The metalloprotease ADAM8 is associated with and regulates the function of the adhesion receptor PSGL-1 through ERM proteins
The metalloprotease ADAM8 is associated with and regulates the function of the adhesion receptor PSGL-1 through ERM proteins
复制标题
DOI：
10.1002/eji.201141764
复制
发表时间：
2011-12-01
影响因子：
5.4
通讯作者：
Urzainqui, Ana
中科院分区：
文献类型：
--
作者：
Dominguez-Luis, Maria;Lamana, Amalia;Urzainqui, Ana
p -选择素糖蛋白配体-1 （PSGL-1）参与白细胞与活化的内皮细胞的初始接触，其粘附功能通过其蛋白水解过程受到调节。我们发现金属蛋白酶ADAM8既通过ezrin-radixin-moesin肌动蛋白结合蛋白与PSGL-1相关联，又能引起该粘附受体的蛋白水解裂解。因此，ADAM8敲低会增加PSGL-1的表达，功能分析表明ADAM8能够减少白细胞对p -选择素的滚动，从而减少活化内皮细胞的滚动。我们认为ADAM8调控PSGL-1的表达和功能。
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.