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首页> 外文期刊>Cell motility and the cytoskeleton >Calyculin A-induced actin phosphorylation and depolymerization in renal epithelial cells.
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Calyculin A-induced actin phosphorylation and depolymerization in renal epithelial cells.

机译：Calyculin A诱导肾上皮细胞中的肌动蛋白磷酸化和解聚。

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This study reports actin phosphorylation and coincident actin cytoskeleton alterations in renal epithelial cell line, LLC-PK1. Serine phosphorylation of actin was first observed in vitro after the cell lysate was incubated with phosphatase inhibitors and ATP. Both the phosphorylated actin and actin kinase activities were found in the cytoskeletal fraction. Actin phosphorylation was later detected in living LLC-PK1 cells after incubation with the phosphatase inhibitor calyculin A. Calyculin A-induced actin phosphorylation was associated with reorganization of the actin cytoskeleton, including net actin depolymerization, loss of cell-cell junction and stress fiber F-actin filaments, and redistribution of F-actin filaments in the periphery of the rounded cells. Actin phosphorylation was abolished by 3-h ATP depletion but not by the non-specific kinase inhibitor staurosporine. These results demonstrate that renal epithelial cells contain kinase/phosphatase activities and actin can be phosphorylated in LLC-PK1 cells. Actin phosphorylation may play an important role in regulating the organization of the actin cytoskeleton in renal epithelium. Cell Motil. Cytoskeleton 54:286-295, 2003. Copyright 2003 Wiley-Liss, Inc.
机译：这项研究报告肾上皮细胞系，LLC-PK1中的肌动蛋白磷酸化和同时发生的肌动蛋白细胞骨架改变。将细胞裂解液与磷酸酶抑制剂和ATP孵育后，首先在体外观察到肌动蛋白的丝氨酸磷酸化。磷酸化的肌动蛋白和肌动蛋白激酶的活性都发现在细胞骨架部分。在与磷酸酶抑制剂calyculin A孵育后，后来在活的LLC-PK1细胞中检测到肌动蛋白磷酸化。calyculinA诱导的肌动蛋白磷酸化与肌动蛋白细胞骨架的重组有关，包括净肌动蛋白解聚，细胞-细胞连接丧失和应力纤维F -肌动蛋白丝，以及F-肌动蛋白丝在圆形细胞周围的重新分布。肌动蛋白的磷酸化被3-h ATP消耗所消除，但非特异性激酶抑制剂星形孢菌素则没有。这些结果表明，肾上皮细胞具有激酶/磷酸酶活性，并且肌动蛋白可以在LLC-PK1细胞中被磷酸化。肌动蛋白磷酸化可能在调节肾上皮肌动蛋白细胞骨架的组织中起重要作用。细胞动力。 Cytoskeleton 54：286-295，2003。版权所有2003 Wiley-Liss，Inc.。

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