title: Aedes aegypti ferritin.
abstract: Diseases transmitted by hematophagous (blood-feeding) insects are responsible for millions of human deaths worldwide. In hematophagous insects, the blood meal is important for regulating egg maturation. Although a high concentration of iron is toxic for most organisms, hematophagous insects seem unaffected by the iron load in a blood meal. One means by which hematophagous insects handle this iron load is, perhaps, by the expression of iron-binding proteins, specifically the iron storage protein ferritin. In vertebrates, ferritin is an oligomer composed of two types of subunits called heavy and light chains, and is part of the constitutive antioxidant response. Previously, we found that the insect midgut, a main site of iron load, is also a primary site of ferritin expression and that, in the yellow fever mosquito, Aedes aegypti, the expression of the ferritin heavy-chain homologue (HCH) is induced following blood feeding. We now show that the expression of the Aedes ferritin light-chain homologue (LCH) is also induced with blood-feeding, and that the genes of the LCH and HCH are tightly clustered. mRNA levels for both LCH- and HCH-genes increase with iron, H2O2 and hemin treatment, and the temporal expression of the genes is very similar. These results confirm that ferritin could serve as the cytotoxic protector in mosquitoes against the oxidative challenge of the bloodmeal. Finally, although the Aedes LCH has no iron responsive element (IRE) at its 5'-untranslated region (UTR), the 5'-UTR contains several introns that are alternatively spliced, and this alternative splicing event is different from any ferritin message seen to date.
authors.affiliation: College of Agriculture and Life Sciences, The University of Arizona, Tucson, AZ, USA.
authors.forename: Dawn L
authors.initials: DL
authors.lastname: Geiser
authors.forename: Carrie A
authors.initials: CA
authors.lastname: Chavez
authors.forename: Roberto
authors.initials: R
authors.lastname: Flores-Munguia
authors.forename: Joy J
authors.initials: JJ
authors.lastname: Winzerling
authors.forename: Daphne Q-D
authors.initials: DQ
authors.lastname: Pham
mesh_terms: D000330:Aedes / Q000235:genetics / Q000378:metabolism*; D017398:Alternative Splicing / Q000235:genetics; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002478:Cells, Cultured; D019610:Cytoprotection / Q000502:physiology*; D005293:Ferritins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D005786:Gene Expression Regulation / Q000187:drug effects; D006031:Glycosylation; D006427:Hemin / Q000494:pharmacology; D006861:Hydrogen Peroxide / Q000494:pharmacology; D007501:Iron / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000494:pharmacology / Q000633:toxicity; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D012333:RNA, Messenger / Q000096:biosynthesis / Q000235:genetics; D012045:Regulatory Sequences, Nucleic Acid; D024363:Transcription Initiation Site / Q000502:physiology
chemical_list: D012333:RNA, Messenger; D006427:Hemin; D005293:Ferritins; D006861:Hydrogen Peroxide; D007501:Iron