Cloning, Characterization and Anti-Inflammatory Properties of Bothrops jararaca Snake Antithrombin

Cloning, Characterization and Anti-Inflammatory Properties of Bothrops jararaca Snake Antithrombin

Author Morais-Zani, Karen de Google Scholar
Grego, Kathleen Fernandes Google Scholar
Torquato, Ricardo José Soares Autor UNIFESP Google Scholar
Silva, Caroline Serino Google Scholar
Tanaka, Aparecida Sadae Autor UNIFESP Google Scholar
Tanaka-Azevedo, Anita Mitico Google Scholar
Institution Inst Butantan
Universidade de São Paulo (USP)
Universidade Federal de São Paulo (UNIFESP)
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 similar to 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
heparin affinity
surface plasmon resonance
Language English
Sponsor Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
Grant number FAPESP: 2009/03484-3
FAPESP: 2009/50199-2
FAPESP: 2009/53844-6
FAPESP: 2011/21558-4
Date 2015-01-01
Published in Protein And Peptide Letters. Sharjah: Bentham Science Publ Ltd, v. 22, n. 5, p. 410-418, 2015.
ISSN 0929-8665 (Sherpa/Romeo, impact factor)
Publisher Bentham Science Publ Ltd
Extent 410-418
Access rights Closed access
Type Article
Web of Science ID WOS:000354338300004

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