Characterization and immunological analysis of ferritin from the hemolymph of Galleria mellonella

Kim, Beom Su; Lee, Chang Seok; Yun, Chi Young; Yeo, Sung Moon; Park, Won Mock; Kim, Hak R.

doi:10.1016/s1095-6433(01)00287-2

Cited by 25 publications

(29 citation statements)

References 23 publications

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“…Our findings agree with those of others who have reported ferritin in the ovaries and eggs of insects Georgieva et al, 2002;Kurama et al, 1995;Kim et al, 2001;Bottke, 1982). However, to our knowledge, this is the first documentation that egg ferritin is loaded with iron, and further, with iron obtained in a meal.…”

Section: Discussionsupporting

confidence: 94%

Fate of blood meal iron in mosquitoes

Zhou

Kohlhepp

Geiser

et al. 2007

Journal of Insect Physiology

109

130

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Iron is an essential element of living cells and organisms as a component of numerous metabolic pathways. Hemoglobin and ferric-transferrin in vertebrate host blood are the two major iron sources for female mosquitoes. We used inductively coupled plasma mass spectrometry (ICP-MS) and radioisotope-labeling to quantify the fate of iron supplied from hemoglobin or as transferrin in Aedes aegypti. At the end of the first gonotrophic cycloe, ~87% of the ingested total meal heme iron was excreted, while 7% was distributed into the eggs and 6% was stored in different tissues. In contrast, 8% of the iron provided as transferrin was excreted and of that absorbed, 77% was allocated to the eggs and 15% distributed in the tissues. Further analyses indicate that of the iron supplied in a blood meal, ~7% appears in the eggs and of this iron 98% is from hemoglobin and 2% from ferrictransferrin. Whereas of iron from a blood meal retained in body of the female, ~97% is from heme and <1 % is from transferrin. Evaluation of iron-binding proteins in hemolymph and egg following intake of 59 Fe-transferrin revealed that ferritin is iron loaded in these animals, and indicate that this protein plays a critical role in meal iron transport and iron storage in eggs in A. aegypti.

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Section: Discussionsupporting

confidence: 94%

Fate of blood meal iron in mosquitoes

Zhou

Kohlhepp

Geiser

et al. 2007

Journal of Insect Physiology

109

130

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“…The 32 kDa of G. mellonella ferritin was confirmed to have an Nlinked glycosylation site within the deduced amino acid sequence (Asn-X-Thr/Ser), whereas the 26-kDa subunit did not have an N-linked glycosylation site. According to the concanavalin A stain, only the 32-kDa subunit was glycosylated while the 26-kDa subunit was not (Kim et al, 2001a). 2 for species name and accession numbers).…”

Section: Discussionmentioning

confidence: 99%

“…As described by Kim et al (2001a), ferritin was isolated by density gradient ultracentrifugation and FPLC gel filtration. Amino acid analysis was conducted at the Korea Basic Science Institute.…”

Section: N-terminal Sequence Analysismentioning

confidence: 99%

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Cloning and expression of 32 kDa ferritin from Galleria mellonella

Kim

Lee

Seol

et al. 2002

Arch Insect Biochem Physiol

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We have sequenced a cDNA clone encoding 32-kDa ferritin subunit in the Wax Moth, Galleria mellonella. The 32-kDa ferritin subunit cDNA was obtained from PCR using identical primer designed from highly conserved regions of insect ferritins. RACE PCR was used to obtain the complete protein coding sequence. The 32-kDa ferritin subunit encoded a 232 amino acid polypeptide, containing a 19 leader peptide. The iron-responsive element (IRE) sequence with a predicted stem-loop structure was present in the 5'-untranslated region of the wax moth 32-kDa ferritin subunit mRNA. The 32-kDa sequence alignment had 78 and 69% identity with Manduca sexta and Calpodes ethlius (G), respectively. The G. mellonella ferritin subunits showed minimal identity with each other (19%). The glycosylation site (Asn-X-Ser/Thr) was found in the 32-kDa subunit but not in the 26-kDa subunit. Northern blot analysis showed that the mRNA expression of the 32-kDa ferritin was detected in the fat body and midgut. The fat body expression increased after 6 h and the mRNA in midgut dramatically increased about 3-fold the expression level at 12 h after iron feeding. Western blot revealed that a protein level of the 32-kDa subunit is abundant in midgut after 12 and 24 h iron feeding.

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“…C. ethlius ferritin has a molecular mass of more than 600 kDa and is composed of two major subunits (24 and 31 kDa) and two minor subunits (26 and 28 kDa) (Nichol and Locke, 1989). G. mellonella ferritin was determined to have a molecular mass of 630 kDa, and consists of two major polypeptides of 26 and 32 kDa and one minor polypeptide of 30 kDa (Kim et al, 2001a(Kim et al, , 2002. Previously the N-terminal sequence of H. cunea ferritin HCH was determined as XPQXHINPV (Yun et al, 1998), which was in agreement with sequenced data.…”

Section: Purification Of Ferritin Hch In H Cuneamentioning

confidence: 99%

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

Kim

Yun

Cheon

et al. 2004

Arch Insect Biochem Physiol

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We have sequenced a cDNA clone encoding a 26-kDa ferritin subunit, which was heavy chain homologue (HCH), in fall webworm, Hyphantria cunea. The HCH cDNA was obtained from the screening of a cDNA library using a PCR product. H. cunea ferritin is composed of 221 amino acid residues and their calculated mass is 26,160 Da. The protein contains the conserved motifs for the ferroxidase center typical for heavy chains of vertebrate ferritin. The iron-responsive element sequence with a predicted stem-loop structure is present in the 5'-untranslated region of ferritin HCH mRNA. The sequence alignment of ferritin HCH shows 68.9 and 68.7% identity with Galleria mellonella HCH (26 kDa ferritin) and Manduca sexta HCH, respectively. While G type insect ferritin vertebrate light chain homologue (LCH) is distantly related to H. cunea ferritin HCH (17.2-20.8%), the Northern blot analysis revealed that H. cunea ferritin HCH was ubiquitously expressed in various tissues and all developmental stages. The ferritin expression of midgut is more responsive to iron-fed, compared to fat body in H. cunea.

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Characterization and immunological analysis of ferritin from the hemolymph of Galleria mellonella

Cited by 25 publications

References 23 publications

Fate of blood meal iron in mosquitoes

Fate of blood meal iron in mosquitoes

Cloning and expression of 32 kDa ferritin from Galleria mellonella

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

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