Eisenia fetida Protease-III-1 Functions in Both Fibrinolysis and Fibrogenesis
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...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Hindawi Limited
2007-01-01
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| Series: | Journal of Biomedicine and Biotechnology |
| Online Access: | http://dx.doi.org/10.1155/2007/97654 |
| Summary: | 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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| ISSN: | 1110-7243 1110-7251 |