<i>Hyphantria cunea</i> ferritin heavy chain homologue: cDNA sequence and mRNA expression

Kim, Hong Ja; Yun, Chi Young; Cheon, Hyang-Mi; Chae, Boa; Lee, In Hee; Park, Seun Ja; Kang, Young Jin; Seo, Sook Jae

doi:10.1002/arch.10141

Cited by 7 publications

(5 citation statements)

References 49 publications

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“…3B). Current data suggest that all insect tissues make ferritin as all tissues examined show expression of both the LCH and HCH messages (Table 2), though at different expression levels [15, 17, 19, 21-25, 33, 60, 62, 66, 67]. However, as stated earlier, where or how insect ferritin is iron loaded or unloaded remains unknown.…”

Section: Functions Of Insect Ferritinsmentioning

confidence: 76%

Insect ferritins: Typical or atypical?

Pham¹,

Winzerling²

2010

Biochimica et Biophysica Acta (BBA) - General Subjects

105

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Insects transmit millions of cases of disease each year, and cost millions of dollars in agricultural losses. The control of insect-borne diseases is vital for numerous developing countries, and the management of agricultural insect pests is a very serious business for developed countries. Control methods should target insect-specific traits in order to avoid non-target effects, especially in mammals. Since insect cells have had a billion years of evolutionary divergence from those of vertebrates, they differ in many ways that might be promising for the insect control field—especially, in iron metabolism because current studies have indicated that significant differences exist between insect and mammalian systems. Insect iron metabolism differs from that of vertebrates in the following respects. Insect ferritins have a heavier mass than mammalian ferritins. Unlike their mammalian counterparts, the insect ferritin subunits are often glycosylated and are synthesized with a signal peptide. The crystal structure of insect ferritin also shows a tetrahedral symmetry consisting of 12 heavy chain and 12 light chain subunits in contrast to that of mammalian ferritin that exhibits an octahedral symmetry made of 24 heavy chain and 24 light chain subunits. Insect ferritins associate primarily with the vacuolar system and serve as iron transporters—quite the opposite of the mammalian ferritins, which are mainly cytoplasmic and serve as iron storage proteins. This review will discuss these differences.

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Section: Functions Of Insect Ferritinsmentioning

confidence: 76%

Insect ferritins: Typical or atypical?

Pham¹,

Winzerling²

2010

Biochimica et Biophysica Acta (BBA) - General Subjects

105

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“…Conversely, only one canonical polyadenylation signal was identified in GmmFer1HCH, though several non-canonical sites were identified ( Figure 3A), one of which is similar to a non-canonical site in Ae. aegypti and the rest of which are similar to non-canonical sites identified in H. cunea (Kim et al, 2004a). The use of these dual polyadenylation signals in GmmFer2LCH and of the non-canonical sites in GmmFer1HCH for the production of messages of different lengths has not yet been confirmed.…”

Section: Characterization Of G M Morsitans Gmmfer2lch and Gmmfer1hcmentioning

confidence: 93%

“…aegypti mature LCH peptide (Asp22/23) (Geiser et al, 2003), known dipteran LCH homologues lack glycosylation, including G. m. morsitans (Lind et al, 1998a). Previously published alignments of insect LCHs, including that of D. melanogaster, maintain conservation of three Cys residues (Kim et al, 2004b, Kim et al, 2004a. In our alignment, GmmFer2LCH maintains the three conserved Cys residues in the N-terminus in alignment with D. melanogaster; however, in our alignment, the D. melanogaster sequence does not align with the conserved Cys residues of other insect sequences as was described previously (Kim et al, 2004b).…”

Section: Characterization Of G M Morsitans Gmmfer2lch and Gmmfer1hcmentioning

confidence: 99%

Molecular characterization of iron binding proteins from Glossina morsitans morsitans (Diptera: Glossinidae)

Strickler-Dinglasan

Güz

Attardo

et al. 2006

Insect Biochemistry and Molecular Biology

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The regulation of iron is critical for maintaining homeostasis in the tsetse fly (Diptera:Glossinidae), in which both adult sexes are strict blood feeders. We have characterized the cDNAs for two putative iron-binding proteins (IBP) involved in transport and storage; transferrin (GmmTsf1) and ferritin from Glossina morsitans morsitans. GmmTsf1 transcripts are detected in the female fat body and in adult reproductive tissues, and only in the adult developmental stage in a bloodmeal independent manner. In contrast, the ferritin heavy chain (GmmFer1HCH) and light chain (GmmFer2LCH) transcripts are expressed ubiquitously, suggesting a more general role for these proteins in iron transport and storage. Protein domain predictions for each IBP suggest both the conservation and loss of several motifs present in their vertebrate homologues. In concert with many other described insect transferrins, putative secreted GmmTsf1 maintains 3 of the 5 residues necessary for ironbinding in the N-terminal lobe, but exhibits a loss of this iron-binding ability in the C-terminal role as well as a loss of large sequence blocks. Both putative GmmFer1HCH and GmmFer2LCH proteins have signal peptides, similar to other insect ferritins. GmmFer2LCH has lost the 5'UTR ironresponsive element (IRE) and, thus, translation is no longer regulated by cellular iron levels. On the other hand, GmmFer1HCH maintains both the conserved ferroxidase center and the 5'UTR IRE; however, transcript variants suggest a more extensive regulatory mechanism for this subunit.

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“…2000), Galleria mellonella (Kim et al . 2001a & 2001b, 2002), Hyphantria cunea (Kim et al . 2004a), Apriona germari (Kim et al .…”

Section: Introductionmentioning

confidence: 99%

Upregulation of hemolymph and tissue ferritin by dietary HgCl₂ in the wax moth Galleria mellonella

Choi

Seo

Yuk

et al. 2006

Entomological Research

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The effect of Hg treatment on hemolymph and tissue ferritin in the wax moth Galleria mellonella was examined by western blotting. At 48 h after feeding HgCl2, the level of hemolymph ferritin increased approximately 1.8‐fold over that of control insects that were not fed HgCl2, while there was a small increase in tissue ferritin. Time series experiments showed that tissue ferritin had a typically saturated pattern, with a maximum level from 24 to 72 h, although it decreased 12 h following HgCl2 feeding, while hemolymph ferritin first decreased but subsequently increased. Tissue ferritin in the fat body, gut and Malpighian tubules, the main tissues of ferritin expression, was upregulated over time following treatment with Hg, and in particular, tissue ferritin in the gut increased by a large amount at 12–48 h. The results suggest that in G. mellonella, the ferritin‐inducible mechanisms following treatment with HgCl2 are different for hemolymph and tissue ferritin, as are their biochemical properties.

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Hyphantria cunea ferritin heavy chain homologue: cDNA sequence and mRNA expression

Cited by 7 publications

References 49 publications

Insect ferritins: Typical or atypical?

Insect ferritins: Typical or atypical?

Molecular characterization of iron binding proteins from Glossina morsitans morsitans (Diptera: Glossinidae)

Upregulation of hemolymph and tissue ferritin by dietary HgCl₂ in the wax moth Galleria mellonella

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Hyphantria cunea ferritin heavy chain homologue: cDNA sequence and mRNA expression

Cited by 7 publications

References 49 publications

Insect ferritins: Typical or atypical?

Insect ferritins: Typical or atypical?

Molecular characterization of iron binding proteins from Glossina morsitans morsitans (Diptera: Glossinidae)

Upregulation of hemolymph and tissue ferritin by dietary HgCl2 in the wax moth Galleria mellonella

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Upregulation of hemolymph and tissue ferritin by dietary HgCl₂ in the wax moth Galleria mellonella