Mechanisms of signal transduction activated by sublytic assembly of terminal complement complexes on nucleated cells
Mechanisms of signal transduction activated by sublytic assembly of terminal complement complexes on nucleated cells
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DOI：
10.1385/ir:24:2:191
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发表时间：
2001-01-01
影响因子：
4.4
通讯作者：
Rus, H
中科院分区：
文献类型：
--
作者：
Niculescu, F;Rus, H
C5b-7、C5b-8和C5b-9通过异源三聚体G蛋白激活细胞膜磷脂酶，刺激多种细胞活动，包括前列腺素、白三烯和细胞因子的合成。有丝分裂信号通过RAS、Raf-1、ERK1和磷脂酰肌醇-3激酶(PI3-K)在B淋巴细胞、内皮细胞和平滑肌细胞中被激活。PI3-K被C5b-9激活后，STAT3被磷酸化，并由胞浆转位至胞核。这种复杂的信号机制直接参与许多生物学功能，如内吞和胞吐、细胞周期进程、转录激活和蛋白质合成。这个信号通路的关键作用反映在急、慢性炎症中的细胞生存和增殖上，补体激活是一个普遍存在的事件。
The sublytic assembly or C5b-7, C5b-8, and C5b-9, activates membrane phospholipases through heterotrimeric G proteins and stimulates a variety of cellular activities including prostanoids, leukotrienes, and cytokines synthesis. Activation of mitotic signaling through Ras, Raf- 1, ERK 1, and phosphatidylinositol-3 kinase (PI3-K) was induced in B lymphocytes, endothelial, and smooth muscle cells. PI3-K activation by C5b-9 induced STAT3 phosphorylation and translocation from cytoplasm to nucleus. This complex signaling mechanism is directly involved in many biological functions such as endo- and exocytosis, cell cycle progression, activation of transcription, and protein synthesis. The key role of this signaling pathway is reflected on cell survival and proliferation in acute and chronic inflammation where complement activation is an ubiquitous event.