Manduca sexta hemolymph ferritin: cDNA sequence and mRNA expression

Pham, Daphne Q.-D.; Zhang, Dianzheng; Hufnagel, David H.; Winzerling, Joy J.

doi:10.1016/0378-1119(96)00012-1

Cited by 48 publications

(58 citation statements)

References 29 publications

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“…Unlike most animal ferritins which are cytosolic, including those of vertebrates (reviewed by Andrews et al, 1992) and the crayfish (Huang et al, 1996), and unlike plant ferritins which are targeted to plastids by N-terminal transit peptides (Ragland et al, 1990), insect femtins (Dunkov et al, 1995;Pham et al, 1996) have acquired a novel role and are secreted into the hemolymph. The sequence indicates that this is also true for the D. rnelanogaster ferritin subunit, which is synthesized with a signal peptide (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…This mode of regulation has so far been explored extensively only in vertebrates, but has also been demonstrated experimentally in the mRNA encoding a subunit of Drosophila succinic dehydrogenase (Kohler et al, 1995;Gray et al, 1996;Melefors, 1996). Sequences that closely resemble IRES have been found in ferritin messages from two insects, Aedes aegypti (Dunkov et (Pham et al, 1996), and a crustacean (Huang et al, 1996). The investigation reported here shows that D. melanogaster ferritin message also contains an IRE-like element, and thus it seems likely that the regulation of the synthesis of proteins important for the uptake, storage, and utilization of iron in cells of this organism is similar to that shown to operate in vertebrate cells.…”

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confidence: 98%

“…Some of the insect ferritin subunits are also glycosylated. The sequences of ferritin subunits deduced from DNA from two separate insect species (Dunkov et al, 1995;Pham et al, 1996) contain signal sequences, clearly showing that the molecules are designed for export from the cell. These properties suggest that insect ferritins may serve purposes different from those of their Correspondence 60 John H. Law, Department of Biochemistry, UniFax: + I 520 621 3243.…”

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confidence: 99%

“…The cloning and deduced sequence of single subunits from two insect species, a mosquito and a moth, have been reported (Dunkov et al, 1995;Pham et al, 1996). To apply genetic methods to the problems of ferritin function, it seemed desirable to isolate ferritin from Drosophila melanogaster and to identify the gene or genes for this protein.…”

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confidence: 99%

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Isolation and Properties of Drosophila Melanogaster Ferritin — Molecular Cloning of a cDNA that Encodes One Subunit, and Localization of the Gene on the Third Chromosome

Charlesworth

Georgieva

Gospodov

et al. 1997

European Journal of Biochemistry

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Ferritin was purified from iron-fed Drosophila melanogaster extracts by centrifugation in a gradient of potassium bromide. On polyacrylamide gel electrophoresis, the product showed two protein bands corresponding to the ferritin monomer and dimer. Electrophoresis following dissociation with SDS and 2-mercaptoethanol revealed three strong bands of approximately 25, 26, and 28 kDa. N-terminal amino acid sequences were identical for the 25-kDa and 26-kDa subunits, but different for the 28-kDa subunit. Conserved ferritin PCR primers were used to amplify a 360-bp cDNA product, which was used to isolate a clone from a D. melanogaster cDNA library that contained the complete coding sequence for a ferritin subunit. Additional 5' sequence obtained by the RACE method revealed the presence of a putative iron regulatory element. The PCR product was also used to locate the position of the ferritin subunit gene at region 99F on the right arm of the third chromosome. The deduced amino acid sequence of the D.melanogaster ferritin subunit contained a signal sequence and resembled most closely ferritin of the mosquito Aedes aegypti. The evolution of ferritin sequences is discussed.

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Section: Resultsmentioning

confidence: 99%

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confidence: 98%

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confidence: 99%

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Isolation and Properties of Drosophila Melanogaster Ferritin — Molecular Cloning of a cDNA that Encodes One Subunit, and Localization of the Gene on the Third Chromosome

Charlesworth

Georgieva

Gospodov

et al. 1997

European Journal of Biochemistry

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“…aegypti (AaFerLCH), 40.5 % M. sexta (MsFerLCH), and 39.6% C. ethlius (CeFerG). In M. sexta (Asp135) (Pham et al, 1996) and C. ethlius (Asp133) (Nichol and Locke, 1999) LCH homologues have a functional glycosylation site ( Figure 2B). With the exception of the unusual placement of an Nglycosylation site at the beginning of the Ae.…”

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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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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Manduca sexta hemolymph ferritin: cDNA sequence and mRNA expression

Cited by 48 publications

References 29 publications

Isolation and Properties of Drosophila Melanogaster Ferritin — Molecular Cloning of a cDNA that Encodes One Subunit, and Localization of the Gene on the Third Chromosome

Isolation and Properties of Drosophila Melanogaster Ferritin — Molecular Cloning of a cDNA that Encodes One Subunit, and Localization of the Gene on the Third Chromosome

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

Cloning and expression of 32 kDa ferritin from Galleria mellonella

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