钙调蛋白磷酸酶（Calcineurin，CN）是目前已知的唯一一种活性受细胞内第二信使Ca2+和钙调素（Calmodulin,CaM）调节的蛋白磷酸酶。它广泛分布于哺乳动物的各种组织器官，尤以脑中含量最高，在免疫系统中有重要作用。在实验室的前期工作中发现从中草药金银花中分离纯化得到的绿原酸对CN 有一定激活作用，但其激活机制不清楚，还需进行深入的挖掘。 本研究应用Jurkat细胞（人源淋巴细胞）为模型细胞，应用酶活性检测、RT-PCR、Western Blot等技术为研究手段，检测绿原酸对胞内CN及CN-NFAT信号通路的作用，发现： 1．以pNPP为底物的酶活性测定发现，绿原酸对细胞内CN活性有激活作用，它可在一定范围内对细胞裂解液中的CN有明显激活效果，但是绿原酸浓度过高会对细胞产生毒副作用。 2．通过Western Blot检测绿原酸作用下NFAT蛋白的变化，发现用药后细胞内NFAT脱磷酸化程度明显高于未加药组。说明绿原酸作用后使NFAT脱磷酸化并入核发生作用，即CN-NFAT通路被激活。 3．通过RT-PCR技术检测绿原酸作用后对IL-2表达的影响，未检测到明显的表达差异，但这一结果还需要更科学合理的论证。 综上，通过本实验，初步认为绿原酸通过CN对CN-NFAT信号通路有激活作用。

Calcineurin（CN）is the only known phosphatase at present which activity is regulated by cellar second messenger, Ca2+ and Calcineurin(CaM). It distributes widely in different tissues of mammals, especially highly abundant in brain. The activators of CN are rarely studied, and never to be further investigated. In our previous work, Chlorogenic acid (CGA), the extraction of Flos Lonicerae, was preliminarily proved to be an activator of CN. However, the activation mechanism of CN by CGA remained unclear. In this study, we exploited the activation of CN by CGA at cellular level, take Jurkat cell line as model, used enzymatic dynamic, Western Blot and RT-PCR show that CGA have improved the activity of cytoplastic CN and CN-NFAT pathway. We make some conclusions as followers. 1. CGA activated the activity of CN from 12.5μg/mL to 250μg/mL when the substrate was pNPP at cellular level. But when the concentration of CGA in a very high level, it will do harm to the cell. 2. We use Western Blot tested the protein of NFAT, found that the protein of NFAT have dephosphorylation markedly than control group. We found CGA activated the CN-NFAT pathway. 3. We exploited the activation of CN and CN-NFAT pathway by CGA, but the level of IL-2 mRNA could not be activated in the end, and we still need to do more projects to settle down the conclusion.