Vasodilator-stimulated phosphoprotein is a substrate for protein kinase C
Vasodilator-stimulated phosphoprotein is a substrate for protein kinase C
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DOI：
10.1016/s0014-5793(03)01435-2
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发表时间：
2004-01-02
期刊：
影响因子：
3.5
通讯作者：
Clowes, AW
中科院分区：
文献类型：
--
作者：
Chitaley, K;Chen, L;Clowes, AW
血管扩张剂刺激磷酸化蛋白（VASP）是一种定位于病灶接触区域的肌动蛋白结合蛋白，是环腺苷单磷酸/环鸟苷单磷酸（cAMP/cGMP）依赖蛋白激酶（PKA， PKG）的底物。在这项研究中，我们发现血清刺激血管平滑肌细胞（SMCs）诱导VASP Ser157磷酸化，其机制不依赖于PKA或PKG，我们测试了蛋白激酶C (PKC)，一种细胞骨架功能的调节剂，参与其中的可能性。PKC抑制或下调可阻止大鼠血管SMCs中血清诱导的VASP Ser157位点磷酸化。此外，重组PKCalpha直接磷酸化VASP上的Ser157。总之，我们的数据支持PKC磷酸化VASP并介导血清诱导的VASP调节的假设。(C) 2003年欧洲生化学会联合会。Elsevier B.V.版权所有。
Vasodilator-stimulated phosphoprotein (VASP), an actin binding protein localized to areas of focal contacts, is a substrate for the cyclic adenosine monophosphate/cyclic guanosine monophosphate (cAMP/cGMP)-dependent protein kinases (PKA, PKG). In this study, we show that serum stimulation of vascular smooth muscle cells (SMCs) induces VASP phosphorylation on Ser157, in a mechanism not dependent on PKA or PKG. We tested the possibility that protein kinase C (PKC), a regulator of cytoskeletal function, is involved. PKC inhibition or down-regulation prevented serum-induced phosphorylation of VASP at Ser157 in rat vascular SMCs. Additionally, recombinant PKCalpha directly phosphorylated Ser157 on VASP. In summary, our data support the hypothesis that PKC phosphorylates VASP and mediates serum-induced VASP regulation. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.