Bistratene A causes phosphorylation of talin and redistribution of actin microfilaments in fibroblasts: possible role for PKC-delta.
Bistratene A causes phosphorylation of talin and redistribution of actin microfilaments in fibroblasts: possible role for PKC-delta.
复制标题
Bistratene A 导致成纤维细胞中 talin 磷酸化和肌动蛋白微丝重新分布：PKC-delta 的可能作用。
DOI：
10.1006/excr.1996.0378
复制
发表时间：
1996
影响因子：
3.7
通讯作者：
M. Lavin
中科院分区：
文献类型：
--
作者：
D. Watters;B. Garrone;G. Gobert;S. Williams;R. Gardiner;M. Lavin
Bistratene A是一种海洋毒素，可诱导细胞蛋白磷酸化。我们目前的证据表明，这是通过激活蛋白激酶C-δ发生的。在成纤维细胞中，bistratene A导致细胞变圆，并通过荧光免疫组织化学检测到黏着斑蛋白染色和肌动蛋白应力纤维迅速消失。在bistratene A处理后，粘着斑蛋白talin的磷酸化增加，并且这被PKC的特异性抑制剂calphostin C抑制。在毒素存在下，未观察到黏着斑蛋白、微管蛋白或波形蛋白的磷酸化状态发生变化。用bistratene A处理引起PKC-δ从胞质和膜隔室到核部分的重新分布。对任何其他PKC亚型的亚细胞分布没有影响。这些结果表明，talin的磷酸化参与了bistratene A对成纤维细胞中肌动蛋白微丝的破坏，这很可能是由PKC-δ介导的。
Bistratene A is a marine toxin which induces phosphorylation of cellular proteins. Our current evidence indicates that this occurs through activation of protein kinase C-delta. In fibroblasts bistratene A causes rounding up of the cells and a rapid disappearance of vinculin staining and actin stress fibers as detected by fluorescence immunohistochemistry. Phosphorylation of the focal adhesion protein, talin, is increased after bistratene A treatment and this is inhibited by calphostin C, a specific inhibitor of PKC. No changes in the phosphorylation status of vinculin, tubulin, or vimentin were observed in the presence of the toxin. Treatment with bistratene A caused a redistribution of PKC-delta from cytosolic and membrane compartments to the nuclear fraction. There was no effect on the subcellular distribution of any other PKC isoform. These results demonstrate that phosphorylation of talin is implicated in the disruption of actin microfilaments in fibroblasts by bistratene A and that this is most likely mediated by PKC-delta.