Abstract
THROMBIN, a serine protease with great specificity, is a potent mitogen for resting chick embryo fibroblasts in culture1–3. So far only a limited number of peptide bonds in a few native proteins have been found to be sensitive to proteolysis by thrombin, namely four Arg–Gly bonds in fibrinogen4 and a few arginyl and lysyl bonds in actin5. It is likely therefore that the number of fibroblast surface proteins susceptible to this protease will also be limited, whereas with trypsin many surface proteins are attacked. Thus thrombin may be an excellent probe for studies of the role of changes in cell surface composition during mitogenesis or cell-cell interaction. A large, external transformation sensitive (LETS) protein6–10, postulated10,11 to be involved in cellular growth control, is insensitive to thrombin2. This observation led to the conclusion that the removal of LETS is not a necessary condition for cell growth when a protease is used to stimulate growth.
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TENG, N., BO CHEN, L. Thrombin-sensitive surface protein of cultured chick embryo cells. Nature 259, 578–580 (1976). https://doi.org/10.1038/259578a0
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DOI: https://doi.org/10.1038/259578a0
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