Therefore, complimentary studies are necessary to improve the knowledge on the specific mechanisms by which the cardiovascular responses to TsTX are impaired in malnourished animals. In summary, protein

malnutrition attenuates the cardiovascular responses and increases the selleck chemicals survival time induced by central injection of TsTX, defying the concept that malnourishment would worsen severe scorpion envenomation chances of survival; possibly compromising TsTX pharmacodynamics and changing the excitability of encephalic nuclei involved in cardiovascular control. The authors are grateful to Cláudia Carneiro and to Immunopathology Laboratory (UFOP), for providing equipments; to Milton Alexandre de Paula and Jair Pator Mota, for technical assistance; and to CNPq, FAPEMIG, CAPES and UFOP, for the financial support. “
“In Brazil, snakes of the genus Bothrops

are responsible for more than 70% of all reported snake bites ( Bochner and Struchiner, 2003 and Saúde, 2010). There are approximately thirty species in this genus, phylogenetically Ibrutinib nmr distributed across seven groups named after the representative species Bothrops alternatus; Bothrops atrox; Bothrops jararaca; Bothrops jararacussu; B. microphthalmus; Bothrops neuwiedi; and

B. taeniatus. However, some researchers consider the groups B. microphtalmus and B. taeniatus to be members of the Bothrocophias and Bothriopsis genera, respectively ( Campbell and Lamar, 2004 and Gutberlet and Campbell, 2001). The species Bothrops moojeni belongs to the B. atrox group, together with the species Bothrops asper; Bothrops leucurus and Bothrops marajoensis ( Furtado et al., 2010). Various components have been isolated from Bothrops venom, including enzymes such as serine proteinases, Idelalisib clinical trial metalloproteinases, phospholipases A2 (PLA2), l-amino acid oxidases (LAAO), nucleotidases, and hyaluronidases; and proteins with other activities, such as disintegrins, members of the C-type lectin family, and others ( Braud et al., 2000, Chaves et al., 1995, Kini, 2006, Nunes et al., 2011, Sant’Ana et al., 2011 and Toyama et al., 2011). Serine proteinases contain a reactive serine residue at the active site, which is stabilized by the presence of histidine and aspartic acid residues (Serrano and Maroun, 2005).