A heme-degradation pathway in a blood-sucking insect
| Autor: | Igor C. Almeida, Hatisaburo Masuda, Clarissa M. Maya-Monteiro, Pedro L. Oliveira, Gabriela O. Paiva-Silva, Boris C. Dunkov, Christine Cruz-Oliveira, Ernesto S. Nakayasu |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2006 |
| Předmět: |
Oxygenase
Spectrometry Mass Electrospray Ionization Porphyrins Time Factors Heme Catalysis chemistry.chemical_compound Hemoglobins Animals Rhodnius prolixus Chromatography High Pressure Liquid chemistry.chemical_classification Multidisciplinary Biliverdin biology Hydrolysis Biliverdine Biological Sciences biology.organism_classification Porphyrin Heme oxygenase Oxidative Stress Enzyme Biochemistry chemistry Models Chemical Rhodnius Heme Oxygenase (Decyclizing) Hemoglobin |
| Popis: | 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 IXα, in this insect, the end product of heme detoxification is a dicysteinyl-BV IXγ. 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. |
| Databáze: | OpenAIRE |
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