Changes in K+,Na+-sensitive actin gelation factor during the differentiation of myeloid leukemia cells.
Changes in K+,Na+-sensitive actin gelation factor during the differentiation of myeloid leukemia cells.
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粒细胞白血病细胞分化过程中K、Na敏感性肌动蛋白凝胶因子的变化。
DOI：
10.1093/oxfordjournals.jbchem.a135096
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发表时间：
1985
期刊：
影响因子：
--
通讯作者：
K. Nagata
中科院分区：
文献类型：
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作者：
K. Takagi;Y. Ichikawa;K. Nagata
从小鼠白血病细胞系（M1）中分离出由两个38，000道尔顿肽组成的同源二聚体蛋白。38 K-二聚体蛋白与纯化的骨骼肌肌动蛋白的结合摩尔比在1：3时饱和，并且当38 K-二聚体/肌动蛋白的比率超过1：12时，发生凝胶化。这种凝胶化被10 mM KCl或20 mM NaCl的存在完全抑制。蛋白质诱导肌动蛋白丝成束，这需要更高的38 K-二聚体/肌动蛋白的比例，不受单价阳离子的存在。在Ml细胞的分化过程中，38 K蛋白对单价阳离子的敏感性降低;也就是说，需要20 mM KCl或50 mM NaCl来抑制从分化细胞分离的38 K蛋白的胶凝。另一方面，在分化过程中，Ml细胞的细胞内K+含量从70 +/-5mM降至18 +/-3mM，Na+从10 +/-5mM升至40 +/-10mM。这些发现表明，分化带来了有利于38 K蛋白诱导肌动蛋白凝胶化的条件，反过来，在该细胞系中仅在分化后诱导的运动和吞噬活性。
A homodimer protein consisting of two 38,000 dalton peptides was isolated from a murine leukemia cell line (M1). The binding molar ratio of the 38K-dimer protein to purified skeletal muscle actin was saturated at 1:3, and when the 38K-dimer/actin ratio exceeded 1:12, gelation occurred. This gelation was completely inhibited by the presence of either 10 mM KCl or 20 mM NaCl. The protein induced actin filament bundling, which required a higher 38K-dimer/actin ratio and was not affected by the presence of monovalent cations. During the differentiation of Ml cells, the sensitivity of the 38K protein to monovalent cations was decreased; that is 20 mM KCl or 50 mM NaCl was required to inhibit the gelation by the 38K protein isolated from differentiated cells. On the other hand, the intracellular K+ content of Ml cells decreased from 70 +/- 5 mM to 18 +/- 3 mM, and Na+ increased from 10 +/- 5 mM to 40 +/- 10 mM during the differentiation. These findings suggest that the differentiation brought about conditions favourable for the 38K protein to induce actin gelation, and in turn, the locomotive and phagocytic activities which were induced only after differentiation in this cell line.