D'Souza S E, Byers-Ward V J, Gardiner E E, Wang H, Sung S S
Joseph J. Jacobs Center for Thrombosis and Vascular Biology, Department of Molecular Cardiology, The Cleveland Clinic Foundation, Cleveland, OH 44195, USA.
J Biol Chem. 1996 Sep 27;271(39):24270-7. doi: 10.1074/jbc.271.39.24270.
Monocytic cells bind fibrinogen (fg) through integrin alphaMbeta2. fg-bound monocytic cells demonstrate an enhanced adhesion to endothelial cells, which is dependent on intercellular adhesion molecule-1 (ICAM-1). Our studies differentiate fg interactions with stimulated and resting endothelial cells, which are ICAM-1 dependent and independent, respectively. This report documents a direct interaction between fg and intact ICAM-1 and with a two-Ig domain form of ICAM-1. A small region within the first Ig domain of ICAM-1, ICAM-1-(8-21) (KVILPRGGSVLVTC), was identified to interact with fg in a specific and selective manner. ICAM-1-(8-21) bound to plasmin-derived fg fragments X, D100, and D80 but not to fragment E. Consistent with this finding, fg gamma-chain peptide, fg-gamma-117-133, blocked fg interaction with ICAM-1-(8-2 1. ICAM-1-(8-21) peptide and antibodies directed against ICAM-1-(8-21) also blocked the adhesion and binding of ICAM-1-bearing Raji cells with fg. ICAM-1-(8-21) and fg-gamma-117-133 are likely to be one of the contact pairs mediating fg-ICAM-1 interactions.
单核细胞通过整合素αMβ2结合纤维蛋白原（fg）。结合了fg的单核细胞对内皮细胞的黏附增强，这依赖于细胞间黏附分子-1（ICAM-1）。我们的研究区分了fg与刺激的和静息的内皮细胞的相互作用，它们分别依赖和不依赖ICAM-1。本报告记录了fg与完整ICAM-1以及ICAM-1的双Ig结构域形式之间的直接相互作用。确定了ICAM-1第一个Ig结构域内的一个小区域ICAM-1-(8-21)（KVILPRGGSVLVTC）以特异性和选择性方式与fg相互作用。ICAM-1-(8-21)与纤溶酶衍生的fg片段X、D100和D80结合，但不与片段E结合。与这一发现一致，fgγ链肽fg-γ-117-133阻断了fg与ICAM-1-(8-21)的相互作用。ICAM-1-(8-21)肽和针对ICAM-1-(8-21)的抗体也阻断了携带ICAM-1的Raji细胞与fg的黏附和结合。ICAM-1-(8-21)和fg-γ-117-133可能是介导fg-ICAM-1相互作用的接触对之一。
