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Synthesis of biologically active rat transforming growth factor I


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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Tam, J., Marquardt, H., Rosberger, D. et al. Synthesis of biologically active rat transforming growth factor I. Nature 309, 376–378 (1984).

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