Bielanski W J, Keogh J P, Wang S L, Liu J, Konturek S J, Slomiany A, Slomiany B L
Research Center, New Jersey Dental School, University of Medicine and Dentistry of New Jersey, Newark 07103-2425.
Biochem Int. 1991 Oct;25(3):419-27.
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.
使用一种黏膜膜制剂研究了转化生长因子α（TGF-α）与胃黏膜表皮生长因子（EGF）受体相互作用的能力。TGF-α抑制了[125I]EGF与其受体的特异性结合，但TGF-α的IC50比未标记的EGF至少大100倍。交联研究显示[125I]TGF-α未附着到EGF受体大小的组分上，并且未标记的TGF-α在抑制[125I]EGF与170 kDa受体的交联方面仅具有微弱的效果。然而，当用膜制剂重建胞质部分时，[125I]TGF-α与EGF受体的结合增强，其方式依赖于胞质蛋白的浓度。因此，TGF-α与胃黏膜中EGF受体的结合特性不同于EGF的结合特性。
