Galectin-3 promotes adhesion of human neutrophils to laminin.
Galectin-3 promotes adhesion of human neutrophils to laminin.
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DOI：
10.4049/jimmunol.156.10.3939
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发表时间：
1996-05
影响因子：
4.4
通讯作者：
I. Kuwabara;Fu-Tong Liu
中科院分区：
文献类型：
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作者：
I. Kuwabara;Fu-Tong Liu
Galectin-3 是由三个结构域组成的不断增长的动物凝集素家族的一员，其中氨基末端的一半由短片段和串联重复组成，羧基末端的一半代表碳水化合物识别结构域。此前，我们已经证明半乳糖凝集素 3 与人类中性粒细胞表面结合并能够激活这些细胞。我们现在研究了外源性半乳糖凝集素-3对人中性粒细胞粘附到层粘连蛋白包被的微量滴定板上的影响，发现这种凝集素以剂量依赖性方式促进粘附。该效果取决于凝集素的碳水化合物结合功能及其氨基末端区域。尽管凝集素结合不需要 Ca2+ 和 Mg2+，但在 EDTA 存在下，半乳糖凝集素 3 诱导的粘附显着降低，并且与 37 摄氏度相比，4 摄氏度时的粘附显着降低。半乳糖凝集素 3 还诱导中性粒细胞粘附到纤连蛋白，而纤连蛋白不被凝集素识别，但需要更高浓度的凝集素，并且 效果完全取决于Ca2+和Mg2+。我们得出结论，galectin-3 通过两种不同机制的组合诱导中性粒细胞粘附到层粘连蛋白：1) 凝集素以碳水化合物依赖性和 Ca2+-、Mg2+ 独立的方式将中性粒细胞与层粘连蛋白桥接起来，2) 在二价阳离子存在的情况下，凝集素诱导中性粒细胞活化，从而产生正向调节 其他细胞粘附分子并增强对层粘连蛋白的粘附。结果表明，galectin-3 可能在中性粒细胞穿过炎症部位基底膜的过程中发挥作用。
Galectin-3 is a member of a growing family of animal lectins composed of three domains, with the amino-terminal half consisting of a short segment followed by tandem repeats, and the carboxyl-terminal half representing the carbohydrate-recognition domain. Previously, we have shown that galectin-3 binds to the surface of human neutrophils and is capable of activating these cells. We have now studied the effect of exogenous galectin-3 on adhesion of human neutrophils to laminin-coated microtiter plates and found that this lectin promotes the adhesion in a dose-dependent manner. The effect was dependent on the lectin's carbohydrate-binding function, as well as its amino-terminal region. The galectin-3-induced adhesion was reduced significantly in the presence of EDTA, even though Ca2+ and Mg2+ are not required for the lectin binding, and the adhesion was significantly less at 4 degrees C, as compared with 37 degrees C. Galectin-3 also induced neutrophil adhesion to fibronectin, which is not recognized by the lectin, but much higher concentrations of the lectin were required, and the effect is completely dependent on Ca2+ and Mg2+. We conclude that galectin-3 induces neutrophil adhesion to laminin through a combination of two distinct mechanisms: 1) the lectin bridges neutrophils to laminin, in a carbohydrate-dependent and Ca2+-, Mg2+-independent manner, and 2) the lectin induces activation of neutrophils, in the presence of the divalent cations, resulting in the positive regulation of other cell adhesion molecules and enhanced adhesion to laminin. The results suggest that galectin-3 may play a role in the traversing of neutrophils through the basement membrane at inflammation sites.