Shyy Y J, Li Y S, Kolattukudy P E
Department of Surgery, Molecular Cellular and Developmental Biology, Ohio State University, Columbus 43210.
Biochem Biophys Res Commun. 1993 Apr 30;192(2):693-9. doi: 10.1006/bbrc.1993.1470.
Multiple signal transduction pathways including protein kinase C, tyrosine phosphorylation, and an independent third signaling mechanism are involved in the activation of monocyte chemotactic protein-1 gene. Northern blot analysis showed that the incubation of endothelial cell with dioctanoylglycerol induced maximum level of monocyte chemotactic protein-1 transcripts. The TPA-induced monocyte chemotactic protein-1 expression was abolished by treating the cells with both staurosporine and genistein; however, only a portion of the LPS-induced expression was inhibited by staurosporine/genistein. This is in accordance with the observation that LPS induced the expression of monocyte chemotactic protein-1 in desensitized cells. Thus, a third signal transduction pathway other than protein kinase C or tyrosine kinase is involved in the LPS-induced monocyte chemotactic protein-1 expression in human endothelial cell.
包括蛋白激酶C、酪氨酸磷酸化以及一种独立的第三种信号传导机制在内的多种信号转导途径参与了单核细胞趋化蛋白-1基因的激活。Northern印迹分析表明，用二辛酰甘油孵育内皮细胞可诱导单核细胞趋化蛋白-1转录本达到最高水平。用星形孢菌素和染料木黄酮处理细胞可消除佛波酯诱导的单核细胞趋化蛋白-1表达；然而，只有一部分脂多糖诱导的表达被星形孢菌素/染料木黄酮抑制。这与脂多糖在脱敏细胞中诱导单核细胞趋化蛋白-1表达的观察结果一致。因此，除蛋白激酶C或酪氨酸激酶之外的第三种信号转导途径参与了人内皮细胞中脂多糖诱导的单核细胞趋化蛋白-1表达。
