An unexpected inhibitory activity of Kunitz-type serine proteinase inhibitor derived from Boophilus microplus trypsin inhibitor on cathepsin L

An unexpected inhibitory activity of Kunitz-type serine proteinase inhibitor derived from Boophilus microplus trypsin inhibitor on cathepsin L

Autor Sasaki, S. D. Google Scholar
Cotrin, S. S. Google Scholar
Carmona, A. K. Google Scholar
Tanaka, A. S. Google Scholar
Instituição Universidade Federal de São Paulo (UNIFESP)
Resumo Several BPTI-Kunitz-type serine proteinase inhibitors were described in tick Boophilus microplus and Rhipicephalus sanguineus species. in this work, we present a synthetic gene based on two tick BPTI-Kunitz-type serine proteinase inhibitors, the first domain of B. micro-plus trypsin inhibitor-A (BmTI-A) and the carrapatin, the inhibitors were named BmTIsint and BmTIsint Mut. Our present results showed that BmTIsint and BmTIsint Mut inhibited trypsin (K-i 3.3 and 1.0 nM) and human plasma kallikrein (K-i 16.5 and 35 nM), but in contrast to BmTI-A, the inhibitors did not inhibit human neutrophil elastase. BmTIsint was able to produce immunological response in mice but not in bovines. in addition, it is the first description of a BPTI-Kunitz-type inhibitor as a cysteine proteinase inhibitor, BmTIsint apparent dissociation constant (Ki) for cathepsin L was 108 nM. Our findings open the possibility up to obtain new molecules as potent serine or cysteine proteinase inhibitors using BmTIsint as a model. (c) 2006 Elsevier Inc. All rights reserved.
Palavra-chave cysteine proteinase inhibitor
serine proteinase inhibitor
tick
ectoparasite
Boophilus microplus
Idioma Inglês
Data de publicação 2006-03-03
Publicado em Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc Elsevier Science, v. 341, n. 1, p. 266-272, 2006.
ISSN 0006-291X (Sherpa/Romeo, fator de impacto)
Publicador Elsevier B.V.
Extensão 266-272
Fonte http://dx.doi.org/10.1016/j.bbrc.2005.12.178
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000235313400039
Endereço permanente http://repositorio.unifesp.br/handle/11600/28790

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