期刊
FRONTIERS IN IMMUNOLOGY
卷 9, 期 -, 页码 -出版社
FRONTIERS MEDIA SA
DOI: 10.3389/fimmu.2018.02474
关键词
CD9; ADAM17; alpha 5 beta 1; integrin; tetraspanin; cell adhesion; fibronectin; metalloproteinase
类别
资金
- Ministerio Espanol de Economia y Competitividad (MINECO) [SAF2016-77096-R]
- Fundacion Ramon Areces Ayudas a la Investigacion en Ciencias de la Vida y de la Materia
- [SFB 877]
- [SPP1710]
Integrin alpha 5 beta 1 is a crucial adhesion molecule that mediates the adherence of many cell types to the extracellular matrix through recognition of its classic ligand fibronectin as well as to other cells through binding to an alternative counter-receptor, the metalloproteinase ADAM17/TACE. Interactions between integrin alpha 5 beta 1 and ADAM17 may take place both in trans (between molecules expressed on different cells) or in cis (between molecules expressed on the same cell) configurations. It has been recently reported that the cis association between alpha 5 beta 1 and ADAM17 keeps both molecules inactive, whereas their dissociation results in activation of their adhesive and metalloproteinase activities. Here we show that the tetraspanin CD9 negatively regulates integrin alpha 5 beta 1-mediated cell adhesion by enhancing the cis interaction of this integrin with ADAM17 on the cell surface. Additionally we show that, similarly to CD9, the monoclonal antibody 2A10 directed to the disintegrin domain of ADAM17 specifically inhibits integrin alpha 5 beta 1-mediated cell adhesion to its ligands fibronectin and ADAM17.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据