Abstract
The hypothesis that some transformed cells produce endogenous transforming growth factors (TGFs) has been supported by isolation of peptide factors from transformed cells1–5. One group of TGFs, TGF-I, produced only by transformed cells, displays sequence homology with the functionally related mouse submaxillary epidermal growth factor (mEGF)5. Both TGF-I and mEGF exhibit similar activities in competition for binding to the EGF receptor, stimulation of DNA synthesis and cell growth. Another group of TGFs, TGF-II (also known as TGFβ)2, present both in normal and transformed cells, is structurally and functionally unrelated to TGF-I or EGF, and does not compete for binding to the EGF receptor or induce cell growth. However, TGF-I or EGF in the presence of TGF-II produces a synergistic effect that is responsible for the observed phenotypic transformation of NRK fibroblasts4. The complete amino acid sequence of rat TGF-I (rTGF-I) from transformed Fischer rat embryo fibroblasts, has recently been determined5. Using this proposed sequence, we have now prepared synthetic rTGF-I by the solid-phase synthesis method and find that it exhibits chemical and biological properties indistinguishable from those of natural rTGF-I. Since synthetic rTGF-I is free of any biological contaminants, our findings provide independent evidence that rTGF-I is an active principle in the transformation of cells6.
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References
Delarco, J. E. & Todaro, G. J. Proc. natn. Acad. Sci. U.S.A. 75, 4001–4005 (1978).
Roberts, A. B. et al. Nature 295, 417–419 (1982).
Ozanne, B., Wheeler, T. & Kaplan, P. L. Fedn Proc. 41, 3004–3007 (1982).
Anzano, M. et al. Cancer Res. 42, 4776–4778 (1982).
Marquardt, H. et al. Science 223, 1079–1082 (1984).
Twardzik, D. R. et al. Science 216, 894–896 (1982).
Merrifield, R. B. J. Am. chem. Soc. 85, 2149–2156 (1963).
Mitchell, A. R. et al. J. Am. chem. Soc. 98, 7357–7362 (1976).
Tam, J. P., Heath, W. F. & Merrifield, R. B. Tetrahedron Lett. 23, 4435–4438 (1982).
Tam, J. P., Heath, W. F. & Merrifield, R. B. J. Am. chem. Soc. 105, 6442–6454 (1983).
Ahmed, A. K., Schaffer, S. W. & Wetlanfer, D. B. J. biol. Chem. 250, 8477–8482 (1975).
Ellman, G. L. Archs Biochem. Biophys. 82, 70–79 (1959).
Stoker, M. et al. Int. J. Cancer 3, 683–693 (1968).
Savage, C. R., Inagami, T. & Cohen, S. J. biol. Chem. 247, 7612–7617 (1971).
Scott, J. et al. Science 221, 236–240 (1983).
Reynold, F. H. Jr et al. Nature 292, 259–261 (1981).
Pike, L. J. et al. J. biol. Chem. 257, 14628–14631 (1982).
Wong, T. W. & Goldberg, A. R. J. biol. Chem. 258, 1022–1025 (1983).
Kitos, P. A. et al. Expl Cell Res. 27, 307–316 (1962).
Raff, M. C. et al. Cell 15, 813–820 (1978).
Delcarco, J. E. & Todaro, G. J. J. cell. Physiol. 94, 335–342 (1978).
Rapp, et al. J. cell Biochem. 21, 29–38 (1983).
Roberts, A. B. et al. Proc. natn. Acad. Sci. U.S.A. 78, 5339–5343 (1981).
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Tam, J., Marquardt, H., Rosberger, D. et al. Synthesis of biologically active rat transforming growth factor I. Nature 309, 376–378 (1984). https://doi.org/10.1038/309376a0
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DOI: https://doi.org/10.1038/309376a0
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