The characterization of ferritin in an insect

Nichol, Helen; Locke, Michael

doi:10.1016/0020-1790(89)90024-3

Cited by 53 publications

(44 citation statements)

References 45 publications

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“…An additional band, presumably representing a minor subunit, could be seen on heavily loaded gels as a very weakly stained band between those representing the 25-kDa and 26-kDa subunits. Thus, D. rnelanogaster ferritin resembles those reported for several other insects in terms of the larger size of the intact protein and of its subunits, relative to vertebrate ferritins (Nichol and Locke, 1989;Winzerling et al, 1995;Dunkov et al, 1995;Capurro et al, 1996).…”

Section: Resultssupporting

confidence: 59%

“…In many insect species, ferritin occurs abundantly in the extracellular hemolymph, and when it does occur in cells it lies primarily in the vacuolar export channels (Locke and Nichol, 1992). Furthermore, the subunits that make up insect ferritin are of larger size than those of the mammalian counterpart, resulting in a parent molecule of considerably larger size (Nichol and Locke, 1989;Winzerling et al, 1995). Some of the insect ferritin subunits are also glycosylated.…”

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confidence: 99%

“…So far, ferritin proteins have been isolated and characterized from a few insect species (Huebers et al, 1988;Nichol and Locke, 1989;Dunkov et al, 1995;Winzerling et al, 1995;Capurr0 et al, 1996). 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).…”

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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: Resultssupporting

confidence: 59%

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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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“…Homoptera store holoferritin in the cytosol in response to the iron overload from feeding on plant sap (13,66) or nectar (39,67), but in most insects ferritin is largely vacuolar (59,69). Most fat body contains apoferritin in the RER (55,61), as in C. ethlius where it becomes holoferritin only after secretion into the hemolymph (68).…”

Section: Ferritin Distribution In Rer and Sermentioning

confidence: 99%

Surface Membranes, Golgi Complexes, and Vacuolar Systems

Locke

2003

Annu. Rev. Entomol.

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In the absence of fossils, the cells of vertebrates are often described in lieu of a general animal eukaryote model, neglecting work on insects. However, a common ancestor is nearly a billion years in the past, making some vertebrate generalizations inappropriate for insects. For example, insect cells are adept at the cell remodeling needed for molting and metamorphosis, they have plasma membrane reticular systems and vacuolar ferritin, and their Golgi complexes continue to work during mitosis. This review stresses the ways that insect cells differ from those of vertebrates, summarizing the structure of surfacce membranes and vacuolar systems, especially of the epidermis and fat body, as a prerequisite for the molecular studies needed to understand cell function. The objective is to provide a structural base from which molecular biology can emerge from biochemical description into a useful analysis of function.

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“…In insects, ferritin has been investigated mainly by cytological methods (Locke and Nichol, 1992) and it has been isolated and characterized from the moths, Calpodes ethlius (Nichol and Locke, 1989) and Manduca sexta (Huebers et al, 1988;Winzerling et al, 1995), and from the homopteran, Philaenus spumavius (Collin et al, 1988).…”

Section: Introductionmentioning

confidence: 99%