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首页> 外文期刊>Journal of Cellular Physiology >Thrombin-induced phosphorylation of the myristoylated alanine-rich C kinase substrate (MARCKS) protein in bovine pulmonary artery endothelial cells.
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Thrombin-induced phosphorylation of the myristoylated alanine-rich C kinase substrate (MARCKS) protein in bovine pulmonary artery endothelial cells.

机译：Thrombin-induced磷酸化的myristoylated alanine-rich C激酶衬底在牛肺动脉(MARCKS)蛋白内皮细胞。

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摘要

Myristoylated alanine-rich C kinase substrates (MARCKS) is a prominent protein kinase C (PKC) substrate that is targeted to the plasma membrane by an aminoterminal myristoyl group. In its nonphosphorylated form, MARCKS cross-links Factin and binds calmodulin (CaM) reciprocally. However, upon phosphorylation by PKC, MARCKS release the actin or CaM MARCKS may therefore act as a CaM sink in resting cells and regulate CaM availability during cell activation. We have demonstrated previously that thrombin-induced myosin light chain (MLC) phosphorylation and increased monolayer permeability in bovine pulmonary artery endothelial cells (BPAEC) require both PKC-and CaM-dependent pathways. We therefore decided to investigate the phosphorylation of MARCKS in BPAEC to ascertain whether this occurs in a temporally relevant manner to participate in the thrombin-induced events. MARCKS is phosphorylated in response to thrombin with a time course similar to that seen with MLC. As expected, MARCKS is also phosphorylatedby phorbol 12-myristate 13 acetate (PMA), a PKC activator, but with a slower onset and more prolonged duration. Bradykinin also enhances MARCKS phosphorylation in BPAEC, but histamine does not. MARCKS is distributed evently between the membrane and cytosol in BPAEC, and neither thrombin nor PMA caused significant translocation of the protein. Specific PKC inhibitors attenuated MARCKS phosphorylation by either thrombin or PMA. Since thrombin-induced MLC phosphorylation is also attenuated by these inhibitors, MARCKS may be involved in MLC kinase activation and subsequent BPAEC contraction. W7, a CaM antagonist, enhances the phosphorylation of MARCKS. This was expected since CaM binding to MARCKS has been shown to decrease MARCKS phosphorylation by PKC. On the other hand, tyrosine kinase inhibitors, genistein and tyrphostin, attenuate MARCKS phosphorylation but have no effect on MLC phosphorylation, suggesting that MARCKS may be phosphorylated by kinases other than PKC. Phosphorylation of MARCKS outside the PKC phosphorylation domain would not be expected to induce the release of CaM. These data provide support for the hypothesis that MARCKS may serve as a regulator of CaM availability in BPAEC.
机译：Myristoylated alanine-rich C激酶基质(MARCKS)是一个著名的蛋白激酶C (PKC)针对等离子体膜基质由一个aminoterminal十四酰组。nonphosphorylated形式,MARCKS交叉连接Factin和钙调蛋白结合(CaM)相互地。根据PKC磷酸化,MARCKS释放肌动蛋白或凸轮MARCKS可能因此作为凸轮水槽在静息细胞和调节凸轮可用性在细胞的激活。之前证明thrombin-induced肌球蛋白轻链磷酸化和(多层陶瓷)在牛单层通透性增加肺动脉内皮细胞(BPAEC)既需要PKC-and CaM-dependent通路。因此决定进行调查的磷酸化MARCKS BPAEC确定这是否发生在暂时相关参与thrombin-induced方式事件。凝血酶时间进程很相似多层陶瓷。phosphorylatedby佛波醇12-myristate 13醋酸(PMA), PKC激活,但较慢的开始长时间的持续时间。提高MARCKS BPAEC磷酸化,但是组胺没有。在BPAEC细胞膜和细胞溶质之间,凝血酶和PMA引起显著易位的蛋白质。减毒MARCKS磷酸化抑制剂凝血酶或PMA。多层陶瓷磷酸化也减毒的抑制剂,MARCKS可能参与多层陶瓷激酶激活和随后BPAEC收缩。一个凸轮的对手,提高磷酸化MARCKS。MARCKS已经被证明可以减少MARCKS磷酸化PKC。酪氨酸激酶抑制剂,染料木黄酮和tyrphostin,减弱MARCKS磷酸化对多层陶瓷没有影响磷酸化,暗示MARCKS可能被激酶磷酸化除了PKC。PKC磷酸化域不会将诱导凸轮的释放。假设MARCKS提供支持作为监管机构的凸轮可用性吗BPAEC。

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