Takuma T, Tajima Y, Ichida T
Department of Oral Biochemistry, School of Dentistry, Health Sciences University of Hokkaido, Japan.
FEBS Lett. 1996 Feb 12;380(1-2):83-6. doi: 10.1016/0014-5793(96)00009-9.
We evaluated the role of protein tyrosine phosphorylation in amylase exocytosis from parotid acinar cells by using genistein, a tyrosine kinase inhibitor. Amylase release stimulated by isoproterenol was dose-dependently inhibited by genistein. Genistein also inhibited the exocytosis evoked by dibutyryl- or 8-chlorophenylthio-cAMP. Daidzein, a negative control agent of genistein, elicited no inhibitory effect. Isoproterenol had dual effects on protein tyrosine phosphorylation; it increased that phosphorylation of 190- and 210-kDa proteins and decreased that of a 90-kDa one. The phosphorylation was dose-dependently inhibited by genistein but not by daidzein. These results suggest that protein tyrosine phosphorylation plays a role in the process of amylase exocytosis from parotid acinar cells.
我们通过使用酪氨酸激酶抑制剂染料木黄酮,评估了蛋白质酪氨酸磷酸化在腮腺腺泡细胞淀粉酶胞吐作用中的作用。染料木黄酮剂量依赖性地抑制了异丙肾上腺素刺激的淀粉酶释放。染料木黄酮还抑制了二丁酰 - 或8 - 氯苯硫基 - cAMP诱发的胞吐作用。染料木黄酮的阴性对照剂大豆苷元未产生抑制作用。异丙肾上腺素对蛋白质酪氨酸磷酸化有双重作用;它增加了190 kDa和210 kDa蛋白质的磷酸化,并降低了90 kDa蛋白质的磷酸化。这种磷酸化被染料木黄酮剂量依赖性地抑制,但不被大豆苷元抑制。这些结果表明蛋白质酪氨酸磷酸化在腮腺腺泡细胞淀粉酶胞吐过程中起作用。