The PDZ-binding domain of syndecan-2 inhibits LFA-1 high-affinity conformation
详细信息 查看全文
- 作者：Xavier Rovira-Clavé ; a ; x.rovira.c@gmail.com" class="auth_mail ; Maria Angulo-Ibá ; ñ ; eza ; maria.angulib@gmail.com" class="auth_mail ; Manuel Reinaa ; 1 ; mreina@ub.edu" class="auth_mail ; Enric Espela ; b ; 1 ; eespel@ub.edu" class="auth_mail
- 关键词：EGTA ; ethylene glycol tetraacetic acid ; HUVEC ; human umbilical vein endothelial cell ; ICAM-1 ; intercellular adhesion molecule 1 ; LFA-1 ; lymphocyte function-associated antigen 1 ; pLys ; poly-d-lysine ; PMA ; phorbol-12-myristate-13-acetate ; PtdIns[4 ; 5]P2 ; phosphatidylinositol 4 ; 5-bisphosphate ; SED ; staphylococcal enterotoxin D ; SDC ; syndecan ; VCAM-1 ; vascular cell adhesion molecule 1 ; VLA-4 ; very late antigen 4
- 刊名：Cellular Signalling
- 出版年：July 2014
- 年：2014
- 卷：26
- 期：7
- 页码：1489-1499
- 全文大小：1300 K
文摘
- •
Adhesion of Jurkat T cells overexpressing syndecan-2 to HUVEC and B cells is examined.
- •
Expression of syndecan-2 in Jurkat impaired adhesion to HUVEC and B cells.
- •
Expression of syndecan-2 in Jurkat locked LFA-1 in a low-affinity conformation.
- •
Syndecan-2 PDZ-binding domain is key to lock LFA-1 in a low-affinity conformation.