Tyrosine phosphorylation and activation of PKC and its role in celluar regulation

它已经展示了PKC，它包括十个异黄酮的一个家族，是由受体介导的羟基产生的1，2-二酰甘油醇。On the other hand， the PKC isoforms have been indicated to be tyrosine phosphorylated in response to the treatment of cells with hydrogen peroxide （H-D22-D22-D2）。在PKC异构体中， PKCδ是有效的酪氨酸磷酸化和催化激活的。在本研究中，PKCδ的磷酸化相关激活得到了分析。首先，PKCδ的内部本地化是在PKCδ的非公开显微镜下观察到的，通过监测其GFP-融合蛋白的荧光。GFP-融合蛋白通过刺激产生1，2-二酰甘油醇的膜被转移到膜上，在那里，融合蛋白没有在H-D22-D2 O-D22-D2处理的细胞中移动。因此， PKCδ被合并为由H-D22-D2 O-D22-D2作为一种模式的独立于1，2-Dia的膜转移定位 ... More Cyglycerol。It is well known that H-D22-D22-D2 suppresses the protein-tyrosine phosphatase reaction and thus increase tyrosine phosphorylation of various cellular proteins。几种蛋白质-酪氨酸磷酸酶抑制剂，如何，并不直接诱导酪氨酸磷酸化的PKCδ，表明激活蛋白质-酪氨酸激酶不如抑制蛋白质-酪氨酸磷酸酶是有必要的，以促进PKCδ的共同修饰。photyrosine residues were determined by the study of a series of mutant protein of PKC？and by the mass spectrometric analysis of the phosphopetides of PKC？recovered from the H？D22？D22？D2-treated cells。三种酪氨酸溶液已被识别，并在Lck的这些酪氨酸溶液中进行体外磷酸化，一种非受体蛋白质酪氨酸激酶，激活酶。通过酪氨酸磷酸化激活PKCδ在H-D22-D2 O-D22-D22-D2治疗后至少检测到3小时，并且因此活性酶可能在细胞长时间响应中具有一个重要的作用。Less（低）

It has been shown that PKC, which comprises a family of ten isoforms, is activated by 1, 2-diacylglycerol produced from receptor-mediated hydrolysis of inositol phospholipids. On the other hand, the PKC isoforms have been indicated to be tyrosine phosphorylated in response to the treatment of cells with hydrogen peroxide (HィイD22ィエD2OィイD22ィエD2). Among the PKC isoforms, PKCδ is efficiently tyrosine phosphorylated and catalytically activated. In this study, phosphorylation-dependent activation of PKCδ was analyzed. Firstly, the intracellular localization of PKCδ was observed under confocal microscope by monitoring the fluorescence of the GFP-fusion protein of PKCδ. The GFP-fusion protein was translocated to the membrane by the stimuli generating 1, 2-diacylglycerol, whereas the fusion protein did not move in the HィイD22ィエD2OィイD22ィエD2-treated cells. Therefore, PKCδ was concluded to be activated by HィイD22ィエD2OィイD22ィエD2 in a manner independent of the membrane translocation induced by 1, 2-dia … More cyglycerol. It is well known that HィイD22ィエD2OィイD22ィエD2 suppresses the protein-tyrosine phosphatase reaction and thus increase tyrosine phosphorylation of various cellular proteins. Several protein-tyrosine phosphatase inhibitors, however, did not induce tyrosine phosphorylation of PKCδ, indicating that activation of protein-tyrosine kinase rather than inhibition of protein-tyrosine phosphatase is necessary for the covalent modification of PKCδ. Phosphotyrosine residues were determined by the study of a series of mutant protein of PKCδ and by the mass spectrometric analysis of the phosphopetides of PKCδ recovered from the HィイD22ィエD2OィイD22ィエD2-treated cells. Three tyrosine residues were identified, and in vitro phosphorylation of these tyrosine residues by Lck, a non-receptor type protein-tyrosine kinase, activated the enzyme. Activation of PKCδ by tyrosine phosphorylation was detected even three hours after the HィイD22ィエD2OィイD22ィエD2 treatment, and thus the active enzyme may have an important role in the long-term responses of the cells to the extracellular stimuli. Less