Kwiatkowski D J
Hematology-Oncology Unit, Massachusetts General Hospital, Boston 02114.
J Biol Chem. 1988 Sep 25;263(27):13857-62.
Three actin-associated proteins, actin-binding protein, gelsolin, and profilin, influence gelation, solation, and polymerization, respectively, of actin in vitro. As assessed with specific cDNA probes and immunoaffinity reagents, a 7-50-fold increase in gelsolin, 3-5-fold increase in actin-binding protein, and less than 2-fold increases in actin and profilin protein and mRNA levels accompanied tetradecanoylphorbolacetate-induced differentiation of the myeloid cell lines U937 and HL60 into macrophage-like cells. Such induction in actin-binding protein or gelsolin did not occur in K562 cells, which respond minimally to tetradecanoylphorbolacetate, or following 1,25-dihydroxyvitamin D3-induced monocyte-like differentiation of U937, which results in a less motile phenotype. These observations suggest that increases in gelsolin and actin-binding protein are essential to the expression of many regulated motile functions which takes place during differentiation of myeloid cells.
三种肌动蛋白相关蛋白，即肌动蛋白结合蛋白、凝溶胶蛋白和前纤维蛋白，分别在体外影响肌动蛋白的凝胶化、溶胶化和聚合。用特异性cDNA探针和免疫亲和试剂评估发现，十四酰佛波醇乙酸酯诱导髓系细胞系U937和HL60分化为巨噬细胞样细胞时，凝溶胶蛋白增加7 - 50倍，肌动蛋白结合蛋白增加3 - 5倍，肌动蛋白和前纤维蛋白的蛋白质及mRNA水平增加不到2倍。在对十四酰佛波醇乙酸酯反应极小的K562细胞中，或在1,25 - 二羟基维生素D3诱导U937分化为单核细胞样细胞（导致运动性较低的表型）后，肌动蛋白结合蛋白或凝溶胶蛋白没有出现这种诱导增加。这些观察结果表明，凝溶胶蛋白和肌动蛋白结合蛋白的增加对于髓系细胞分化过程中发生的许多受调控的运动功能的表达至关重要。
