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Journal of Biomedicine and Biotechnology
Volume 2007, Article ID 97654, 10 pages
http://dx.doi.org/10.1155/2007/97654
Research Article

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 α-fibrinogenase, moderate β-fibrinogenase, and low γ-fibrinogenase activities. Interestingly, EfP-III-1 activated plasminogen and released active plasmin, suggesting a tPA-like function. Furthermore, EfP-III-1 showed a factor Xa-like function on prothrombin, producing alpha-thrombin. The function in both activating prothrombin and catalyzing fibrinogenolysis suggests that EfP-III-1 may play a role in the balance between procoagulation and anticoagulation.