Hu G F, Riordan J F
Center for Biochemical and Biophysical Sciences and Medicine, Harvard Medical School, Boston, MA 02115.
Biochem Biophys Res Commun. 1993 Dec 15;197(2):682-7. doi: 10.1006/bbrc.1993.2533.
Angiogenin interacts with actin to form a complex, which like actin itself, can accelerate plasmin generation by tissue plasminogen activator (tPA). In contrast to actin, the angiogenin-actin complex does not inhibit plasmin activity. In the presence of the angiogenin-actin complex, the overall proteolytic activity of a mixture of plasminogen and tPA is 11-fold higher than in its absence and 6-fold higher than in the presence of actin alone. These results suggest that binding and displacement of cell surface actin by angiogenin might be involved in cell migration and tumor invasion, processes that depend on the proteolytic degradation of basement membrane and the extracellular matrix. Therefore, the activity of the angiogenin-actin complex reported here may have physiological and pathological significance in the process of angiogenin-induced angiogenesis.
血管生成素与肌动蛋白相互作用形成复合物,该复合物与肌动蛋白本身一样,能够通过组织纤溶酶原激活剂(tPA)加速纤溶酶的生成。与肌动蛋白不同,血管生成素 - 肌动蛋白复合物不会抑制纤溶酶活性。在血管生成素 - 肌动蛋白复合物存在的情况下,纤溶酶原和tPA混合物的整体蛋白水解活性比不存在该复合物时高11倍,比仅存在肌动蛋白时高6倍。这些结果表明,血管生成素对细胞表面肌动蛋白的结合和置换可能参与细胞迁移和肿瘤侵袭过程,这些过程依赖于基底膜和细胞外基质的蛋白水解降解。因此,本文报道的血管生成素 - 肌动蛋白复合物的活性在血管生成素诱导的血管生成过程中可能具有生理和病理意义。