Lavagno L, Ferrero E, Ortolan E, Malavasi F, Funaro A
Laboratory of Immunogenetics, Department of Genetics, Biology and Biochemistry, University of Torino, Torino, Italy.
J Biol Regul Homeost Agents. 2007;21(1-2):5-11.
CD157 is a GPI-anchored cell surface glycoprotein expressed by human peripheral blood neutrophils. Cross-linking of CD157 induces intracellular Ca2+ mobilization and re-shaping in neutrophils, thus regulating their adhesive and migratory properties. Results obtained by immunolocalization and confocal microscopy indicate that CD157 lies in close proximity to the CD11b/CD18 complex which is strongly expressed on the activated neutrophil cell membrane where it plays a predominant role in adhesion. This study analyses the physical association between CD157 and CD18 in human neutrophils by co-immunoprecipitation experiments. The anti-CD157 monoclonal antibody RF3 co-precipitates CD18, and the anti-CD18 antibody TS1/18 co-precipitates CD157 from human neutrophil lysates. These results confirm that CD157 physically interacts with CD11b/CD18 complex in human neutrophils.
CD157是一种由人外周血中性粒细胞表达的糖基磷脂酰肌醇（GPI）锚定的细胞表面糖蛋白。CD157的交联可诱导中性粒细胞内的Ca2+动员和重塑，从而调节其黏附性和迁移特性。免疫定位和共聚焦显微镜检查结果表明，CD157与CD11b/CD18复合物紧密相邻，该复合物在活化的中性粒细胞细胞膜上强烈表达，在黏附中起主要作用。本研究通过免疫共沉淀实验分析了人中性粒细胞中CD157与CD18之间的物理关联。抗CD157单克隆抗体RF3能共沉淀CD18，抗CD18抗体TS1/18能从人中性粒细胞裂解物中共沉淀CD157。这些结果证实，在人中性粒细胞中，CD157与CD11b/CD18复合物存在物理相互作用。
