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首页> 外文期刊>Endothelium: Journal of endothelial cell research >Phosphorylation and localization of protein-zero related (PZR) in cultured endothelial cells.
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Phosphorylation and localization of protein-zero related (PZR) in cultured endothelial cells.

机译：磷酸化和蛋白质零相关（PZR）在培养的内皮细胞中的定位。

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摘要

Protein-zero related (PZR) is an immunoglobulin V (IgV)-type immunoreceptor with two immunoreceptor tyrosine-based inhibitory motifs (ITIMs). PZR interacts with Src homology 2 domain-containing tyrosine phosphatase (SHP-2) via its tyrosine-phosphorylated ITIMs, for which c-Src is a putative kinase. Towards elucidating PZR function in endothelial cells (ECs), the authors cloned PZR from bovine aortic endothelial cells (BAECs) and characterized it. Mature bovine PZR had 94.8% and 92.7% sequence identity with canine and human proteins, respectively, and the two ITIM sequences were conserved among higher vertebrates. PZR was expressed in many cell types and was localized to cell contacts and intracellular granules in BAECs and mesothelioma (REN) cells. Coimmunoprecipitation revealed that PZR, Grb-2-associated binder-1 (Gab1), and platelet endothelial cell adhesion molecule-1 (PECAM-1) were three major SHP-2-binding proteins in BAECs. H(2)O(2) enhanced PZR tyrosine phosphorylation and PZR/SHP-2 interaction in ECs in a dose-and time-dependent manner. To see if tyrosine kinases other than Src are also capable of phosphorylating PZR, the authors cotransfected HEK293 cells with PZR and one of several tyrosine kinases and found that c-Src, c-Fyn, c-Lyn, Csk, and c-Abl, but not c-Fes, phosphorylated PZR and increased PZR/SHP-2 interaction. These results suggest that PZR is a cell adhesion protein that may be involved in SHP-2-dependent signaling at interendothelial cell contacts.
机译：零蛋白相关（PZR）是一种免疫球蛋白V（IgV）型免疫受体，具有两个基于酪氨酸的免疫受体抑制基序（ITIM）。 PZR通过其酪氨酸磷酸化的ITIM与Src同源性2结构域的酪氨酸磷酸酶（SHP-2）相互作用，其中c-Src是一个假定的激酶。为了阐明内皮细胞（EC）中的PZR功能，作者从牛主动脉内皮细胞（BAEC）中克隆了PZR并对其进行了表征。成熟的牛PZR与犬和人蛋白质的序列同一性分别为94.8％和92.7％，并且两个ITIM序列在高级脊椎动物中是保守的。 PZR在多种细胞类型中表达，并定位于BAEC和间皮瘤（REN）细胞中的细胞接触和细胞内颗粒。免疫共沉淀显示，PZR，Grb-2相关黏附剂1（Gab1）和血小板内皮细胞粘附分子1（PECAM-1）是BAEC中的三种主要SHP-2结合蛋白。 H（2）O（2）增强EC中的PZR酪氨酸磷酸化和PZR / SHP-2相互作用，呈剂量和时间依赖性。为了查看除Src以外的酪氨酸激酶是否也能够磷酸化PZR，作者将HEK293细胞与PZR和几种酪氨酸激酶之一共转染，发现c-Src，c-Fyn，c-Lyn，Csk和c-Abl，但c-Fes没有，磷酸化的PZR和增加的PZR / SHP-2相互作用。这些结果表明，PZR是一种细胞粘附蛋白，在内皮细胞接触时可能参与SHP-2依赖性信号传导。

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