Aedes aegypti ferritin: A cytotoxic protector against iron and oxidative challenge?

Dawn L. Geiser, Carrie A. Chavez, Roberto Flores-Munguia, Joy Winzerling, Daphne Q D Pham

Research output: Contribution to journalArticle

46 Citations (Scopus)

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 heroin 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 blood-meal. 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.

Original languageEnglish (US)
Pages (from-to)3667-3674
Number of pages8
JournalEuropean Journal of Biochemistry
Volume270
Issue number18
DOIs
StatePublished - Sep 2003

Fingerprint

Aedes
Ferritins
Iron
Blood
Insects
Apoferritins
Meals
Light
Genes
5' Untranslated Regions
Culicidae
Iron-Binding Proteins
Yellow Fever
Poisons
Heroin
Alternative Splicing
Oligomers
Introns
Ovum
Vertebrates

Keywords

  • Aedes aegypti mosquito
  • Alternative splicing
  • Iron
  • Light-chain ferritin
  • Oxidative stress

ASJC Scopus subject areas

  • Biochemistry

Cite this

Aedes aegypti ferritin : A cytotoxic protector against iron and oxidative challenge? / Geiser, Dawn L.; Chavez, Carrie A.; Flores-Munguia, Roberto; Winzerling, Joy; Pham, Daphne Q D.

In: European Journal of Biochemistry, Vol. 270, No. 18, 09.2003, p. 3667-3674.

Research output: Contribution to journalArticle

Geiser, Dawn L. ; Chavez, Carrie A. ; Flores-Munguia, Roberto ; Winzerling, Joy ; Pham, Daphne Q D. / Aedes aegypti ferritin : A cytotoxic protector against iron and oxidative challenge?. In: European Journal of Biochemistry. 2003 ; Vol. 270, No. 18. pp. 3667-3674.
@article{612aa11a0f704d9a824461c7adf990be,
title = "Aedes aegypti ferritin: A cytotoxic protector against iron and oxidative challenge?",
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 heroin 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 blood-meal. 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.",
keywords = "Aedes aegypti mosquito, Alternative splicing, Iron, Light-chain ferritin, Oxidative stress",
author = "Geiser, {Dawn L.} and Chavez, {Carrie A.} and Roberto Flores-Munguia and Joy Winzerling and Pham, {Daphne Q D}",
year = "2003",
month = "9",
doi = "10.1046/j.1432-1033.2003.03709.x",
language = "English (US)",
volume = "270",
pages = "3667--3674",
journal = "FEBS Journal",
issn = "1742-464X",
publisher = "Wiley-Blackwell",
number = "18",

}

TY - JOUR

T1 - Aedes aegypti ferritin

T2 - A cytotoxic protector against iron and oxidative challenge?

AU - Geiser, Dawn L.

AU - Chavez, Carrie A.

AU - Flores-Munguia, Roberto

AU - Winzerling, Joy

AU - Pham, Daphne Q D

PY - 2003/9

Y1 - 2003/9

N2 - 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 heroin 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 blood-meal. 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.

AB - 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 heroin 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 blood-meal. 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.

KW - Aedes aegypti mosquito

KW - Alternative splicing

KW - Iron

KW - Light-chain ferritin

KW - Oxidative stress

UR - http://www.scopus.com/inward/record.url?scp=0141447418&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0141447418&partnerID=8YFLogxK

U2 - 10.1046/j.1432-1033.2003.03709.x

DO - 10.1046/j.1432-1033.2003.03709.x

M3 - Article

C2 - 12950250

AN - SCOPUS:0141447418

VL - 270

SP - 3667

EP - 3674

JO - FEBS Journal

JF - FEBS Journal

SN - 1742-464X

IS - 18

ER -