• 主题
高级搜索  >
历史搜索 清空历史
首页> 美国卫生研究院文献>Scientific Reports >Interaction of Complement Defence Collagens C1q and Mannose-Binding Lectin with BMP-1/Tolloid-like Proteinases
【2h】

Interaction of Complement Defence Collagens C1q and Mannose-Binding Lectin with BMP-1/Tolloid-like Proteinases

机译：补体防御胶原C1q和甘露糖结合凝集素与BMP-1 / Tolloid样蛋白酶的相互作用。

代理获取
本网站仅为用户提供外文OA文献查询和代理获取服务，本网站没有原文。下单后我们将采用程序或人工为您竭诚获取高质量的原文，但由于OA文献来源多样且变更频繁，仍可能出现获取不到、文献不完整或与标题不符等情况，如果获取不到我们将提供退款服务。请知悉。
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

The defence collagens C1q and mannose-binding lectin (MBL) are immune recognition proteins that associate with the serine proteinases C1r/C1s and MBL-associated serine proteases (MASPs) to trigger activation of complement, a major innate immune system. Bone morphogenetic protein-1 (BMP-1)/tolloid-like proteinases (BTPs) are metalloproteinases with major roles in extracellular matrix assembly and growth factor signalling. Despite their different functions, C1r/C1s/MASPs and BTPs share structural similarities, including a specific CUB-EGF-CUB domain arrangement found only in these enzymes that mediates interactions with collagen-like proteins, suggesting a possible functional relationship. Here we investigated the potential interactions between the defence collagens C1q and MBL and the BTPs BMP-1 and mammalian tolloid-like-1 (mTLL-1). C1q and MBL bound to immobilized BMP-1 and mTLL-1 with nanomolar affinities. These interactions involved the collagen-like regions of the defence collagens and were inhibited by pre-incubation of C1q or MBL with their cognate complement proteinases. Soluble BMP-1 and mTLL-1 did not inhibit complement activation and the defence collagens were neither substrates nor inhibitors of BMP-1. Finally, C1q co-localized with BMP-1 in skin biopsies following melanoma excision and from patients with recessive dystrophic epidermolysis bullosa. The observed interactions provide support for a functional link between complement and BTPs during inflammation and tissue repair.
机译：防御性胶原C1q和甘露糖结合凝集素（MBL）是与丝氨酸蛋白酶C1r / C1s和MBL相关的丝氨酸蛋白酶（MASP）相关的免疫识别蛋白，可触发补体的激活，这是一种主要的先天免疫系统。骨形态发生蛋白-1（BMP-1）/类瘤样蛋白酶（BTP）是金属蛋白酶，在细胞外基质组装和生长因子信号传导中起主要作用。尽管它们的功能不同，但C1r / C1s / MASP和BTP具有结构相似性，包括仅在介导与胶原样蛋白相互作用的这些酶中发现的特定CUB-EGF-CUB结构域排列，表明可能存在功能关系。在这里，我们研究了防御性胶原C1q和MBL与BTP BMP-1和哺乳动物Tolloid-like-1（mTLL-1）之间的潜在相互作用。 C1q和MBL以纳摩尔亲和力与固定的BMP-1和mTLL-1结合。这些相互作用涉及防御胶原蛋白的胶原蛋白样区域，并通过将C1q或MBL与它们的同源补体蛋白酶预孵育而被抑制。可溶性BMP-1和mTLL-1不会抑制补体激活，而防御胶原既不是BMP-1的底物也不是其抑制剂。最后，C1q与BMP-1在黑色素瘤切除后的皮肤活检中以及隐性营养不良性大疱性表皮松解症患者中共定位。观察到的相互作用为炎症和组织修复过程中补体和BTP之间的功能联系提供了支持。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
代理获取

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