Autor |
Araujo, APU
![]() Hansen, D. ![]() Vieira, D. F. ![]() Oliveira, C. de ![]() Santana, L. A. ![]() Beltramini, L. M. ![]() Sampaio, CAM ![]() Sampaio, M. U. ![]() Oliva, MLV ![]() |
Instituição | Universidade Federal de São Paulo (UNIFESP) Universidade de São Paulo (USP) |
Resumo | Bauhinia bauhinoides cruzipain inhibitor (BbCl) and Bauhinia bauhinioides kallikrein inhibitor (BbKl) are cysteine and serine proteinase inhibitors structurally homologous to plant Kunitz-type inhibitors, but are devoid of disulfide bridges. Based on cDNA sequences, we found that BbKI and BbCI are initially synthesized as a prepropepticle comprising an N-terminal signal peptide (19 residues), the mature protein (164 residues) and a C-terminal targeting peptide (10 residues). Partial cDNAs encoding the mature enzymes plus N-terminal His-tags and thrombin cleavage sites were expressed in E coli and the soluble proteins were purified by one-step nickel affinity chromatography. After thrombin cleavage, both proteins exhibited potent inhibitory activities toward their cognate proteinases like the wild-type proteins. BbCl inhibits human neutrophil elastase (K-i(app) 5.3 nM), porcine pancreatic elastase (K-i(app) 40 nM), cathepsin G (K-i(app) 160 nM) and the cysteine proteinases cruzipain (K-i(app) 1.2 nM), cruzain (K-i(app) 0.3 nM) and cathepsin L (K-i(app) 2.2 nM), while BbKl strongly inhibits plasma kallikrein (K-i(app) 2.4 nM) and plasmin (K-i(app) 33 nM). Circular dichroism spectra of BbCl and BbKl were in agreement with the P-trefoil fold described for Kunitz inhibitors. the inhibitory potency of both BbCl- and BbKl-type inhibitors suggests that other, non-covalent interactions may compensate for the lack of disulficle bridges. |
Assunto |
cathepsins
cruzipain elastase gene kallikreins proteinase inhibitors |
Idioma | Inglês |
Data | 2005-06-01 |
Publicado em | Biological Chemistry. Berlin: Walter de Gruyter & Co, v. 386, n. 6, p. 561-568, 2005. |
ISSN | 1431-6730 (Sherpa/Romeo, fator de impacto) |
Editor | Walter de Gruyter & Co |
Extensão | 561-568 |
Fonte |
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Direito de acesso | Acesso restrito |
Tipo | Artigo |
Web of Science | WOS:000230256800007 |
URI | http://repositorio.unifesp.br/handle/11600/28340 |
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