Plasminogen N-terminal activation peptide modulates the activity of angiostatin-related peptides on endothelial cell proliferation and migration |
| |
Authors: | Hayashi Moyuru Tamura Yosuke Dohmae Naoshi Kojima Soichi Shimonaka Motoyuki |
| |
Institution: | a Department of Chemistry, Tokyo University of Science, 1-3 Kagurazaka, Shinjuku-ku, Tokyo 162-8601, Japan b Biomolecular Characterization Team, RIKEN, Wako-shi, Saitama 351-0198, Japan c Molecular Cellular Pathology Research Unit, RIKEN, Wako-shi, Saitama 351-0198, Japan |
| |
Abstract: | Angiostatin, a potent inhibitor of angiogenesis, is derived from the fibrinolytic proenzyme, plasminogen, by enzymatic processing. Plasminogen N-terminal activation peptide (PAP) is one of the products concomitantly released aside from angiostatin (kringles 1-4) and mini-plasminogen (kringle 5 plus the catalytic domain) when plasminogen is processed. To determine whether PAP alone or together with the angiostatin-related peptides derived from the processing of plasminogen modulate the proliferation and motility of endothelial cells, we have generated a recombinant PAP and used it to study its effects on endothelial cells in the presence and absence of the angiostatin-related peptides. Our results showed that PAP alone slightly increased the migration but not the proliferation of endothelial cells. However, in the presence of the angiostatin-related peptides, PAP attenuated the inhibitory activity of the angiostatin-related peptides on the proliferation and migration of endothelial cells. The inhibitory effect of PAP on the angiostatin-related peptides could be due to its binding to the kringle domains of the latter peptides. |
| |
Keywords: | Plasminogen Plasminogen N-terminal activation peptide Angiostatin Kringle domain |
本文献已被 ScienceDirect PubMed 等数据库收录! |
|