TAILIEUCHUNG - Báo cáo khoa học: Oxygen-induced changes in hemoglobin expression in Drosophila

The amyloidbpeptide (Ab) with 39–42 residues is the major component of amyloid plaques found in brains of Alzheimer’s disease patients, and solu-ble oligomeric peptide aggregates mediate toxic effects on neurons. The Ab aggregation involves a conformational change of the peptide structure to b-sheet. | ễFEBS Journal Oxygen-induced changes in hemoglobin expression in Drosophila Eva Gleixner1 Daniela Abriss1 Boris Adryan2 Melanie Kraemer1 Frank Gerlach1 3 Reinhard Schuh2 Thorsten Burmester3 and Thomas Hankeln1 1 Institute of Molecular Genetics University of Mainz Germany 2 Max-Planck-Institute for BiophysicalChemistry Department of Molecular DevelopmentalBiology Gottingen Germany 3 Biocenter Grindeland ZoologicalMuseum University of Hamburg Germany Keywords globin hyperoxia hypoxia respiration tracheae Correspondence T. Hankeln Institute of Molecular Genetics University of Mainz J. J. Becherweg 30a D-55099 Mainz Germany Fax 49 6131 392 4585 Tel 49 6131 392 3277 E-mail hankeln@ Received 4 July 2008 revised 7 August 2008 accepted 12 August 2008 doi The hemoglobin gene 1 dmeglob of the fruit fly Drosophila melanogaster is expressed in the tracheal system and fat body and has been implicated in hypoxia resistance. Here we investigate the expression levels of dmeglobl and lactate dehydrogenase a positive control in embryos third instar larvae and adult flies under various regimes of hypoxia and hyperoxia. As expected mRNA levels of lactate dehydrogenase increased under hypoxia. We show that expression levels of dmeglobl are decreased under both short- and long-term hypoxia compared with the normoxic 21 O2 control. By contrast a hypoxia reoxygenation regime applied to third instar larvae elevated the level of dmeglobl mRNA. An excess of O2 hyperoxia also triggered an increase in dmeglobl mRNA. The data suggest that Drosophila hemoglobin may be unlikely to function merely as a myoglobinlike O2 storage protein. Rather dmeglobl may protect the fly from an excess of O2 either by buffering the flux of O2 from the tracheoles to the cells or by degrading noxious reactive oxygen species. The exchange of respiratory gases in insects is enabled by the tracheal system which mediates diffusive gas transport to the inner organs 1 2 . In .

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