Protein Degradation of Fœtal and Cancer Tissues in the Presence of Ethionine

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INTRACELLULAR proteolytic enzymes are present in many tissues and they hydrolyse proteins during autolysis. Some experimental data support the idea of a physiological action of these enzymes: the augmentation of catheptic activity during the regression of cancer1, and of larval tails of Xenopus 2. But it has been shown that intracellular protein degradation is dependent on energy3, and that o-fluorophenylalanine, a well-known anti-amino-acid, inhibits protein catabolism4,5. Steinberg et al. 5 also showed that this compound does not influence catheptic proteolysis. These observations lead to the supposition of a mechanism of protein degradation different from that of the simple catheptic hydrolysis. Similar conclusions are reported by Yakovlev6, who studied the action of phosphate, dinitrophenol and other substances on proteolysis of tissues. He reported also that fœtal tissues behave against dinitrophenol differently from the normal rat tissues.

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  1. 1

    Fodor, P. J., Funk, C., and Tomashefsky, P., Arch. Biochem. Biophys, 56, 281 (1955).

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    Weber, R., Experientia, 13, 153 (1957).

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    Simpson, M. V., J. Biol. Chem., 201, 143 (1953).

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    Steinberg, D., and Vaughan, M., Arch. Biochem. Biophys., 65, 93 (1956).

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    Steinberg, D., Vaughan, M., and Anfinsen, C. B., Science, 124, 389 (1956).

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    Yakovlev, N. N., Fiziolog. J., 35, 236 (1949).

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    Troll, W., and Cannan, R. K., J. Biol. Chem., 200, 803 (1953).

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RENDI, R. Protein Degradation of Fœtal and Cancer Tissues in the Presence of Ethionine. Nature 181, 351 (1958) doi:10.1038/181351a0

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