Abstract
WE demonstrated previously that the epidermal cells of chick embryos are induced to differentiate by glucocorticoids1,2. Hydrocortisone (0.01 µg ml−1) added to a serum-free chemically-defined medium produced an intense keratinised layer over the uppermost cells3 and many tonofilaments within the basal and intermediate cells4 of the epidermis after 4 d in culture of 13-d-old embryonic chick tarsometatarsal skin. Within 12–16 h of hydrocortisone addition it is possible to show the synthesis of a urea–mercaptoethanol soluble, glycine-rich and metabolically stable epidermal structural protein5 and the accumulation of a urea–mercaptoethanol insoluble epidermal protein(s)4. These changes of protein metabolism induced by hydrocortisone paralleled those seen during in ovo keratinisation of the epidermis4,5. The amino acid composition of the two proteins was very similar suggesting that the soluble protein is converted to the insoluble one in the process of epidermal keratinisation of chick embryonic skin. We show here that the levels of transglutaminase (TG), an enzyme that possibly mediates cross-linking of keratinous polypeptide chains by a ɛ-(γ-glutamyl) lysine bond6–8, increases both during in ovo development of the epidermis and during hydrocortisone-induced in vitro keratinisation of chick embryonic cultured skin.
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OBINATA, A., ENDO, H. Induction of epidermal transglutaminase by hydrocortisone in chick embryonic skin. Nature 270, 440–441 (1977). https://doi.org/10.1038/270440a0
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DOI: https://doi.org/10.1038/270440a0
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