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  • Title: Transforming growth factor-alpha binds to the epidermal growth factor receptor in gastric mucosa.
    Author: Bielanski WJ, Keogh JP, Wang SL, Liu J, Konturek SJ, Slomiany A, Slomiany BL.
    Journal: Biochem Int; 1991 Oct; 25(3):419-27. PubMed ID: 1805786.
    Abstract:
    The ability of transforming growth factor-alpha (TGF-alpha) to interact with the gastric mucosal epidermal growth factor (EGF) receptor was investigated using a mucosal membrane preparation. TGF-alpha inhibited specific binding of [125I]EGF to its receptor, but the IC50 for TGF-alpha was at least 100 fold greater than that observed for unlabeled EGF. Cross-linking studies revealed no attachment of [125I]TGF-alpha to EGF-receptor size components, and the unlabeled TGF-alpha was only weakly effective in inhibiting cross-linking of [125I]EGF to the 170 kDa receptor. However, when the cytosolic fraction was reconstituted with the membrane preparation, an enhancement in binding of [125I]TGF-alpha to the EGF receptor occurred in a manner dependent on the concentration of cytosolic protein. Hence the binding characteristics of TGF-alpha to the EGF receptor in gastric mucosa are different from those for EGF.
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