4 research outputs found

    根霉3078的代谢产物的研究

    Get PDF
    从根霉 30 78菌丝体的甲醇提取物中分离得到 9个化合物 ,通过波谱分析 ,鉴定为 5α,8α 表二氧 (2 0S ,2 2E ,2 4R) 麦角甾 6 ,2 2 二烯 3β 醇 (1)、甘油醇 1 单油酸酯 (2 )、4 羟基苯乙酮 (3)、4 羟基苯乙酸 (4 )、(2 0S ,2 2E ,2 4R) 麦角甾 7,2 2 二烯 3β ,5α ,6 β 三醇 (5 )、(S) 3 羟基 3 苯基丙酸 (6 )、胸腺嘧啶 (7)、尿嘧啶(8)和腺苷 (9

    协作征管:共建环保“税时代”

    Get PDF
    背景材料:1月1日起,《中华人民共和国环境保护税法》《中华人民共和国环境保护税法实施条例》同步施行。环保税的开征,意味着我国税收在生态环境方面的调控作用进一步强化,推动企业加速绿色转型

    THE INTERACTION OF THE INTRACELLULAR DOMAIN OF β-AMYLOID PRECURSOR PROTEIN WITH JKTBP2

    No full text
    β-淀粉样前体蛋白APP(β-amyloidprecursorprotein)与阿尔茨海默氏症密切相关,它经分泌酶γ切割后生成的胞内端AID(APPintracellulardomain)能够诱导细胞凋亡。为了研究AID在阿尔茨海默氏症病理过程中的作用,我们以AID为诱饵蛋白用酵母双杂交系统筛选与之有相互作用的蛋白。我们发现人不均一核蛋白D类似蛋白JKTBP2的90-204位肽段可以结合AID。利用293T细胞表达蛋白后进行免疫共沉淀,结果证实二者间存在相互作用。这些结果指出JKTBP2可能在阿尔茨海默氏症形成中有重要作用。APP (β-amyloid precursor protein) plays an important role in the formation of Alzheimer's Disease (AD), and its proteolytic product, the intracellular domain AID is believed to be involved in this process by promoting cell apoptosis. To further understand the function of AID in the pathology of AD, we utilized AID as a bait to identify AID interacting proteins in a yeast two-hybrid system. One of the positive clones encodes the fragment corresponding to amino acids 90-204 of heterogeneous nuclear ribonucleoprotein D-like JKTBP2. The interaction between JKTBP2~(90-204) and AID was further confirmed by co-immunoprecipitation in the mammalian 293T cells. These results indicate that JKTBP2 may have an important function in AD formation.国家自然科学基金(30270681);; 国家杰出青年科学基金(30125021

    A Study of AID and Interacting Protein by Yeast Two-hybrid

    No full text
    AID(APPintracellulardomain)是由淀粉样前体蛋白APP经γ分泌酶切割产生的胞内端,它可能参与细胞凋亡,基因转录等活动,并对阿尔茨海默氏症的形成有一定影响.为进一步研究AID的功能,在本实验中,我们用AID为诱饵蛋白,运用酵母双杂交系统筛选与其结合的蛋白,得到其中两个阳性克隆,一个为RPS21,另一个为FLJ20551.接着又在酵母体系用β半乳糖苷酶报告基因验证了它们的相互作用,并在哺乳动物细胞中用免疫共沉淀的方法再次验证了它们相互作用的特异性.这些结果表明RPS21和FLJ20551可能通过与AID相互作用而影响阿尔茨海默氏症的形成.Amyloid precursor protein (APP),a key protein in pathogenesis of Alzheimer’s Disease (AD),is a type Ⅰ transmembrane protein which can be cleaved by β- and γ-secretase to release the amyloidogenic β-amyloid peptides and the APP intracellular domain (AID).While Aβ has been widely believed to initiate pathogenic cascades culminating AD,the physiological functions of AID remain elusive.To study the function of AID,we attempted to identify its interacting proteins by Yeast Two-Hybrid screening using AID as the bait.Among many positive clones identified,two candidates are particularly of interest:one encodes ribosomal protein S21 (RPS21),and the other encodes a fragment of a novel protein FLJ20551.The interaction specificity with AID of both the fragment and the full-length of the preys was confirmed by using the β-galatosidase reporter.Furthermore,we demonstrated,in mammalian 293T cells,the successful expression of the clone encoding RPS21 and verified the interaction between RPS21 and AID by co-immunoprecipitation approach.Our study identified two new AID binding proteins,RPS21 and FLJ20551,and may assign novel roles for the two proteins in mediating APP/AID functions in physiological and pathological processes including AD pathogenesis.国家自然科学基金(30270681, 30125021 );; 教育部“高校博士点基金”( 20030003087 );; 教育部回国人员科研启动基金资
    corecore