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A heme-degradation pathway in a blood-sucking insect.

Authors
  • Paiva-Silva, Gabriela O
  • Cruz-Oliveira, Christine
  • Nakayasu, Ernesto S
  • Maya-Monteiro, Clarissa M
  • Dunkov, Boris C
  • Masuda, Hatisaburo
  • Almeida, Igor C
  • Oliveira, Pedro L
Type
Published Article
Journal
Proceedings of the National Academy of Sciences of the United States of America
Publication Date
May 23, 2006
Volume
103
Issue
21
Pages
8030–8035
Identifiers
PMID: 16698925
Source
Medline
License
Unknown

Abstract

Hematophagous insects are vectors of diseases that affect hundreds of millions of people worldwide. A common physiological event in the life of these insects is the hydrolysis of host hemoglobin in the digestive tract, leading to a massive release of heme, a known prooxidant molecule. Diverse organisms, from bacteria to plants, express the enzyme heme oxygenase, which catalyzes the oxidative degradation of heme to biliverdin (BV) IX, CO, and iron. Here, we show that the kissing bug Rhodnius prolixus, a vector of Chagas' disease, has a unique heme-degradation pathway wherein heme is first modified by addition of two cysteinylglycine residues before cleavage of the porphyrin ring, followed by trimming of the dipeptides. Furthermore, in contrast to most known heme oxygenases, which generate BV IXalpha, in this insect, the end product of heme detoxification is a dicysteinyl-BV IXgamma. Based on these results, we propose a heme metabolizing pathway that includes the identified intermediates produced during modification and cleavage of the heme porphyrin ring.

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