Szallasi Z, Denning M F, Chang E Y, Rivera J, Yuspa S H, Lehel C, Olah Z, Anderson W B, Blumberg P M
Laboratory of Cellular Carcinogenesis and Tumor Promotion, National Cancer Institute, Bethesda, MD 20892, USA.
Biochem Biophys Res Commun. 1995 Sep 25;214(3):888-94. doi: 10.1006/bbrc.1995.2370.
In rat basophilic leukemia cells (RBL-2H3) activation of the high affinity receptor for IgE induces tyrosine phosphorylation of PKC delta. We carried out solid phase synthesis of 15 amino acid long oligopeptides corresponding to the sequences around each of the 19 tyrosine residues in PKC delta. Only three oligopeptides, corresponding to tyrosine 52, 155, and 565, were phosphorylated when exposed to lyn kinase. Single mutants in each of these three tyrosine residues of PKC delta were prepared. Upon expression in the RBL-2H3 cells, only the mutant in tryosine 52 showed abolition of the IgE-antigen induced tyrosine phosphorylation.
在大鼠嗜碱性白血病细胞（RBL - 2H3）中，IgE高亲和力受体的激活会诱导蛋白激酶Cδ（PKCδ）的酪氨酸磷酸化。我们对与PKCδ中19个酪氨酸残基周围序列相对应的15个氨基酸长的寡肽进行了固相合成。当暴露于lyn激酶时，只有对应于酪氨酸52、155和565的三个寡肽发生了磷酸化。制备了PKCδ这三个酪氨酸残基各自的单突变体。在RBL - 2H3细胞中表达时，只有酪氨酸52位点的突变体显示出IgE - 抗原诱导的酪氨酸磷酸化消失。
