Structure of gene and pseudogenes of human apoferritin H

Costanzo, Francesco; Colombo, Monika; Staempfli, Susanne; Santoro, Claudio; Marone, Maria; Frank, Rainer; Delius, Hajo; Cortese, Riccardo

doi:10.1093/nar/14.2.721

Cited by 126 publications

(68 citation statements)

References 40 publications

(25 reference statements)

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“…21 Interestingly, ferritin in cancer cells consists mainly of heavy chains. 22,23 Others have suggested that there is another species of ferritin in cancer cells called super-heavy chain or P43. 24 In the present studies, we sought to characterize the nature of ferritin in melanoma cells and to investigate its possible effects on immune responses.…”

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confidence: 99%

Immunosuppressive effects of melanoma-derived heavy-chain ferritin are dependent on stimulation of IL-10 production

et al. 2001

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confidence: 99%

Immunosuppressive effects of melanoma-derived heavy-chain ferritin are dependent on stimulation of IL-10 production

et al. 2001

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“…Standardization was with respect to 28s and 18s rRNAs as well as by control hybridization with a human a-actin cDNA probe (pHM-aPX, kindly provided by Patrick Lemaire, EMBL, Heidelberg). The cDNA probes for individual genes were: pal-5 for al-antitrypsin [36]; pHL 1423 for human lysozyme; pHIL1-P for IL-1p (kindly provided by C. Schneider, ICGEB, Trieste, Italy) ; pha2ml for human a2-macroglobulin (kindly provided by G. Bell, Chiron, Emmeryville, USA) [37]; pFB for complement factor B (gift of D. Campbell, Oxford, UK); FRL600 for ferritin light chain [38] and FR36 for ferritin heavy chain [39] (gifts of F. Costanzo, Naples, Italy); IL-6 (IFNP2) cDNA [40] was a gift of Dr P. Seghal (Rockfeller University, New York, NY). The probes were 32P-labeled according to Feinberg and Vogelstein [41].…”

Section: Rna Extraction and Northern Blot Analysismentioning

confidence: 99%

Characterization of mononuclear‐phagocyte terminal maturation by mRNA phenotyping using a set of cloned cDNA probes

Ganter

Bauer

Majello³

et al. 1989

European Journal of Biochemistry

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The terminal step in the maturation of mononuclear cells from circulating monocytes to resident macrophages is accompanied by dramatic changes in cell morphology and physiology. Applying a cultivation system which allows peripheral monocytes to undergo terminal maturation in vitro under absolutely endotoxin-free conditions, we have determined the pattern of expression of a set of eight genes by mRNA phenotyping. The results can be summarized as follows: the two protease inhibitors al-antitrypsin and a2-macroglobulin show a inverse pattern of expression. al-Antitrypsin mRNA is repressed, a,-macroglobulin mRNA is strongly induced during maturation to macrophages. Therefore, these two genes are excellent markers of the terminal maturation. In addition, ferritinlight-chain mRNA progressively increases during the course of differentiation, providing a further marker for maturation. Gene expression as a function of activation was studied in mononuclear cells stimulated with bacterial endotoxin (lipopolysaccharide). In monocytes, complement-factor-B, interleukin-1 and interleukin-6 mRNAs are drastically induced upon lipopolysaccharide activation whereas lysozyme RNA is strongly repressed. However, the ability of all four genes to respond to endotoxin was markedly diminished or abolished in mature macrophages, indicating that susceptibility to a certain type of activation may be restricted to a specific stage of maturation. Our data show that mRNA phenotyping is excellently suited for the characterization of the differentiation and activation state of mononuclear phagocytes.The mononuclear phagocyte lineage consists of cells at different stages of maturation linking monoblasts and promonocytes as precursors in the bone marrow with circulating blood monocytes, which leave the bloodstream and become resident macrophages in a variety of tissues and body cavities (for reviews, see [l -31). Besides ingestion and killing of bacteria and parasites and in addition to serving as antigenpresenting cells to lymphocytes, mononuclear phagocytes function upon injury or infection to release a wide range of cytokines acting as inflammatory mediators. Recently mononuclear phagocytes were found to also secrete factors central to the wound-healing response [4].Cells of the mononuclear phagocyte system exhibit marked heterogeneity. Differentiated macrophages can be distinguished from monocytes not only by increased size and maturation of organelles [5 -91 but also by substantial changes in the pattern of surface antigens [9 -171. The situation is complicated, however, in that both monocytes and macrophages change their physiological behaviour upon stimulation by bacterial agents such as the endotoxin lipopolysaccharide [18]. It is therefore desirable to establish a marker system which allows characterization of mononuclear phagocytes in regard to the stage of maturation and the state of activation.We have employed a previously described in vitro cultivation system [15,19, 201 Abbreviations. IL-6, interleukin-6; IL-1, interleukin-1.monocy...

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“…1) and human H gene (6) contain a modest excess of G-C bases, 64% and 72%, respectively. Upstream of the TATAA box is a 29-bp sequence (-65 to -38), of which 27 bases are conserved in the human H-flanking region (6), and the last 6 are also found in the chicken H gene (33). In the rat (Fig.…”

Section: Spiomentioning

confidence: 99%

“…However, the isolation of genomic copies encoding the human H subunit (6,7) and human and rat L subunits (8,9) has demonstrated the presence of several processed pseudogenes. In addition,…”

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confidence: 99%

“…isolation of H-subunit cDNAs (H cDNAs) from human liver, lymphocytes, HeLa cells, and endothelial cells yielded identical sequences (6), and only one of the numerous gene copies of the rat L subunit appears to be expressed (9). Accordingly, in order to complete the picture for the rat ferritin genes, we have examined the gene copies for the rat H subunit and report that only one appears to be expressed.…”

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Conservation of ferritin heavy subunit gene structure: implications for the regulation of ferritin gene expression.

Murray

White

Munro

1987

Proc. Natl. Acad. Sci. U.S.A.

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Ferritin stores iron within a protein shell consisting of 24 subunits of two types, heavy (H) and light (L). According to Southern blotting, the rat genome contains four copies homologous to the H-subunit cDNA (H cDNA). To determine whether only one of these is expressed, H cDNAs isolated from rat liver and heart mRNAs were compared and found to share identical nucleotide sequences. Next, genomic clones for three of the four rat H-subunit loci were isolated. Two were classical processed pseudogenes, whereas the third contained an expressed gene. RNase intron mapping of this expressed gene generated the same exon protection pattern when total RNA from rat liver or heart was used, indicating that this gene accounts for most or all of the H-subunit mRNAs (H mRNAs) in these tissues. Comparison of the expressed rat H-subunit gene (H gene) structure with published sequences for other species displays considerable conservation. The coding sequence of the rat H gene predicts 95% similarity to the human amino acid sequence, thus being more highly conserved than the L-subunit sequence of these species. Near the cap region of the 5' untranslated region, the rat H mRNA displays a 28-nucleotide sequence that is almost totally conserved in the corresponding region of the human, bullfrog, and chicken H mRNA and is also faithfully represented in the rat and human L-subunit mRNAs (L mRNAs), thus making this sequence a prime candidate for involvement in the known translational regulation of both subunits by iron. In the 5' flanking region, partially conserved sequences common to H gene and L-subunit gene (L gene) of the rat may be involved in transcriptional regulation by iron, whereas those conserved only in the H gene of man and the rat imply that other factors may independently control H-subunit regulation.

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Structure of gene and pseudogenes of human apoferritin H

Cited by 126 publications

References 40 publications

Immunosuppressive effects of melanoma-derived heavy-chain ferritin are dependent on stimulation of IL-10 production

Immunosuppressive effects of melanoma-derived heavy-chain ferritin are dependent on stimulation of IL-10 production

Characterization of mononuclear‐phagocyte terminal maturation by mRNA phenotyping using a set of cloned cDNA probes

Conservation of ferritin heavy subunit gene structure: implications for the regulation of ferritin gene expression.

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