Journal of Biomedicine and Biotechnology
Volume 2007 (2007), Article ID 97654, 10 pages
http://dx.doi.org/10.1155/2007/97654
Eisenia fetida Protease-III-1 Functions in Both Fibrinolysis and Fibrogenesis
1State Key Laboratory of Brain and Cognitive Science, Institute of Biophysics, Baiao Pharmaceuticals
Beijing C.L., Chinese Academy of Sciences, 15 Da Tun Road, Chao Yang District, Beijing 100101, China
2Graduate School, Chinese Academy of Sciences, Beijing 100039, China
3College of Life Science, South China Normal University, Guangzhou 510631, China
Received 10 December 2006; Accepted 19 March 2007
Academic Editor: Abdelali Haoudi
Copyright © 2007 Jing Zhao et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Abstract
The fibrinolytic function of earthworm protease-III-1 (EfP-III-1) has
been studied in recent years. Here, we found that EfP-III-1 acted not
only in fibrinogenolysis, but also in fibrogenesis.
We have used EfP-III-1 to hydrolyze fibrinogen, and to activate
plasminogen and prothrombin. Based on the N-terminal sequences of the hydrolytic
fragments, EfP-III-1 was showed to specifically recognize the carboxylic
sites of arginine and lysine. Analyses by fibrinogenolysis mapping and amino acid
sequencing revealed that the isozyme could cleave the alpha, beta, and gamma chains
of fibrinogen, showing a high