de Fougerolles A R, Klickstein L B, Springer T A
Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115.
J Exp Med. 1993 Apr 1;177(4):1187-92. doi: 10.1084/jem.177.4.1187.
Based on protein sequence, we have isolated a cDNA for intercellular adhesion molecule 3 (ICAM-3), the most recently defined counter-receptor for lymphocyte function-associated antigen 1 (LFA-1). Expression of the cDNA yields a product that reacts with monoclonal antibody to ICAM-3 and functions as a ligand for LFA-1. The deduced 518-amino acid sequence of the predicted mature protein defines a highly glycosylated type I integral membrane protein with five immunoglobulin (Ig)-like domains. The five Ig-like domains of ICAM-3 are highly homologous with those of human ICAM-1 (52% identity) and human ICAM-2 (37% identity).
基于蛋白质序列,我们分离出了细胞间黏附分子3(ICAM-3)的cDNA,它是淋巴细胞功能相关抗原1(LFA-1)最新确定的反受体。该cDNA的表达产生一种产物,它能与抗ICAM-3单克隆抗体发生反应,并作为LFA-1的配体发挥作用。预测的成熟蛋白推导的518个氨基酸序列定义了一种高度糖基化的I型整合膜蛋白,具有五个免疫球蛋白(Ig)样结构域。ICAM-3的五个Ig样结构域与人ICAM-1的相应结构域高度同源(同一性为52%),与人ICAM-2的相应结构域也高度同源(同一性为37%)。