Interactions between galectin-3 and Mac-2-binding protein mediate cell-cell adhesion.
Interactions between galectin-3 and Mac-2-binding protein mediate cell-cell adhesion.
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发表时间：
1996-10
期刊：
影响因子：
11.2
通讯作者：
Hidenori Inohara;Shiro Akahani;K. Koths;A. Raz
中科院分区：
文献类型：
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作者：
Hidenori Inohara;Shiro Akahani;K. Koths;A. Raz
Galectin-3是一种β-半乳糖苷类凝集素，参与细胞相互作用的多种过程。最近，Mac-2结合蛋白被确定为其配体。Mac-2结合蛋白是一种高度N-糖基化的分泌型蛋白，其亚基Mr为97,000。本研究描述了Galectin-3和Mac-2结合蛋白在整个细胞中的相互作用，并测量了它们的相对表达水平。A375细胞与亲和纯化的Mac-2结合蛋白孵育后，其与细胞表面的Galectin-3以特定的碳水化合物依赖的方式结合。Mac-2结合蛋白还可诱导同型细胞聚集，这种聚集可被抗Galectin-3抗体的乳糖或Fab‘片段抑制。Northern印迹分析显示Galectin-3和Mac-2结合蛋白的转录调控存在差异。这些结果为Mac-2结合蛋白的功能提供了第一个直接证据，并提示它可能通过与Galectin-3的相互作用在肿瘤细胞转移过程中发挥作用。
Galectin-3 is a beta-galactoside-specific lectin implicated in diverse processes involved in cellular interactions. Recently, the Mac-2-binding protein, a heavily N-glycosylated secreted protein with a subunit Mr of 97,000, was identified as its ligand. The present study characterizes the interaction between galectin-3 and Mac-2-binding protein in whole cells and measures their relative expression levels. Incubation of A375 cells with affinity-purified Mac-2-binding protein resulted in its binding to galectin-3 on the cell surface in a specific carbohydrate-dependent manner. Mac-2-binding protein also induced homotypic cell aggregation, which was inhibited by lactose or Fab' fragments of an anti-galectin-3 antibody. Northern blotting analysis revealed differences in the transcriptional regulation of galectin-3 and Mac-2-binding protein. These results provide the first direct evidence for a Mac-2-binding protein function and suggest that it may play a role in tumor cell embolization during metastasis through interaction with galectin-3.