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    • 7. 发明申请
    • 受容体細胞内C末側領域会合分子
    • 与受体细胞中C末端相关的分子
    • WO2003070946A1
    • 2003-08-28
    • PCT/JP2003/001699
    • 2003-02-18
    • 株式会社エフェクター細胞研究所松島 綱治寺島 裕也
    • 松島 綱治寺島 裕也
    • C12N15/11
    • C07K14/521
    • There is drawn a novel hypothesis on a novel intracellular signaling mechanism that though no phosphorylation arises in the C-terminal domain in a receptor cell, an unknown molecule would associate to the Pro-C terminal domain of a G protein-coupled receptor to a chemokine to thereby inhibit the receptor-dependent leukocyte migration. By discussing this hypothesis, attempts were made to search for a CCR2-binding protein to thereby clarify a novel target in treating inflammatory diseases and other various diseases. As a result, a novel cellular protein associating directly and specifically to the Pro-12-C terminal domain of CCR2 is found out and it is clarified that this protein forms a cluster together with CCR2 after stimulating CCL2. Thus, the presence of a novel signaling system is clarified in the CCL2-CCR2 pathway in addition to the known G protein-mediated intracellular signaling systems. It is also found out that this novel protein associates to the C-terminal domain in a cell of a receptor CCR5.
    • 对新型细胞内信号传导机制提出了新的假设,尽管在受体细胞的C末端结构域中没有发生磷酸化,但是未知的分子将与G蛋白偶联受体的Pro-C末端结构域结合到趋化因子 从而抑制受体依赖性白细胞迁移。 通过讨论这一假设,尝试寻找CCR2结合蛋白,从而阐明治疗炎性疾病和其他各种疾病的新靶点。 结果发现了一种与CCR2的Pro-12-C末端结构域直接和特异性结合的新型细胞蛋白,并且阐明了这种蛋白质在刺激CCL2后与CCR2形成簇。 因此,除了已知的G蛋白介导的细胞内信号系统之外,在CCL2-CCR2途径中阐明了新的信号系统的存在。 还发现该新型蛋白质与受体CCR5的细胞中的C末端结构域相关联。