BmTI-A, a serine protease inhibitor, reduces the chronic allergic lung inflammation in a mice model

Florencio, Ariana Corrêa; Arantes-Costa, Fernanda M.; Almeida, Robson S. de; Brüggemann, Thayse Regina; Sasaki, Sergio D.; Martins, Mílton A.; Tibério, Iolanda F.L.C.; Lopes, Fernanda Degobbi Tenório Quirino dos Santos; Leick, Edna Aparecida

doi:10.1183/13993003.congress-2015.pa3952

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“…Previous studies suggest that serine protease inhibitor rBmTI-A has a protective potential against pulmonary emphysema in mice, attenuating the characteristic effects of disease onset and progression (Lourenço et al, 2018(Lourenço et al, , 2014 In addition, rBmTI-A is effective in attenuating the changes in lung mechanics, inflammation and remodeling of the airways in an animal model of chronic allergic pulmonary inflammation (Florencio et al, 2015). Soares et al (Soares et al, 2016) demonstrated a possible role of rBmTI-A inhibitor in controlling angiogenesis in human umbilical vein endothelial cell (HUVEC) line.…”

Section: Introductionmentioning

confidence: 99%

Structural modelling and thermostability of a serine protease inhibitor belonging to the Kunitz-BPTI family from the Rhipicephalus microplus tick

et al. 2021

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rBmTI-A is a recombinant serine protease inhibitor that belongs to the Kunitz-BPTI family and that was cloned from Rhipicephalus microplus tick. rBmTI-A has inhibitory activities on bovine trypsin, human plasma kallikrein, human neutrophil elastase and plasmin with dissociation constants in nM range. It is characterized by two inhibitory domains and each domain presents six cysteines that form three disulfide bonds, which contribute to the high stability of its structure. Previous studies suggest that serine protease inhibitor rBmTI-A has a protective potential against pulmonary emphysema in mice and anti-inflammatory potential, besides rBmTI-A presented a potent inhibitory activity against in vitro vessel formation. In this study, the tertiary structure of BmTI-A was modeled based on the structure of its Sabellastarte magnifica homologue. The structure stabilization was evaluated by molecular dynamics analysis. Circular dichroism data corroborated the secondary structure found by the homology modeling.Thermostability analysis confirmed the thermostability and the relation between the effects of the temperature in the inhibitor activity. The loss of activity observed was gradual, and, after 60 minutes of incubation at 90ºC the inhibitor lost it completely.

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Section: Introductionmentioning

confidence: 99%