ENHANCED PHOSPHORYLATION OF 65 AND 74-KDA PROTEINS BY TUMOR NECROSIS FACTOR AND INTERLEUKIN-1 IN HUMAN PERIPHERAL BLOOD MONONUCLEAR CELLS
ENHANCED PHOSPHORYLATION OF 65 AND 74-KDA PROTEINS BY TUMOR NECROSIS FACTOR AND INTERLEUKIN-1 IN HUMAN PERIPHERAL BLOOD MONONUCLEAR CELLS
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DOI：
10.1016/1043-4666(90)90038-u
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发表时间：
1990-01-01
期刊：
影响因子：
3.8
通讯作者：
MATSUSHIMA K
中科院分区：
文献类型：
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作者：
SHIROO M;MATSUSHIMA K
肿瘤坏死因子 (TNF) 和白介素-1 (IL-1) 增强人外周血单核细胞 (PBMC) 中相同胞质 65 kDa 蛋白（P65 或 l-plastin）和 74 kDa 蛋白 (P74) 丝氨酸残基的磷酸化。 P65和P74的等电点分别为5.6和4.7至5.0。这些蛋白质的磷酸化在几分钟内增加，并在 10 分钟内达到最高水平，约为未刺激水平的 3 倍。 p65 和 P74 的磷酸化可通过有效的蛋白激酶 C (PKC) 激活剂 PMA 得到广泛增强。然而，在用 TNF 或 IL-1 刺激的 PBMC 中，PKC 没有从胞质溶胶易位到膜，这表明 PKC 不参与 TNF 或 IL-1 信号转导。 cAMP 依赖性蛋白 (PKA) 激活剂毛喉素和 PGE2 未能增加磷酸化，这与显示 TNF 和 IL-1 均不增加 PBMC 中 cAMP 水平的数据一致。这些结果表明，TNF 和 IL-1 对 P65 和 P74 的磷酸化诱导不是由 PKC 和 PKA 介导的，而是可能由另一种蛋白激酶介导，并导致 TNF 和 IL-1 之间生物活性的重叠。
Tumor necrosis factor (TNF) and interleukin-1 (IL-1) enhanced the phosphorylation of identical cytosolic 65 kDa protein (P65 or l-plastin) and 74 kDa protein (P74) at serine residues in human peripheral blood mononuclear cells (PBMC). The isoelectric points of P65 and P74 were 5.6 and 4.7 to 5.0, respectively. The phosphorylation of these proteins increased with a few minutes and reached maximal levels of approximately 3 times the unstimulated levels of 10 minutes. The phosphorylation of p65 and P74 was extensively enhanced by a potent protein kinase C (PKC) activator, PMA. However, there was no translocation of PKC from cytosol to membrane in PBMC that was stimulated with either TNF or IL-1, which suggests that PKC does not participate in TNF or IL-1 signal transduction. cAMP dependent protein (PKA) activators, forskolin and PGE2, failed to increase the phosophorylation, which is in agreement with the data showing that neither TNF nor IL-1 increased cAMP levels in PBMC. These results suggest that induction of phosphorylation of P65 and P74 by TNF and IL-1 is not mediated by PKC and PKA but may be mediated by another protein kinase and result in overlapping of biological activities between TNF and IL-1.