Pulmonary Research Group, Department of Medicine, University of Alberta, Edmonton, Canada.
Nitric Oxide. 2012 Jan 1;26(1):74-80. doi: 10.1016/j.niox.2011.12.003. Epub 2011 Dec 14.
Mast cells (MC) play a pivotal role in allergic inflammation and nitric oxide (NO) is known to regulate MC function. One mechanism of NO mediated actions is the post-translational modification protein tyrosine nitration mediated by reactive nitrogen species. In this study we identified targets for nitration in the human mast cell line LAD2 after treatment with a nitric oxide donor and with peroxynitrite. Using two dimensional gel electrophoresis and western blot analyses with monoclonal and polyclonal antibodies we identified 15-hydroxy prostaglandin dehydrogenase (PGDH), a major prostaglandin catabolizing enzyme, as a target for nitration in LAD2. This is the first report on expression of this enzyme in MC and also the first report that PGDH is a target of protein tyrosine nitration. Since MC synthesize and metabolize many prostaglandins including prostaglandin E(2), the major substrate for PGDH, nitration of this prostaglandin catabolizing enzyme is likely functionally significant.
肥大细胞（MC）在过敏炎症中发挥关键作用，已知一氧化氮（NO）可调节 MC 功能。NO 介导作用的一种机制是通过活性氮物种介导的蛋白质酪氨酸硝化的翻译后修饰。在这项研究中，我们在人肥大细胞系 LAD2 中鉴定了在使用一氧化氮供体和过氧亚硝酸盐处理后的硝化靶标。使用二维凝胶电泳和单克隆和多克隆抗体的 Western blot 分析，我们鉴定了 15-羟基前列腺素脱氢酶（PGDH），一种主要的前列腺素分解代谢酶，作为 LAD2 中硝化的靶标。这是该酶在 MC 中表达的第一个报道，也是 PGDH 是蛋白质酪氨酸硝化靶标的第一个报道。由于 MC 合成和代谢许多前列腺素，包括 PGDH 的主要底物前列腺素 E2，因此这种前列腺素分解代谢酶的硝化很可能具有功能意义。
