Abstract
Epidermal growth factor (EGF) has a profound effect on the differentiation of specific cells in vivo, and has been shown to be a potent mitogenic factor for a variety of cultured cells, of both ectodermal and mesodermal origin (see ref. 1 for review). This 53-amino acid polypeptide of known sequence2 contains six cysteine residues3, which are thought to form three intrachain disulphide bonds4. Urogastrone, a polypeptide bearing anti-gastric secretory activity isolated from human urine5, which is presumably synthesized in submandibular and Brunner's glands6,7, shares extensive sequence homology (70%) with EGF and may represent the human EGF equivalent. Here we present the sequence of a mouse EGF cDNA clone, which suggests that EGF is synthesized as a large protein precursor of 1,168 amino acids. Our data indicate that the discrepancy between EGF levels in male and female mouse submaxillary glands (MSGs) is due to different EGF mRNA levels in these tissues, and suggest that precursor EGF processing may differ from that described previously for other polypeptide hormones.
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Gray, A., Dull, T. & Ullrich, A. Nucleotide sequence of epidermal growth factor cDNA predicts a 128,000-molecular weight protein precursor. Nature 303, 722–725 (1983). https://doi.org/10.1038/303722a0
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DOI: https://doi.org/10.1038/303722a0
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