Author | Caiaffa, C. D. | |
Author | Stiebler, R. | |
Author | Oliveira, M. F. | |
Author | Lara, F. A. | |
Author | Silva, G. O. Paiva | |
Author | Oliveira, P. L. | |
Access date | 2018-04-26T13:13:40Z | |
Available date | 2018-04-26T13:13:40Z | |
Document date | 2010 | |
Citation | CAIAFFA, C. D. et al. Sn-protoporphyrin inhibits both heme degradation and hemozoin formation in Rhodnius prolixus midgut. Insect Biochemistry and Molecular Biology, v.40, p.855-860, 2010. | pt_BR |
ISSN | 0965-1748 | pt_BR |
URI | https://www.arca.fiocruz.br/handle/icict/26127 | |
Language | eng | pt_BR |
Publisher | Elsevier | pt_BR |
Rights | restricted access | |
Subject in Portuguese | Heme | pt_BR |
Subject in Portuguese | Estresse Oxidativo | pt_BR |
Subject in Portuguese | Rhodnius prolixus | pt_BR |
Subject in Portuguese | Heme oxygenase | pt_BR |
Subject in Portuguese | Hematofagia | pt_BR |
Title | Sn-protoporphyrin inhibits both heme degradation and hemozoin formation in Rhodnius prolixus midgut | pt_BR |
Type | Article | |
DOI | 10.1016/j.ibmb.2010.08.005 | |
Abstract | Hematophagy is a feeding habit that involves the ingestion of huge amounts of heme. The hematophagous hemipteran Rhodnius prolixus evolved many genetic resources to protect cells against heme toxicity. The primary barrier against the deleterious effects of heme is the aggregation of heme into hemozoin in the midgut lumen. Hemozoin formation is followed by the enzymatic degradation of heme by means of a unique pathway whose end product is dicysteinyl-biliverdin IX-γ (Rhodnius prolixus biliverdin, RpBv). These mechanisms are complemented by a heme-binding protein (RHBP) in the hemolymph that attenuates the pro-oxidant effects of heme. In this work, we show that when insects are fed with blood enriched with a heme analog, Sn-protoporphyrin (SnPP-IX), both hemozoin synthesis and RpBv production are inhibited in a dose-dependent manner. These effects are accompanied by increased oxidative damage to the midgut epithelium and inhibition of oviposition, indicating that hemozoin formation and heme degradation are protective mechanisms that work together and contributed to the adaptation of this insect to successfully feed on vertebrate blood. | pt_BR |
Affilliation | Universidade Federal do Rio de Janeiro. Instituto de Bioquímica Médica Leopoldo de Meis. Programa de Biologia Molecular e Biotecnologia. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Universidade Federal do Rio de Janeiro. Instituto de Bioquímica Médica Leopoldo de Meis. Programa de Biologia Molecular e Biotecnologia. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Universidade Federal do Rio de Janeiro. Instituto de Bioquímica Médica Leopoldo de Meis. Programa de Biologia Molecular e Biotecnologia. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Microbiologia Celular. Rio de Janeiro, RJ. Brasil. | pt_BR |
Affilliation | Universidade Federal do Rio de Janeiro. Instituto de Bioquímica Médica Leopoldo de Meis. Programa de Biologia Molecular e Biotecnologia. Rio de Janeiro, RJ, Brasil / Instituto Nacional de Ciência e Tecnologia em Entomologia Molecular. Brasil. | pt_BR |
Affilliation | Universidade Federal do Rio de Janeiro. Instituto de Bioquímica Médica Leopoldo de Meis. Programa de Biologia Molecular e Biotecnologia. Rio de Janeiro, RJ, Brasil / Instituto Nacional de Ciência e Tecnologia em Entomologia Molecular. Brasil | pt_BR |
Subject | Heme | pt_BR |
Subject | Heme oxygenase | pt_BR |
Subject | Hematophagy | pt_BR |
Subject | Rhodnius prolixus | pt_BR |
Subject | Oxidative stress | pt_BR |
DeCS | Heme Oxigenase (Desciclizante) | pt_BR |
e-ISSN | 1879-0240 | |
Embargo date | 2030-01-01 | |