...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Biological chemistry >Attenuated Kinin Release from Human Neutrophil Elastase-Pretreated Kininogens by Tissue and Plasma Kallikreins
【24h】

Attenuated Kinin Release from Human Neutrophil Elastase-Pretreated Kininogens by Tissue and Plasma Kallikreins

机译：通过组织和血浆激肽释放酶从人中性粒细胞弹性蛋白酶预处理的激肽原中减弱激肽的释放

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Components of kinin-forming systems operating at inflammatory sites are likely to interact with elastase that is released by recruited neutrophils and may, at least temporarily, constitute the major proteolytic activity present at these sites. The aim of this work was to determine the effect of kininogen degradation by human neutrophil elastase (HNE) on kinin generation by tissue and plasma kallikreins. We shjow that the digestion of both low molecular mass (LK) and high molecular mass (HK) forms of human kininogen by HNE renders them essentially unsusceptible to processing by human urinary kallikrein (tissue-type) and also significantly quenches the kinin release from HK by plasma kallikrein. Studies with synthetic model heptadecapeptide substrates, ISLMKRPPGFSPFRSSR and SLMKRPPGFSPFRSSRI, confirmed the inability of tissue kallikrein to process peptides at either termini of the internal kinin sequence, while plasma kallikrein wasd shown to release the kinin C-terminus relatively easily. The HNE-generated fragments of kininogens were separated by HPLC and the fractions containing internal kinin sequences were identified by a kininspecific immunoenzymatic test after trypsin digestion. These fractions were analyzed by electrosparayionization mass spectrometry. In this way, multiple peptides containing the kinin sequence flanked by only a few amino acid residues at each terminus were identified in elastase digests of both LK and HK. These results suggest that elastase may be involved in quenching the kinin-release cascade at the late stages of the inflammatory reaction.
机译：在炎症部位起作用的激肽形成系统的成分很可能与由募集的嗜中性粒细胞释放的弹性蛋白酶相互作用，并且可能至少暂时构成这些部位存在的主要蛋白水解活性。这项工作的目的是确定人嗜中性粒细胞弹性蛋白酶（HNE）对激肽原的降解对组织和血浆激肽释放酶激肽产生的影响。我们认为，通过HNE消化人激肽原的低分子量（LK）和高分子量（HK）形式均使其基本上不易被人尿激肽释放酶（组织型）加工，并且还显着抑制了HK释放的激肽通过血浆激肽释放酶。对合成模型七肽底物ISLMKRPPGFSPFRSSR和SLMKRPPGFSPFRSSRI的研究证实了激肽释放酶不能在内部激肽序列的任一末端处理肽，而血浆激肽释放酶则显示相对容易释放激肽C端。通过HPLC分离HNE产生的激肽原的片段，并在胰蛋白酶消化后通过激肽特异性免疫酶测试鉴定含有内部激肽序列的级分。这些组分通过电喷雾质谱法分析。以此方式，在LK和HK的弹性蛋白酶消化物中鉴定出了包含激肽序列的多个肽，所述肽在每个末端仅侧接几个氨基酸残基。这些结果表明，在炎症反应的后期，弹性蛋白酶可能参与了激肽释放级联的猝灭。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号