Author | Waniek, Peter J. | |
Author | Costa, Juliana E. Pacheco | |
Author | Jansen, Ana M. | |
Author | Costa, Jane | |
Author | Araújo, Catarina A. C. | |
Access date | 2016-09-01T17:02:35Z | |
Available date | 2016-09-01T17:02:35Z | |
Document date | 2012 | |
Citation | WANIEK, Peter J. et al. Cathepsin L of Triatoma brasiliensis (Reduviidae, Triatominae): Sequence characterization, expression pattern and zymography. . Journal of Insect Physiology, v.58, p.178–187, 2012. | pt_BR |
ISSN | 0022-1910 | pt_BR |
URI | https://www.arca.fiocruz.br/handle/icict/15579 | |
Language | eng | pt_BR |
Publisher | Elsevier | pt_BR |
Rights | restricted access | |
Subject in Portuguese | Trypanosoma cruzi | pt_BR |
Subject in Portuguese | Enzimas digestivas | pt_BR |
Subject in Portuguese | Triatoma brasiliensis | pt_BR |
Subject in Portuguese | Cisteína Proteases | pt_BR |
Subject in Portuguese | Catepsina L. | pt_BR |
Title | Cathepsin L of Triatoma brasiliensis (Reduviidae, Triatominae): sequence characterization, expression pattern and zymography | pt_BR |
Type | Article | |
DOI | 10.1016/j.jinsphys.2011.11.008 | |
Abstract | Triatoma brasiliensis is considered one of the main vectors of Chagas disease commonly found in semi-arid areas of northeastern Brazil. These insects use proteases, such as carboxypeptidase B, aminopeptidases and different cathepsins for blood digestion. In the present study, two genes encoding cathepsin L from the midgut of T. brasiliensis were identified and characterized. Mature T. brasiliensis cathepsin L-like proteinases (TBCATL-1, TBCATL-2) showed a high level of identity to the cathepsin L-like proteinases of other insects, with highest similarity to Rhodnius prolixus. Both cathepsin L transcripts were highly abundant in the posterior midgut region, the main region of the blood digestion. Determination of the pH in the whole intestine of unfed T. brasiliensis revealed alkaline conditions in the anterior midgut region (stomach) and acidic conditions in the posterior midgut region (small intestine). Gelatine in-gel zymography showed the activity of at least four distinct proteinases in the small intestine and the cysteine proteinase inhibitors transepoxysuccinyl-l-leucylamido-(4-guanidino)butane (E-64) and cathepsin B inhibitor and N-(l-3-trans-propylcarbamoyl-oxirane-2-carbonyl)-l-isoleucyl-l-proline (CA-074) were employed to characterize enzymatic activity. E-64 fully inhibited cysteine proteinase activity, whereas in the samples treated with CA-074 residual proteinase activity was detectable. Thus, proteolytic activity could at least partially be ascribed to cathepsin L. Western blot analysis using specific anti cathepsin L antibodies confirmed the presence of cathepsin L in the lumen of the small intestine of the insects. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Biologia de Tripanosomatídeos. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Biologia de Tripanosomatídeos. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Biodiversidade Entomológica. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Biologia de Tripanosomatídeos. Rio de Janeiro, RJ, Brasil / Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Biodiversidade Entomológica. Rio de Janeiro, RJ, Brasil.. | pt_BR |
Subject | Digestive enzymes | pt_BR |
Subject | Cysteine proteinases | pt_BR |
Subject | Cathepsin L. | pt_BR |
Subject | Triatoma brasiliensis | pt_BR |
Subject | Insect midgut | pt_BR |
Subject | Trypanosoma cruzi | pt_BR |
Embargo date | 2030-01-01 | |