Metabolic pathways inAnopheles stephensimitochondria
| Autor: | Shirley Luckhart, Ashley A Horton, Cecilia R Giulivi, Catherine Ross-Inta |
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| Rok vydání: | 2008 |
| Předmět: |
Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone
Bioenergetics Cellular respiration Cell Respiration Citric Acid Cycle Malates Antimycin A Glutamic Acid Oxidative phosphorylation Mitochondrion Biology Biochemistry Oxidative Phosphorylation Article Cell Line Oxygen Consumption Tandem Mass Spectrometry parasitic diseases Anopheles Pyruvic Acid Animals Amino Acids Molecular Biology Anopheles stephensi Cell Biology biology.organism_classification Insect Vectors Malaria Mitochondria Citric acid cycle Metabolic pathway Carbohydrate Metabolism Oligomycins Oxoglutarate dehydrogenase complex Oxidation-Reduction Metabolic Networks and Pathways Chromatography Liquid |
| Zdroj: | Biochemical Journal. 415:309-316 |
| ISSN: | 1470-8728 0264-6021 |
| Popis: | No studies have been performed on the mitochondria of malaria vector mosquitoes. This information would be valuable in understanding mosquito aging and detoxification of insecticides, two parameters that have a significant impact on malaria parasite transmission in endemic regions. In the present study, we report the analyses of respiration and oxidative phosphorylation in mitochondria of cultured cells [ASE (Anopheles stephensi Mos. 43) cell line] from A. stephensi, a major vector of malaria in India, South-East Asia and parts of the Middle East. ASE cell mitochondria share many features in common with mammalian muscle mitochondria, despite the fact that these cells are of larval origin. However, two major differences with mammalian mitochondria were apparent. One, the glycerol–phosphate shuttle plays as major a role in NADH oxidation in ASE cell mitochondria as it does in insect muscle mitochondria. In contrast, mammalian white muscle mitochondria depend primarily on lactate dehydrogenase, whereas red muscle mitochondria depend on the malate–oxaloacetate shuttle. Two, ASE mitochondria were able to oxidize proline at a rate comparable with that of α-glycerophosphate. However, the proline pathway appeared to differ from the currently accepted pathway, in that oxoglutarate could be catabolized completely by the tricarboxylic acid cycle or via transamination, depending on the ATP need. |
| Databáze: | OpenAIRE |
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