Carson M, Weber A, Zigmond S H
J Cell Biol. 1986 Dec;103(6 Pt 2):2707-14. doi: 10.1083/jcb.103.6.2707.
We examined the actin-nucleating activity in polymorphonuclear leukocyte lysates prepared at various times after chemotactic peptide addition. The actin nucleation increases two- to threefold within 15 s after peptide addition, decays to basal levels within 90 s, and is largely independent of cytoplasmic calcium fluxes. The peptide-induced nucleation sites behave as free barbed ends and therefore may increase the level of polymerized actin in vivo. The new nucleation sites may also determine the cellular sites of actin polymerization. This localization of actin polymerization could be important for the directional extension of lamellipodia during chemotaxis.
我们检测了趋化肽添加后不同时间制备的多形核白细胞裂解物中的肌动蛋白成核活性。趋化肽添加后15秒内，肌动蛋白成核增加两到三倍，90秒内衰减至基础水平，且很大程度上独立于细胞质钙通量。肽诱导的成核位点表现为自由的倒刺末端，因此可能会增加体内聚合肌动蛋白的水平。新的成核位点也可能决定肌动蛋白聚合的细胞位点。这种肌动蛋白聚合的定位对于趋化作用期间片状伪足的定向延伸可能很重要。
