Title:Cloning, Characterization and Anti-Inflammatory Properties of <i>Bothrops jararaca</i> 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:Instituto Butantan, Laboratorio de Herpetologia, Avenida Vital Brazil, 1500, 05503-900, Sao Paulo, Brasil.
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.
