Kulichkova V A, Ermolaeva Iu B, Mittenberg A G, Volkova I V, Tsimokha A S, Evteeva I N, Gauze L N, Konstantinova I M
Tsitologiia. 2005;47(9):774-9.
It has been first shown that EGF regulates a proteolytic activity of proteasomes. Following a 15 min action with 100 ng/ml EGF, three types of peptidase activity of both cytoplasmic and nuclear proteasomes were induced in A431 cells, although, this effect on different populations of proteasomes was selective. EGF preferentially stimulates chymotrypsin-like activity of cytoplasmic proteasomes, and induces a similar increase of chymotrypsin-like, trypsin-like and peptydylglutamyl peptide hydrolase activities of nuclear particles. Tyrphostin, an inhibitor of tyrosine kinase activity of EGF receptor, prevents the EGF effect on both proteolytic and RNase activity of nuclear and cytoplasmic proteasomes. It is concluded that EGF may rapidly and selectively stimulate enzymatic activity of EGF receptor.
首次表明表皮生长因子（EGF）可调节蛋白酶体的蛋白水解活性。用100 ng/ml EGF作用15分钟后，A431细胞中细胞质和细胞核蛋白酶体的三种肽酶活性均被诱导，不过，这种对不同蛋白酶体群体的作用具有选择性。EGF优先刺激细胞质蛋白酶体的类胰凝乳蛋白酶活性，并诱导核颗粒的类胰凝乳蛋白酶、类胰蛋白酶和肽基谷氨酰肽水解酶活性出现类似增加。酪氨酸激酶活性抑制剂 tyrphostin可阻止EGF对细胞核和细胞质蛋白酶体的蛋白水解及核糖核酸酶活性的影响。得出的结论是，EGF可能快速且选择性地刺激表皮生长因子受体的酶活性。
