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研究细菌内毒素（ＬＰＳ）对血管内皮细胞的直接损伤机制，有助于了解内毒素血症对血管内皮的直接损害机制及其在多脏器损害中的作用。本研究通过观察ＬＰＳ刺激血管内皮细胞后，对内皮细胞中细胞外信号调节激酶（ＥＲＫ）１／ＥＲＫ２和Ｐ３８分裂原激活的蛋白激酶（ＭＡＰＫ）磷酸化的影响，发现ＬＰＳ（１ｍｇ／Ｌ）直接作用内皮细胞后Ｐ３８ＭＡＰＫ磷酸化程度明显增强，并与ＬＰＳ剂量有明显依赖关系。２．５ｍｇ／ＬＬＰＳ刺激后，Ｐ３８ＭＡＰＫ磷酸化在１５ｍｉｎ反应最强，３０ｍｉｎ后减弱，约６０ｍｉｎ后消失。而ＥＲＫ１和ＥＲＫ２的磷酸化在１５～３０ｍｉｎ明显，６０ｍｉｎ减弱，其总强度不如Ｐ３８ＭＡＰＫ。由此证明，ＬＰＳ直接作用内皮细胞后其信号可以通过跨膜传导，将ＭＡＰＫ激活，并可能引起细胞核内的基因转录和胞浆内功能蛋白的磷酸化，导致血管内皮细胞的多种功能变化。
Studying the direct damage mechanism of bacterial endotoxin (LPS) to vascular endothelial cells helps to understand the direct damage mechanism of endotoxemia to vascular endothelium and its role in multiple organ damage. In this study, LPS (1 mg / L) was directly investigated by observing the effect of LPS on the phosphorylation of extracellular signal-regulated kinase (ERK) 1 / ERK2 and P38 mitogen-activated protein kinase (MAPK) After treated with endothelial cells, the phosphorylation of P38MAPK was significantly increased, which was significantly dependent on the LPS dose. After 2.5mg / LLPS stimulation, P38MAPK phosphorylation strongest in 15min, 30min later weakened, disappeared after about 60min. The phosphorylation of ERK1 and ERK2 in 15 ~ 30min significantly, 60min weakened, its overall strength as P38MAPK. Thus, LPS can directly activate endothelial cells by transmembrane signal transduction, activate MAPK and induce intracellular transcription of genes and phosphorylation of functional proteins in the cytoplasm, leading to a variety of functional changes of vascular endothelial cells.