Servicio de Reumatología, Hospital Universitario de Canarias, La Laguna, Santa Cruz de Tenerife, Spain.
Eur J Immunol. 2011 Dec;41(12):3436-42. doi: 10.1002/eji.201141764.
The P-selectin glycoprotein ligand-1 (PSGL-1) is involved in the initial contact of leukocytes with activated endothelium, and its adhesive function is regulated through its proteolytic processing. We have found that the metalloprotease ADAM8 is both associated with PSGL-1 through the ezrin–radixin–moesin actin-binding proteins and able to cause the proteolytic cleavage of this adhesion receptor. Accordingly, ADAM8 knockdown increases PSGL-1 expression, and functional assays show that ADAM8 is able to reduce leukocyte rolling on P-selectin and hence on activated endothelial cells. We conclude that ADAM8 modulates the expression and function of PSGL-1.
P 选择素糖蛋白配体-1（PSGL-1）参与白细胞与活化内皮细胞的初始接触，其黏附功能通过其蛋白水解加工来调节。我们发现，金属蛋白酶 ADAM8 通过 ezrin–radixin–moesin 肌动蛋白结合蛋白与 PSGL-1 相关，并能够导致这种黏附受体的蛋白水解切割。因此，ADAM8 的敲低会增加 PSGL-1 的表达，功能测定表明 ADAM8 能够减少白细胞在 P 选择素上的滚动，进而减少在活化的内皮细胞上的滚动。我们得出结论，ADAM8 调节 PSGL-1 的表达和功能。
