Comparison of human eosinophil and neutrophil ligands for P-selectin: ligands for P-selectin differ from those for E-selectin.
Comparison of human eosinophil and neutrophil ligands for P-selectin: ligands for P-selectin differ from those for E-selectin.
复制标题
人嗜酸性粒细胞和中性粒细胞 P-选择素配体的比较：P-选择素的配体与 E-选择素的配体不同。
DOI：
10.1165/ajrcmb.12.3.7532979
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发表时间：
1995
期刊：
影响因子：
--
通讯作者：
Bochner,BS
中科院分区：
文献类型：
--
作者：
Wein,M;Sterbinsky,SA;Bickel,CA;Schleimer,RP;Bochner,BS
嗜酸性粒细胞（EOS）和中性粒细胞（PMN）在各种炎症反应期间表现出不同的积累模式。我们假设 EOS 和 PMN 的 P-选择素配体可能不同，并且这些配体可能与之前鉴定的 E-选择素配体不同。将重组人 P-选择素固定在塑料表面，并比较 51Cr 标记的人 EOS 或 PMN 的粘附力。 EOS 和 PMN 以浓度依赖性方式粘附，具有相似的最大净粘附力。与阻断性 P-选择素抗体预孵育可抑制两种细胞类型的粘附，而非阻断性抗体则不会。为了确定反配体是否是唾液酸化蛋白，在测试粘附之前用各种糖苷酶和蛋白酶处理细胞。神经氨酸酶处理显着抑制两种细胞类型的结合，而内切β-半乳糖苷酶则没有显着效果。用几种蛋白酶进行预处理会降低两种细胞类型的粘附，尽管它们始终对 PMN 结合产生比 EOS 结合更大的抑制。为了确定P-选择素配体是否是其表达或功能可能因细胞活化而改变的表面结构，用各种刺激物对白细胞进行预处理；仅血小板激活因子 (PAF) 治疗会降低白细胞粘附 P-选择素的能力。因此，EOS和PMN上P-选择素的反配体是相似的唾液酸化、蛋白酶敏感、内切β-半乳糖苷酶抗性结构，其功能和/或表达在PAF治疗后降低。这些特征明显不同于报道的 E-选择素的 EOS 和 PMN 配体的特征，并且表明 P-选择素和 E-选择素在体内炎症反应期间 EOS 和 PMN 募集过程中发挥不同的作用。
Eosinophils (EOS) and neutrophils (PMN) display different patterns of accumulation during various inflammatory reactions. We hypothesized that EOS and PMN may differ in their ligands for P-selectin, and that these ligands may differ from those previously identified for E-selectin. Recombinant human P-selectin was immobilized on plastic surfaces and adhesion of 51Cr-labeled human EOS or PMN was compared. EOS and PMN adhered in a concentration-dependent fashion, with similar maximal net adhesion. Preincubation with a blocking P-selectin antibody inhibited adhesion of both cell types, whereas a non-blocking antibody did not. To determine if the counterligands were sialylated proteins, cells were treated with various glycosidases and proteases before testing adhesion. Neuraminidase treatment markedly inhibited binding of both cell types, while endo-beta-galactosidase had no significant effect. Pretreatment with several proteases reduced adhesion of both cell types, although they consistently caused a greater inhibition of PMN binding than EOS binding. To determine whether the P-selectin ligands were surface structures whose expression or function may be altered by cell activation, leukocytes were pretreated with various stimuli; only platelet-activating factor (PAF) treatment reduced the capacity of leukocytes to adhere to P-selectin. Thus, the counterligands for P-selectin on EOS and PMN are similar sialylated, protease-sensitive, endo-beta-galactosidase-resistant structures, whose function and/or expression is reduced following treatment with PAF. These characteristics are clearly different than those reported for EOS and PMN ligands for E-selectin, and suggest disparate roles for P-selectin and E-selectin during EOS and PMN recruitment during inflammatory responses in vivo.