated
with epidermal growth factor. Furthermore, CIF-B competes with CIF-A for
the same cell membrane receptors in NRK-49F cells. Partial amino acid
sequencing reveals that CIF-B is a distinct molecule with extensive
homology to CIF-A/TGF-beta. These results show that CIF-B and TGF-beta are
structurally and functionally similar molecules, but differ more from each
other than does TGF-beta from different species.
Cartilage-inducing factor-B is a unique protein structurally and functionally related to transforming growth factor-beta
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