Identification of a glycoprotein ligand for E-selectin on mouse myeloid cells.
Identification of a glycoprotein ligand for E-selectin on mouse myeloid cells.
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DOI：
10.1083/jcb.121.2.449
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发表时间：
1993-04
期刊：
影响因子：
--
通讯作者：
Vestweber D
中科院分区：
文献类型：
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作者：
Levinovitz A;Mühlhoff J;Isenmann S;Vestweber D
E-选择素是一种可诱导的中性粒细胞内皮细胞粘附分子，其功能类似于Ca（2+）依赖性凝集素。使用重组，抗体样形式的小鼠E-选择素，我们已经搜索了糖蛋白配体对小鼠中性粒细胞和中性粒细胞祖细胞系32 D CL 3。我们已经确定了一个150 kD的糖蛋白作为唯一的蛋白质，可以亲和分离与可溶性E-选择素从[35 S]甲硫氨酸/[35 S]半胱氨酸标记的32 D cl 3细胞。这种蛋白的结合是严格的Ca（2+）依赖性的，被细胞粘附阻断单克隆抗体阻断，对小鼠E-选择素，并需要唾液酸的存在下，150 kD的配体。除了250 kD的次要组分外，该糖蛋白也从成熟中性粒细胞中亲和分离，但不能从其他几种非髓细胞系中分离。150-kD糖蛋白是32 D cl 3细胞中唯一的蛋白质，其在一步亲和分离后可通过银染检测。
E-selectin is an inducible endothelial cell adhesion molecule for neutrophils which functions as a Ca(2+)-dependent lectin. Using a recombinant, antibody-like form of mouse E-selectin, we have searched for glycoprotein ligands on mouse neutrophils and the neutrophil progenitor cell line 32D cl 3. We have identified a 150-kD glycoprotein as the only protein which could be affinity-isolated with soluble E- selectin from [35S]methionine/[35S]cysteine-labeled 32D cl 3 cells. Binding of this protein was strictly Ca(2+)-dependent, was blocked by a cell adhesion-blocking mAb against mouse E-selectin, and required the presence of sialic acid on the 150-kD ligand. This glycoprotein was also affinity-isolated from mature neutrophils, in addition to a minor component at 250 kD, but could not be isolated from several other non- myeloid cell lines. The 150-kD glycoprotein was the only protein from 32D cl 3 cells, which was detectable by silver-staining after a one- step affinity-isolation.