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Doctoral Thesis
DOI
10.11606/T.87.2013.tde-06062013-154512
Document
Author
Full name
Karen de Morais Zani
Institute/School/College
Knowledge Area
Date of Defense
Published
São Paulo, 2013
Supervisor
Committee
Azevedo, Anita Mitico Tanaka (President)
Cheng, Elisabeth
Grego, Kathleen Fernandes
Lazari, Maria de Fatima Magalhães
Tanizaki, Martha Massako
Title in Portuguese
Estudo da atividade anti-inflamatória da antitrombina nativa da serpente Bothrops jararaca. Clonagem da antitrombina.
Keywords in Portuguese
Antiinflamatórios
Antitrombina
Camundongos
Clonagem
Serpentes
Abstract in Portuguese
A antitrombina de B. jararaca foi isolada por meio de cromatografia de afinidade em coluna HiTrap Heparin HP (GE Healthcare). A análise da interação da antitrombina humana ou de B. jararaca com a heparina em sistema BIAcoreT200 demonstrou que a antitrombina de B. jararaca apresenta maior afinidade pela heparina que a antitrombina humana. Com relação à sua atividade anti-inflamatória, os resultados obtidos evidenciaram o efeito anti-inflamatório do pré e do pós-tratamento com a antitrombina de B. jararaca na resposta inflamatória aguda. A análise proteômica do exsudato inflamatório de camundongos identificou algumas proteínas possivelmente relacionadas ao mecanismo de inibição da antitrombina, como a enzima C3 do sistema complemento, a sorotransferrina, a a1-antitripsina, a apolipoproteína AI, o fibrinogênio, o cininogênio e a albumina. O processo de clonagem permitiu a obtenção da sequência completa da antitrombina de B. jararaca e apesar da longa distância evolutiva entre serpentes e humanos, diversas características da antitrombina encontram-se conservadas.
Title in English
Study of anti-inflammatory activity of Bothrops jararaca native antithrombin. Antithrombin cloning.
Keywords in English
Antiinflammatory
Antithrombin
Cloning
Mice
Snakes
Abstract in English
B. jararaca antithrombin was isolated by affinity chromatography using HiTrap Heparin HP column (GE Healthcare). The interaction analysis of human or B. jararaca antithrombin with heparin using a BIAcoreT200 system (GE Healthcare) demonstrated that the affinity of B. jararaca antithrombin for heparin is higher than human antithrombin. Regarding the anti-inflammatory activity of B. jararaca antithrombin, the results showed the anti-inflammatory effect of pre- and post-treatment with this molecule in acute inflammation. The proteomic analysis of inflammatory exudate of mice identified some proteins possibly related to the mechanism of inhibition of antithrombin, such as C3 complement, serum transferrin, a1-antitrypsin, apolipoprotein AI, fibrinogen, albumin and kininogen. The molecular cloning process allowed the determination of the complete sequence of B. jararaca antithrombin and despite the evolutionary distance between snakes and human, a number of characteristics are preserved in antithrombin molecule.
 
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Publishing Date
2013-06-13
 
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