Colman R W
Sol Sherry Thrombosis Research Center, Temple University School of Medicine, Philadelphia, PA 19140, USA.
Biol Chem. 2001 Jan;382(1):65-70. doi: 10.1515/BC.2001.011.
Cleavage of high molecular weight kininogen (HK) by plasma kallikrein results in a light chain and a heavy chain (HK). The light chain has two domains: D6, which binds (pre)kallikrein, and D5, which binds to anionic surfaces, including heparin as well as zinc. Initially, HK was thought to be important for surface-activated coagulation. HKa or D5 binds to the urokinase receptor on endothelial cells, thereby enhancing the conversion of prourokinase to urokinase by kallikrein, and, thus, cell-associated fibrinolysis. HKa or D5 is antiadhesive by competing with vitronectin binding to the urokinase receptor and/or forming a complex with vitronectin. D5 inhibits endothelial cell migration, proliferation, tube formation and angiogenesis, thus modulating inflammation and neovascularization.
血浆激肽释放酶对高分子量激肽原（HK）的裂解产生一条轻链和一条重链（HK）。轻链有两个结构域：结合（前）激肽释放酶的D6和结合包括肝素以及锌在内的阴离子表面的D5。最初，HK被认为对表面激活的凝血很重要。HKa或D5与内皮细胞上的尿激酶受体结合，从而增强激肽释放酶将纤溶酶原转化为尿激酶的过程，进而促进细胞相关的纤维蛋白溶解。HKa或D5通过与玻连蛋白竞争结合尿激酶受体和/或与玻连蛋白形成复合物而具有抗黏附作用。D5抑制内皮细胞迁移、增殖、管腔形成和血管生成，从而调节炎症和新生血管形成。
