在fMLP刺激的HL-60细胞中PI3-K介导的肌动蛋白聚合  

PI3-K Mediates Polymerization of Actin in FMLP-Stimulated HL-60 Cells

作　　者：崔玉东[1] 稻波修[2] 山盛徹 桑原幹典 

机构地区：[1]黑龙江省八一农垦大学基因工程中心,密山158308 [2]北海道大学兽医学部放射生物学实验室

出　　处：《生物化学与生物物理进展》2001年第3期377-380,共4页Progress In Biochemistry and Biophysics

基　　金：日本五峰生命科学国际基金资助&&

摘　　要：趋化肽fMLP能够诱导中性粒细胞粘附、游走和吞噬 .为了澄清这种趋化反应的发生机理 ,将HL 6 0细胞诱导分化为中性粒细胞样细胞 ,然后利用激酶特异性抑制剂研究了在fMLP刺激下细胞内PI3 K、p38和ERK激酶在肌动蛋白聚合中的作用 .结果 0 1μmol/L的PI3 K抑制物Wortmannin抑制fMLP诱导的肌动蛋白聚合 ;而 5 0 μmol/L的 p38激酶抑制物SB2 0 35 80和 5 0 μmol/L的ERK激酶抑制物PD0 980 5 9对fMLP诱导的肌动蛋白聚合没有影响 ,但 p38和ERK在不同程度上受到PI3 K的调节 .这说明PI3 K介导的肌动蛋白聚合信号传导途径不同于PI3 K介导的 p38和ERK激活途径 .The chemotactic peptide fMLP was known to induce adhesion, migration and phagocytosis of neutrophil. To clear the mechanism of the chemotaxis, the effects of PI3 K, p38 and ERK on actin polymerization were studied with the inhibitors of these kinases in neutrophil like, differentiated HL 60 cells stimulated with fMLP. 0 1 μmol/L Wortmannin (PI3 kinase inhibitor) inhibited the fMLP induced polymerization of actin. 50 μmol/L SB203580 (p38 inhibitor) and 50 μmol/L PD98059 (ERK inhibitor) did not inhibited it, though p38 and ERK were regulated by PI3 K. These results suggest the signaling pathway of actin polymerization mediated by PI3 K was different from that of p38 and ERK activation mediated by PI3 K.

关 键 词：HL-60细胞 PI3-K 肌动蛋白聚合 FMLP 中性粒细胞 

分 类 号：Q26[生物学—细胞生物学] R392.12[医药卫生—免疫学]