<em>Eisenia fetida</em> Protease-III-1 Functions in Both Fibrinolysis and Fibrogenesis

Zhao, Jing; Pan, Rong; He, Jian; Liu, Ying; Li, Dong-Feng; He, Rong-Qiao

doi:https://doi.org/10.1155/2007/97654

BioMed Research International

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Volume 2007 | Article ID 097654 | https://doi.org/10.1155/2007/97654

Eisenia fetida Protease-III-1 Functions in Both Fibrinolysis and Fibrogenesis

Jing Zhao,^1,2Rong Pan,^1,2Jian He,^1,2Ying Liu,^1,2Dong-Feng Li,³and Rong-Qiao He^1,2

Academic Editor: Abdelali Haoudi

Received10 Dec 2006

Accepted19 Mar 2007

Published24 May 2007

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.

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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.

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