de Fougerolles A R, Stacker S A, Schwarting R, Springer T A
Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115.
J Exp Med. 1991 Jul 1;174(1):253-67. doi: 10.1084/jem.174.1.253.
In an endeavor to further characterize human intercellular adhesion molecule-2 (ICAM-2), two murine monoclonal antibodies (mAb) were generated to ICAM-2 transfected COS cells, and designated CBR-IC2/1 and CBR-IC2/2. Immunoprecipitated, reduced ICAM-2 migrated as a broad band of Mr 60,000 in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Treatment with N-glycanase revealed a peptide backbone of Mr 31,000, consistent with the size predicted from the cDNA. ICAM-2 had a broad distribution on hematopoietic cell lines and little expression on other cell lines, the sole exception being cultured endothelial cells which possess high levels of ICAM-2. Resting lymphocytes and monocytes expressed ICAM-2, while neutrophils did not. Staining of tissue sections with anti-ICAM-2 mAb confirmed their strong reactivity to vascular endothelium, but demonstrated a lack of ICAM-2 expression on other tissues. Small clusters of ICAM-2 positive cells were, however, seen in germinal centers. In contrast to ICAM-1 there was little or no induction of ICAM-2 expression on lymphocytes or cultured endothelium upon stimulation with inflammatory mediators. One of the two mAb, CBR-IC2/2, was found to totally inhibit binding of ICAM-2+ COS cells to purified lymphocyte function-associated antigen-1 (LFA-1). Using this mAb, LFA-1-dependent binding to both stimulated and unstimulated endothelium was found to be totally accounted for by ICAM-1 and ICAM-2. Homotypic aggregation of an Epstein-Barr virus-transformed B cell line, JY, was found to be solely ICAM-1 and ICAM-2-dependent, while in the case of the T cell lymphoma cell line, SKW3, anti- ICAM-2 mAb in conjunction with anti-ICAM-1 mAb could not inhibit the LFA-1-dependent aggregation. This suggests an additional LFA-1 ligand exists. Using a cell binding assay to purified LFA-1 in conjunction with anti-ICAM-1 and anti-ICAM-2 mAb, we have demonstrated that this putative third ligand for LFA-1 exists on SKW3 and other cell lines.
为了进一步表征人细胞间黏附分子-2(ICAM-2),制备了两种针对ICAM-2转染COS细胞的鼠单克隆抗体(mAb),分别命名为CBR-IC2/1和CBR-IC2/2。免疫沉淀后经还原处理的ICAM-2在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳中迁移为一条Mr 60,000的宽带。用N-糖苷酶处理后显示出一条Mr 31,000的肽骨架,与从cDNA预测的大小一致。ICAM-2在造血细胞系上分布广泛,在其他细胞系上表达很少,唯一的例外是培养的内皮细胞,其ICAM-2水平很高。静息淋巴细胞和单核细胞表达ICAM-2,而中性粒细胞不表达。用抗ICAM-2 mAb对组织切片进行染色证实它们与血管内皮有强烈反应,但显示其他组织上缺乏ICAM-2表达。然而,在生发中心可见小簇ICAM-2阳性细胞。与ICAM-1不同,用炎性介质刺激后,淋巴细胞或培养的内皮细胞上ICAM-2的表达很少或没有诱导。发现两种mAb之一CBR-IC2/2能完全抑制ICAM-2+ COS细胞与纯化的淋巴细胞功能相关抗原-1(LFA-1)的结合。使用该mAb发现,LFA-1依赖的与刺激和未刺激内皮细胞的结合完全由ICAM-1和ICAM-2介导。发现爱泼斯坦-巴尔病毒转化的B细胞系JY的同型聚集仅依赖于ICAM-1和ICAM-2,而对于T细胞淋巴瘤细胞系SKW3,抗ICAM-2 mAb与抗ICAM-1 mAb联合不能抑制LFA-1依赖的聚集。这表明存在一种额外的LFA-1配体。通过将细胞结合试验用于纯化的LFA-1并结合抗ICAM-1和抗ICAM-2 mAb,我们证明了这种推测的LFA-1的第三种配体存在于SKW3和其他细胞系上。