Purification of chicken liver ferritin by two novel methods and structural comparison with horse spleen ferritin

Passaniti, Antonino; Roth, Thomas

doi:10.1042/bj2580413

Cited by 38 publications

(46 citation statements)

References 32 publications

(37 reference statements)

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“…The nuclear ferritin of the corneal epithelium may lack an L-subunit as appears to be true for other chicken tissues (20). Polyclonal antibodies against human liver ferritin, which are directed largely against ferritin-L, failed to react with the corneal epithelial cell nuclei, whereas strong reactivity was observed with two different anti-human ferritin polyclonals predominantly against the H-chain.…”

Section: Discussionmentioning

confidence: 94%

“…3B), extracts of all tissues behaved as described previously for purified chicken liver ferritin (20). Samples run in 2% SDS, without boiling and without reduction, gave a 240-kDa band (data not shown); in identical samples run in the presence of reducing agents, the band was shifted to 260 kDa (Fig.…”

Section: Figmentioning

confidence: 99%

“…Tissue-specific forms of the human protein complex result from different ratios of the H-and L-subunits (21), with the liver form being predominantly ferritin-L (1). The chicken liver ferritin aggregate, however, while having a molecular mass approximately the same as that of the human, has been reported to contain only the H-subunit (22 kDa) (20).…”

Section: Transcriptionmentioning

confidence: 99%

“…In certain samples some reactivity is also observed at 120 kDa and at the top of the gel (arrowhead). B, the purified adult chicken liver ferritin and each of the tissue samples gives the 260-kDa band expected for nondenatured chicken liver ferritin in the presence of reducing agents (20). The arrowhead indicates the top of the gel.…”

Section: Figmentioning

confidence: 99%

“…3B) protein extracts from embryonic chicken tissues. Extracts of corneal epithelium were compared with those from corneal stroma, liver, heart, and skin, as well as to the chromatographically purified protein (20). Under denaturing conditions (boiling in 1 or 2% SDS plus 1% ␤-mercaptoethanol) …”

Section: Transcriptionmentioning

confidence: 99%

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Ferritin Is a Developmentally Regulated Nuclear Protein of Avian Corneal Epithelial Cells

Cai

Birk

Linsenmayer

1997

Journal of Biological Chemistry

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Previously, we generated monoclonal antibodies against chicken corneal cells (Zak, N. B., and Linsenmayer, T. F. (1983) Dev. Biol. 99, 373). We have now observed that one group of these antibodies reacts with a developmentally regulated component of corneal epithelial cell nuclei. This component is the heavy chain of ferritin, as determined by analyses of immunoisolated cDNA clones and immunoblotting of the protein. Immunoblotting also suggests that the nuclear ferritin may be in a supramolecular form that is similar to the ironbinding ferritin complex found in the cytoplasm of many cells. In vitro cultures and transfection studies show that the nuclear localization depends predominantly on cell type but can be altered by the in vitro environment. The appearance of nuclear ferritin is at least partially under translational regulation, as is known to be true for the cytoplasmic form of the molecule. The tissue and developmental distributions of the mRNA for the molecule are much more extensive than the protein itself, and the removal of iron from cultures of corneal epithelial cells with the iron chelator deferoxamine prevents the appearance of nuclear ferritin. At present the functional role(s) of nuclear ferritin remain unknown, but previous studies on cytoplasmic ferritin raise the possibility that it prevents damage due to free radical generation ("oxidative stress") by sequestering iron. Although it remains to be tested whether nuclear ferritin prevents oxidative damage, we find this an attractive possibility. Since the corneal epithelium is transparent and is constantly exposed to free radical-generating UV light, it is possible that the cells of this tissue have evolved a specialized mechanism to prevent oxidative damage to their nuclear components.Nuclei contain a myriad of different proteins as well as nucleic acids. Nuclear proteins range from general ones, such as the histones that are universally present in cells and determine the structure of chromatin, to the DNA-binding regulatory proteins, some of which are cell-specific and developmentally regulated. In the present investigation, we provide evidence that within the corneal epithelium of embryonic chicks, ferritin is also a developmentally regulated nuclear protein. In other cell types that have been investigated, the molecule is cytoplasmic and is thought to function as a protective antioxidant by sequestering iron (1, 2) (see "Discussion").In earlier work we sought to identify developmentally regulated components of the embryonic avian cornea by generating hybridomas against corneal cell suspensions (3). By immunofluorescence, one group of antibodies (including antibody 6D11) reacted with a corneal epithelial antigen but had little or no detectable reactivity with other tissues in the embryo. During development, this antigen first became detectable by immunofluorescence in 12-day corneas, the time when the epithelium begins to stratify (4). We also found it to arise de novo in cultured corneas, and it has been used as a marker for corneal epithe...

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Section: Discussionmentioning

confidence: 94%

Section: Figmentioning

confidence: 99%

Section: Transcriptionmentioning

confidence: 99%

Section: Figmentioning

confidence: 99%

Section: Transcriptionmentioning

confidence: 99%

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Ferritin Is a Developmentally Regulated Nuclear Protein of Avian Corneal Epithelial Cells

Cai

Birk

Linsenmayer

1997

Journal of Biological Chemistry

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Ferritins in Chordata: Potential evolutionary trajectory marked by discrete selective pressures

et al. 2020

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Ferritins (FTs) are iron storage proteins that are involved in managing iron-oxygen balance. In our work, we present a hypothesis on the putative effect of geological changes that have affected the evolution and radiation of ferritin proteins. Based on sequence analysis and phylogeny reconstruction, we hypothesize that two significant factors have been involved in the evolution of ferritin proteins: fluctuations of atmospheric oxygen concentrations, altering redox potential, and changing availability of water rich in bioavailable ferric ions. Fish, ancient amphibians, reptiles, and placental mammals developed the broadest repertoire of singular FTs, attributable to embryonic growth in aquatic environments containing low oxygen levels and abundant forms of soluble iron. In contrast, oviparous land vertebrates, like reptiles and birds, that have developed in high oxygen levels and limited levels of environmental Fe 2+ exhibit a lower diversity of singular FTs, but display a broad repertoire of subfamilies, particularly notable in early reptiles.

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Electrophoretic patterns of microwaved and γ‐irradiated beef liver proteins

et al. 2001

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The effects of g-irradiation treatments (2.5, 5 and 10 kGy) and microwaves generated from an oven at low and defrost power settings for 0.5, 1 and 2 min on the total proteins and protein patterns of beef liver immediately after treatment and during frozen storage (À18°C) for different periods were studied. Chemical analyses indicated that the protein content of beef liver was reduced after exposure to g-radiation or microwaves and also during frozen storage. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) was used to illustrate the changes in protein bands of different molecular weights and their percentages before and after exposure to gamma and microwave radiation. The main effect of g-radiation on the protein patterns of beef liver was the disappearance of some high-molecular-weight protein bands and the development of other bands characterised by moderate and low molecular weights. This ®nding indicates the degradation of beef liver proteins by girradiation. In contrast, microwave treatment caused an increase in the levels of high-molecularweight protein bands with a concomitant decrease in low-molecular-weight protein bands. This phenomenon demonstrates the polymerisation of low-molecular-weight proteins under the in¯uence of microwaves.

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Purification of chicken liver ferritin by two novel methods and structural comparison with horse spleen ferritin

Cited by 38 publications

References 32 publications

Ferritin Is a Developmentally Regulated Nuclear Protein of Avian Corneal Epithelial Cells

Ferritin Is a Developmentally Regulated Nuclear Protein of Avian Corneal Epithelial Cells

Ferritins in Chordata: Potential evolutionary trajectory marked by discrete selective pressures

Electrophoretic patterns of microwaved and γ‐irradiated beef liver proteins

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