Colombo R, Milzani A, Contini P, Dalle Donne I
Department of Biology, University of Milan, Italy.
Biochem J. 1991 Mar 1;274 ( Pt 2)(Pt 2):421-5. doi: 10.1042/bj2740421.
In spite of the abundant literature, questions on the biological action of Li+ are far from being answered. In the present paper we demonstrate that modification of the salt composition of the medium for actin polymerization, by gradually replacing K+ with Li+, leads to a dose-related change in the time course of actin assembly. The presence of Li+ influences actin polymerization in vitro by enhancing nucleation and decreasing critical monomer concentration at steady state. Furthermore, Li+ stabilizes actin polymers mainly by lowering the absolute value of the dissociation rate constant (K-) and shifting (towards lower values of actin monomer concentrations) the range of G-actin concentrations in which filament-subunit flux can occur. The influence of Li+ on actin and tubulin polymerization in vitro suggests that cytoskeletal structures could be some of the cytoplasmic targets of this ion.
尽管已有大量文献,但关于Li+的生物学作用问题远未得到解答。在本文中,我们证明,通过用Li+逐渐取代K+来改变用于肌动蛋白聚合的培养基盐成分,会导致肌动蛋白组装时间进程呈剂量相关变化。Li+的存在通过增强成核作用和降低稳态下的临界单体浓度来影响体外肌动蛋白聚合。此外,Li+主要通过降低解离速率常数(K-)的绝对值并使能够发生丝-亚基通量的G-肌动蛋白浓度范围(向较低的肌动蛋白单体浓度值)移动来稳定肌动蛋白聚合物。Li+对体外肌动蛋白和微管蛋白聚合的影响表明,细胞骨架结构可能是该离子的一些细胞质靶点。