Abstract
Antithrombin inhibits blood coagulation through the interaction with serine proteases in both intrinsic and extrinsic pathways. In addition, antithrombin also shows anti-inflammatory properties, which are independent of its effects on coagulation. This work shows for the first time the cloning and sequencing of antithrombin from a snake species. This predicted protein is composed by 430 amino acids and presents about 64.5% sequence identity to human antithrombin. Biacore experiments revealed that the binding affinity of Bothrops jararaca snake antithrombin to heparin was ~30 times higher than that of human antithrombin. Furthermore, Bothrops jararaca antithrombin is more effective in preventing acute inflammation induced by carrageenan when compared to human antithrombin. Hence, the results showed herein suggest that Bothrops jararaca antithrombin can play a key role in the control of acute inflammation and that this molecule might be used as a pharmacological tool and as a prototype for drug development.
Keywords: Antithrombin, Bothrops jararaca snake, carrageenan, cloning, heparin affinity, inflammation, surface plasmon resonance.
Protein & Peptide Letters
Title:Cloning, Characterization and Anti-Inflammatory Properties of Bothrops jararaca Snake Antithrombin
Volume: 22 Issue: 5
Author(s): Karen de Morais-Zani, Kathleen F. Grego, Ricardo J.S. Torquato, Caroline S. Silva, Aparecida S. Tanaka and Anita M. Tanaka-Azevedo
Affiliation:
Keywords: Antithrombin, Bothrops jararaca snake, carrageenan, cloning, heparin affinity, inflammation, surface plasmon resonance.
Abstract: Antithrombin inhibits blood coagulation through the interaction with serine proteases in both intrinsic and extrinsic pathways. In addition, antithrombin also shows anti-inflammatory properties, which are independent of its effects on coagulation. This work shows for the first time the cloning and sequencing of antithrombin from a snake species. This predicted protein is composed by 430 amino acids and presents about 64.5% sequence identity to human antithrombin. Biacore experiments revealed that the binding affinity of Bothrops jararaca snake antithrombin to heparin was ~30 times higher than that of human antithrombin. Furthermore, Bothrops jararaca antithrombin is more effective in preventing acute inflammation induced by carrageenan when compared to human antithrombin. Hence, the results showed herein suggest that Bothrops jararaca antithrombin can play a key role in the control of acute inflammation and that this molecule might be used as a pharmacological tool and as a prototype for drug development.
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Morais-Zani de Karen, Grego F. Kathleen, Torquato J.S. Ricardo, Silva S. Caroline, Tanaka S. Aparecida and Tanaka-Azevedo M. Anita, Cloning, Characterization and Anti-Inflammatory Properties of Bothrops jararaca Snake Antithrombin, Protein & Peptide Letters 2015; 22 (5) . https://dx.doi.org/10.2174/0929866522666150216150704
DOI https://dx.doi.org/10.2174/0929866522666150216150704 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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