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Articles de revues sur le sujet « H-ferritin »

Auteur : Grafiati

Publié le 9 mars 2023

Mis à jour le 31 juillet 2025

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1

CORSI, Barbara, Federica PERRONE, Monique BOURGEOIS, et al. "Transient overexpression of human H- and L-ferritin chains in COS cells." Biochemical Journal 330, no. 1 (1998): 315–20. http://dx.doi.org/10.1042/bj3300315.

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The understanding of the in vitro mechanisms of ferritin iron incorporation has greatly increased in recent years with the studies of recombinant and mutant ferritins. However, little is known about how this protein functions in vivo, mainly because of the lack of cellular models in which ferritin expression can be modulated independently from iron. To this aim, primate fibroblastoid COS-7 cells were transiently transfected with cDNAs for human ferritin H- and L-chains under simian virus 40 promoter and analysed within 66 h. Ferritin accumulation reached levels 300-500-fold higher than backgro

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Fargion, S., AL Fracanzani, B. Brando, P. Arosio, S. Levi, and G. Fiorelli. "Specific binding sites for H-ferritin on human lymphocytes: modulation during cellular proliferation and potential implication in cell growth control." Blood 78, no. 4 (1991): 1056–61. http://dx.doi.org/10.1182/blood.v78.4.1056.1056.

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Abstract Interactions between human recombinant H- and L-ferritins and human lymphocytes were studied in vitro by direct binding assays and by flow cytometry. L-ferritin did not cause detectable specific binding, whereas H-ferritin showed a specific and saturable binding that increased markedly in phytohemagglutinin (PHA)-stimulated cells. This ferritin bound up to 30% of CD4+ and CD8+ T-lymphocytes and most B cells, indicating that expression of ferritin binding sites is not related to cell lineage or function. Dual-color flow cytometry experiments showed that ferritin binding sites were pres

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Fargion, S., AL Fracanzani, B. Brando, P. Arosio, S. Levi, and G. Fiorelli. "Specific binding sites for H-ferritin on human lymphocytes: modulation during cellular proliferation and potential implication in cell growth control." Blood 78, no. 4 (1991): 1056–61. http://dx.doi.org/10.1182/blood.v78.4.1056.bloodjournal7841056.

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Interactions between human recombinant H- and L-ferritins and human lymphocytes were studied in vitro by direct binding assays and by flow cytometry. L-ferritin did not cause detectable specific binding, whereas H-ferritin showed a specific and saturable binding that increased markedly in phytohemagglutinin (PHA)-stimulated cells. This ferritin bound up to 30% of CD4+ and CD8+ T-lymphocytes and most B cells, indicating that expression of ferritin binding sites is not related to cell lineage or function. Dual-color flow cytometry experiments showed that ferritin binding sites were present on ce

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Bauminger, E. R., A. Treffry, A. J. Hudson, et al. "Iron incorporation into ferritins: evidence for the transfer of monomeric Fe(III) between ferritin molecules and for the formation of an unusual mineral in the ferritin of Escherichia coli." Biochemical Journal 302, no. 3 (1994): 813–20. http://dx.doi.org/10.1042/bj3020813.

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Iron that has been oxidized by H-chain ferritin can be transferred into other ferritin molecules before it is incorporated into mature ferrihydrite iron cores. Iron(III) dimers are formed at the ferroxidase centres of ferritin H chains at an early stage of Fe(II) oxidation. Mössbauer spectroscopic data now show that the iron is transferred as monomeric species arising from dimer dissociation and that it binds to the iron core of the acceptor ferritin. Human H-chain ferritin variants containing altered threefold channels can act as acceptors, as can the ferritin of Escherichia coli (Ec-FTN). A

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Lobreaux, S., S. J. Yewdall, J. F. Briat, and P. M. Harrison. "Amino-acid sequence and predicted three-dimensional structure of pea seed (Pisum sativum) ferritin." Biochemical Journal 288, no. 3 (1992): 931–39. http://dx.doi.org/10.1042/bj2880931.

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The iron storage protein, ferritin, is widely distributed in the living kingdom. Here the complete cDNA and derived amino-acid sequence of pea seed ferritin are described, together with its predicted secondary structure, namely a four-helix-bundle fold similar to those of mammalian ferritins, with a fifth short helix at the C-terminus. An N-terminal extension of 71 residues contains a transit peptide (first 47 residues) responsible for plastid targetting as in other plant ferritins, and this is cleaved before assembly. The second part of the extension (24 residues) belongs to the mature subuni

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Ebrahimi, Kourosh Honarmand, Eckhard Bill, Peter-Leon Hagedoorn, and Wilfred R. Hagen. "Spectroscopic evidence for the role of a site of the di-iron catalytic center of ferritins in tuning the kinetics of Fe(ii) oxidation." Molecular BioSystems 12, no. 12 (2016): 3576–88. http://dx.doi.org/10.1039/c6mb00235h.

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Spectroscopic studies of human H-type ferritin in comparison with an archaeal ferritin from Pyrococcus furiosus reveal how kinetics of a common mechanism of Fe(ii) oxidation is tuned differently in these two ferritins.

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Fargion, S., P. Arosio, AL Fracanzani, et al. "Characteristics and expression of binding sites specific for ferritin H- chain on human cell lines." Blood 71, no. 3 (1988): 753–57. http://dx.doi.org/10.1182/blood.v71.3.753.753.

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Abstract Purified recombinant human ferritin composed solely of H subunit was radiolabeled and incubated with proerythroleukemic K562 human cells. A specific binding was detected, and it could be displaced only by ferritins, natural or recombinant, containing large proportion of the H subunit. The specific ferritin H-chain binding was saturable, and cells showed 17,000 to 23,000 binding sites per cell. The affinity constant measured at 37 degrees C was of 3 x 10(8) M-1. Treatment with pronase eliminated the specific binding. The binding sites were expressed in a high number during the cellular

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Fargion, S., P. Arosio, AL Fracanzani, et al. "Characteristics and expression of binding sites specific for ferritin H- chain on human cell lines." Blood 71, no. 3 (1988): 753–57. http://dx.doi.org/10.1182/blood.v71.3.753.bloodjournal713753.

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Purified recombinant human ferritin composed solely of H subunit was radiolabeled and incubated with proerythroleukemic K562 human cells. A specific binding was detected, and it could be displaced only by ferritins, natural or recombinant, containing large proportion of the H subunit. The specific ferritin H-chain binding was saturable, and cells showed 17,000 to 23,000 binding sites per cell. The affinity constant measured at 37 degrees C was of 3 x 10(8) M-1. Treatment with pronase eliminated the specific binding. The binding sites were expressed in a high number during the cellular exponent

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Morikawa, K., F. Oseko, and S. Morikawa. "H- and L-rich ferritins suppress antibody production, but not proliferation, of human B lymphocytes in vitro." Blood 83, no. 3 (1994): 737–43. http://dx.doi.org/10.1182/blood.v83.3.737.737.

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Abstract The effect of human spleen(L-rich) and heart(H-rich) ferritins on the proliferation and differentiation of human B lymphocytes was studied in comparison with that of holo- and apo-transferrins. Ferritins rich in H and L chain, as well as the transferrins, did not inhibit the proliferative response of resting and activated B cells stimulated with polyclonal B-cell mitogen, Staphylococcus aureus Cowan strain I. In contrast, the ferritins, but not the transferrins, clearly suppressed the antibody production by B blasts in T-cell-independent as well as T- cell-dependent system. Kinetic st

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Morikawa, K., F. Oseko, and S. Morikawa. "H- and L-rich ferritins suppress antibody production, but not proliferation, of human B lymphocytes in vitro." Blood 83, no. 3 (1994): 737–43. http://dx.doi.org/10.1182/blood.v83.3.737.bloodjournal833737.

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The effect of human spleen(L-rich) and heart(H-rich) ferritins on the proliferation and differentiation of human B lymphocytes was studied in comparison with that of holo- and apo-transferrins. Ferritins rich in H and L chain, as well as the transferrins, did not inhibit the proliferative response of resting and activated B cells stimulated with polyclonal B-cell mitogen, Staphylococcus aureus Cowan strain I. In contrast, the ferritins, but not the transferrins, clearly suppressed the antibody production by B blasts in T-cell-independent as well as T- cell-dependent system. Kinetic study showe

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Cozzi, Anna, Paolo Santambrogio, Daniela Privitera, et al. "Human L-ferritin deficiency is characterized by idiopathic generalized seizures and atypical restless leg syndrome." Journal of Experimental Medicine 210, no. 9 (2013): 1779–91. http://dx.doi.org/10.1084/jem.20130315.

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The ubiquitously expressed iron storage protein ferritin plays a central role in maintaining cellular iron homeostasis. Cytosolic ferritins are composed of heavy (H) and light (L) subunits that co-assemble into a hollow spherical shell with an internal cavity where iron is stored. The ferroxidase activity of the ferritin H chain is critical to store iron in its Fe3+ oxidation state, while the L chain shows iron nucleation properties. We describe a unique case of a 23-yr-old female patient affected by a homozygous loss of function mutation in the L-ferritin gene, idiopathic generalized seizures

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Ruscitti, P., P. Di Benedetto, O. Berardicurti, et al. "FRI0006 ASSESSING PRO-INFLAMMATORY PROPERTIES OF H-FERRITIN BY EX VIVO AND IN VITRO OBSERVATIONS." Annals of the Rheumatic Diseases 79, Suppl 1 (2020): 574.2–574. http://dx.doi.org/10.1136/annrheumdis-2020-eular.3473.

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Background:The concept of ‘hyperferritinemic syndrome’ has recently been proposed, suggesting high levels of ferritin as pathogenic pro-inflammatory mediator [1] Ferritin is an intracellular iron storage protein, comprising 24 subunits, heavy (H) and light (L) based on molecular weight. The H-/L subunits ratio may be different in tissues, since the ferritin enriched in L subunits (L-ferritin) and the ferritin enriched in H subunits (H-ferritin) may be observed in different tissues, according to pathophysiologic status [1].Objectives:We aimed to assess the presence of H- and L-ferritin as well

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Fisher, J., K. Devraj, J. Ingram, et al. "Ferritin: a novel mechanism for delivery of iron to the brain and other organs." American Journal of Physiology-Cell Physiology 293, no. 2 (2007): C641—C649. http://dx.doi.org/10.1152/ajpcell.00599.2006.

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Traditionally, transferrin has been considered the primary mechanism for cellular iron delivery, despite suggestive evidence for additional iron delivery mechanisms. In this study we examined ferritin, considered an iron storage protein, as a possible delivery protein. Ferritin consists of H- and L-subunits, and we demonstrated iron uptake by ferritin into multiple organs and that the uptake of iron is greater when the iron is delivered via H-ferritin compared with L-ferritin. The delivery of iron via H-ferritin but not L-ferritin was significantly decreased in mice with compromised iron stora

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PARTHASARATHY, Narayanan, Suzy V. TORTI, and Frank M. TORTI. "Ferritin binds to light chain of human H-kininogen and inhibits kallikrein-mediated bradykinin release." Biochemical Journal 365, no. 1 (2002): 279–86. http://dx.doi.org/10.1042/bj20011637.

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Ferritin is an iron-storage protein that exists in both intracellular and extracellular compartments. We have previously identified H-kininogen (high-molecular-weight kininogen) as a ferritin-binding protein [Torti and Torti (1998) J. Biol. Chem. 273, 13630–13635]. H-Kininogen is a precursor of the potent pro-inflammatory peptide bradykinin, which is released from H-kininogen following cleavage of H-kininogen by the serine protease kallikrein. In this report, we demonstrate that binding of ferritin to H-kininogen occurs via the modified light chain of H-kininogen, and that ferritin binds prefe

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15

Van Wuytswinkel, O., G. Savino, and J. F. Briat. "Purification and characterization of recombinant pea-seed ferritins expressed in Escherichia coli: influence of N-terminus deletions on protein solubility and core formation in vitro." Biochemical Journal 305, no. 1 (1995): 253–61. http://dx.doi.org/10.1042/bj3050253.

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Plant ferritin subunits are synthesized as precursor molecules; the transit peptide (TP) in their NH2 extremity, responsible for plastid targeting, is cleaved during translocation to this compartment. In addition, the N-terminus of the mature subunit contains a plant-specific sequence named extension peptide (EP) [Ragland, Briat, Gagnon, Laulhère, Massenet, and Theil, E.C. (1990) J. Biol. Chem. 265, 18339-18344], the function of which is unknown. A novel pea-seed ferritin cDNA, with a consensus ferroxidase centre conserved within H-type animal ferritins has been characterized. This pea-seed fe

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SANTAMBROGIO, Paolo, Patrizia PINTO, Sonia LEVI, et al. "Effects of modifications near the 2-, 3- and 4-fold symmetry axes on human ferritin renaturation." Biochemical Journal 322, no. 2 (1997): 461–68. http://dx.doi.org/10.1042/bj3220461.

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Ferritin is a protein of 24 subunits which assemble into a shell with 432 point symmetry. It can be denatured reversibly in acidic guanidine hydrochloride, with the formation of poorly populated renaturation intermediates. In order to increase the accumulation of intermediates and to study the mechanism of ferritin renaturation, we analysed variants of the human ferritin H-chain altered at the N-terminus (Δ1–13), near the 4-fold axis (Leu-169→Arg), the 3-fold axis (Asp-131→Ile+Glu-134→Phe) or the 2-fold axis (Ile-85→Cys). We also carried out specific chemical modifications of Cys-130 (near the

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Treffry, A., E. R. Bauminger, D. Hechel, et al. "Defining the roles of the threefold channels in iron uptake, iron oxidation and iron-core formation in ferritin: a study aided by site-directed mutagenesis." Biochemical Journal 296, no. 3 (1993): 721–28. http://dx.doi.org/10.1042/bj2960721.

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This paper aims to define the role of the threefold intersubunit channels in iron uptake and sequestration processes in the iron-storage protein, ferritin. Iron uptake, measured as loss of availability of Fe(II) to ferrozine (due to oxidation), has been studied in recombinant human H-chain ferritins bearing amino acid substitutions in the threefold channels or ferroxidase centres. Similar measurements with recombinant horse L-chain ferritin are compared. It is concluded that significant Fe(II) oxidation occurs only at the H-chain ferroxidase centres and not in the threefold channels, although

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Lo, James, та Robert AR Hurta. "Transforming growth factor β1 selectively regulates ferritin gene expression in malignant H-ras-transformed fibrosarcoma cell lines". Biochemistry and Cell Biology 78, № 4 (2000): 527–35. http://dx.doi.org/10.1139/o00-062.

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Transforming growth factor β1 is an important growth regulator in many cell types, usually exerting a negative effect on cellular growth. Inhibition of DNA synthesis and cell proliferation is frequently lost during malignant transformation, and in some cases, tumor cell proliferation is actually stimulated by TGF-β1. The present study demonstrates a novel link between alterations in TGF-β1 regulation during malignant conversion, and the expression of ferritin, an important activity involved in a number of biological functions including iron homeostasis and cell-growth control. A series of H-ra

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Mackenzie, Elizabeth L., and Yoshiaki Tsuji. "Elevated intracellular calcium increases ferritin H expression through an NFAT-independent post-transcriptional mechanism involving mRNA stabilization." Biochemical Journal 411, no. 1 (2008): 107–13. http://dx.doi.org/10.1042/bj20071544.

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An increase in intracellular Ca2+ is one of the initiating events in T-cell activation. A calcium-mediated signalling cascade in T-cells involves activation of calcineurin and the dephosphorylation and translocation of NFAT (nuclear factor of activated T-cells), resulting in the transcriptional activation of target genes such as IL-2 (interleukin-2). In the present study, we found that increased intracellular calcium leads to induction of the antioxidant protein ferritin H. We previously reported that the ferritin H gene is transcriptionally activated under oxidative stress conditions through

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Cozzi, Anna, Barbara Corsi, Sonia Levi, Paolo Santambrogio, Giorgio Biasiotto, and Paolo Arosio. "Analysis of the biologic functions of H- and L-ferritins in HeLa cells by transfection with siRNAs and cDNAs: evidence for a proliferative role of L-ferritin." Blood 103, no. 6 (2004): 2377–83. http://dx.doi.org/10.1182/blood-2003-06-1842.

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Abstract We describe the use of small interfering RNAs (siRNAs) to down-regulate H- and L-ferritin levels in HeLa cells. siRNAs repressed H- and L-ferritin expression to about 20% to 25% of the background level in both stable and transient transfections. HeLa cells transfected with H- and L-ferritin cDNAs were analyzed in parallel to compare the effects of ferritin up- and down-regulation. We found that large modifications of L-ferritin levels did not affect iron availability in HeLa cells but positively affected cell proliferation rate in an iron-independent manner. The transient down-regulat

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Pozzi, Cecilia, Flavio Di Pisa, Caterina Bernacchioni, Silvia Ciambellotti, Paola Turano, and Stefano Mangani. "Iron binding to human heavy-chain ferritin." Acta Crystallographica Section D Biological Crystallography 71, no. 9 (2015): 1909–20. http://dx.doi.org/10.1107/s1399004715013073.

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Maxi-ferritins are ubiquitous iron-storage proteins with a common cage architecture made up of 24 identical subunits of five α-helices that drive iron biomineralization through catalytic iron(II) oxidation occurring at oxidoreductase sites (OS). Structures of iron-bound human H ferritin were solved at high resolution by freezing ferritin crystals at different time intervals after exposure to a ferrous salt. Multiple binding sites were identified that define the iron path from the entry ion channels to the oxidoreductase sites. Similar data are available for another vertebrate ferritin: the M p

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PANG, Jong-Hwei S., Chia-Jung WU, and Lee-Young CHAU. "Post-transcriptional regulation of H-ferritin gene expression in human monocytic THP-1 cells by protein kinase C." Biochemical Journal 319, no. 1 (1996): 185–89. http://dx.doi.org/10.1042/bj3190185.

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The mRNA coding for H-ferritin was highly induced in human monocytic THP-1 cells following treatment with phorbol 12-myristate 13-acetate (PMA). The induction was detected at 3 h, reached maximal levels at 12 h, and was sustained for up to 48 h subsequent to PMA exposure. PMA-induced up-regulation of H-ferritin gene expression was also observed in other leukaemic cell lines, HL60 and U937, but not in non-leukaemic cell types, including human fibroblasts, endothelial cells and smooth muscle cells. The effect of PMA could be completely blocked by the protein kinase C inhibitor, H-7. Furthermore,

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Yeh, Kwo-Yih, Mary Yeh, and Jonathan Glass. "Glucocorticoids and dietary iron regulate postnatal intestinal heavy and light ferritin expression in rats." American Journal of Physiology-Gastrointestinal and Liver Physiology 278, no. 2 (2000): G217—G226. http://dx.doi.org/10.1152/ajpgi.2000.278.2.g217.

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To cope with increasing dietary iron exposure, the intestinal epithelium of weaning rats must control intracellular labile iron pools. Intestinal expression of heavy (H) and light (L) ferritin subunits during early weaning and after cortisone administration and/or iron feeding was investigated. Changes in H and L ferritin gene expression were determined by nuclear runoff transcriptional assay, Northern blot analysis, and metabolic labeling of protein synthesis. H ferritin mRNA levels did not change between days 12 and 15, doubled on day 18, and tripled on day 24. L ferritin mRNA was reduced by

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Carraway, M. S., A. J. Ghio, J. L. Taylor, and C. A. Piantadosi. "Induction of ferritin and heme oxygenase-1 by endotoxin in the lung." American Journal of Physiology-Lung Cellular and Molecular Physiology 275, no. 3 (1998): L583—L592. http://dx.doi.org/10.1152/ajplung.1998.275.3.l583.

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Heme oxygenase (HO)-1 expression is increased by forms of oxidative stress that also induce ferritin. Even though this could result from release of iron by heme degradation, we hypothesized that ferritin expression in the lung after endotoxin [lipopolysaccharide (LPS)] would occur independently of HO-1 because iron sequestration is an important response to infection. We tested this hypothesis by instilling saline or LPS (1 mg) into lungs of rats and measuring ferritin expression, HO-1 expression and activity, and HO-1 and ferritin mRNAs at different times. Lungs were also inflation fixed for i

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Smirnova, L. A., Z. I. Kravchuk, and Zh M. Kozich. "H- AND L-FERRITINS IN ACUTE LEUKEMIA." Health and Ecology Issues, no. 2S (December 28, 2011): 81–83. http://dx.doi.org/10.51523/2708-6011.2011-8-2s-28.

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We have studied H- and L-subunits of ferritin in acute leukemia. Our data makes it possible to suggest that the appearance of considerable numbers of ferritin in the serum of patients with clonal blood diseases is connected with its secretion with lymphocytes. As it is impossible to establish the reliable correlation between the dimension of the tumor in leukemia and the level of ferritin, then the ferritin secretion is hypothetically relating to its regulatory functions. We have shown that the separate testing of H- and L-forms of ferritin makes it possible to determine the content of serum f

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Ferreira, Chrystophe, Paolo Santambrogio, Marie-Elise Martin, et al. "H ferritin knockout mice: a model of hyperferritinemia in the absence of iron overload." Blood 98, no. 3 (2001): 525–32. http://dx.doi.org/10.1182/blood.v98.3.525.

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Abstract Ferritin, the iron-storing molecule, is made by the assembly of various proportions of 2 different H and L subunits into a 24-mer protein shell. These heteropolymers have distinct physicochemical properties, owing to the ferroxidase activity of the H subunit, which is necessary for iron uptake by the ferritin molecule, and the ability of the L subunit to facilitate iron core formation inside the protein shell. It has previously been shown that H ferritin is indispensable for normal development, since inactivation of the H ferritin gene by homologous recombination in mice is lethal at

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Pattanapanyasat, K., T. G. Hoy, and A. Jacobs. "The response of intracellular and surface ferritin after T-cell stimulation in vitro." Clinical Science 73, no. 6 (1987): 605–11. http://dx.doi.org/10.1042/cs0730605.

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1. Measurements of T-lymphocyte surface ferritin using flow cytometry show that phytohaemagglutinin (PHA) stimulation causes a marked increase in the number of cells bearing spleen-type (S) and heart-type (H) ferritin on their membrane, whereas no such change occurs in non-stimulated cells. This coincides with increases in interleukin-2 receptors, transferrin receptors and HLA-DR antigen. 2. There is an increase in the intracellular concentration of both S- and H-ferritin in lymphocytes after PHA stimulation: H-ferritin increases five- to seven-fold, but S-ferritin only two- to three-fold. The

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Arosio, Paolo, Fernando Carmona, Raffaella Gozzelino, Federica Maccarinelli, and Maura Poli. "The importance of eukaryotic ferritins in iron handling and cytoprotection." Biochemical Journal 472, no. 1 (2015): 1–15. http://dx.doi.org/10.1042/bj20150787.

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Ferritins, the main intracellular iron storage proteins, have been studied for over 60 years, mainly focusing on the mammalian ones. This allowed the elucidation of the structure of these proteins and the mechanisms regulating their iron incorporation and mineralization. However, ferritin is present in most, although not all, eukaryotic cells, comprising monocellular and multicellular invertebrates and vertebrates. The aim of this review is to provide an update on the general properties of ferritins that are common to various eukaryotic phyla (except plants), and to give an overview on the str

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ORINO, Kouichi, Lori LEHMAN, Yoshiaki TSUJI, Hitoshi AYAKI, Suzy V. TORTI, and Frank M. TORTI. "Ferritin and the response to oxidative stress." Biochemical Journal 357, no. 1 (2001): 241–47. http://dx.doi.org/10.1042/bj3570241.

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Iron is required for normal cell growth and proliferation. However, excess iron is potentially harmful, as it can catalyse the formation of toxic reactive oxygen species (ROS) via Fenton chemistry. For this reason, cells have evolved highly regulated mechanisms for controlling intracellular iron levels. Chief among these is the sequestration of iron in ferritin. Ferritin is a 24 subunit protein composed of two subunit types, termed H and L. The ferritin H subunit has a potent ferroxidase activity that catalyses the oxidation of ferrous iron, whereas ferritin L plays a role in iron nucleation a

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Kim, Kyung-Suk, Hyang-Ran Mun, and Jung-Hoo Lee. "Iron cores of tadpole ferritin: native, reconstituted and recombinant H-chain ferritins." Inorganica Chimica Acta 298, no. 1 (2000): 107–11. http://dx.doi.org/10.1016/s0020-1693(99)00423-5.

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Salatino, Alessandro, Ilenia Aversa, Anna Martina Battaglia, et al. "H-Ferritin Affects Cisplatin-Induced Cytotoxicity in Ovarian Cancer Cells through the Modulation of ROS." Oxidative Medicine and Cellular Longevity 2019 (October 31, 2019): 1–13. http://dx.doi.org/10.1155/2019/3461251.

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Reactive oxygen species (ROS) mediates cisplatin-induced cytotoxicity in tumor cells. However, when cisplatin-induced ROS do not reach cytotoxic levels, cancer cells may develop chemoresistance. This phenomenon can be attributed to the inherited high expression of antioxidant protein network. H-Ferritin is an important member of the antioxidant system due to its ability to store iron in a nontoxic form. Altered expression of H-Ferritin has been described in ovarian cancers; however, its functional role in cisplatin-based chemoresistance of this cancer type has never been explored. Here, we inv

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Bou-Abdallah, Fadi, John Paliakkara, Galina Melman, and Artem Melman. "Reductive Mobilization of Iron from Intact Ferritin: Mechanisms and Physiological Implication." Pharmaceuticals 11, no. 4 (2018): 120. http://dx.doi.org/10.3390/ph11040120.

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Ferritins are highly conserved supramolecular protein nanostructures composed of two different subunit types, H (heavy) and L (light). The two subunits co-assemble into a 24-subunit heteropolymer, with tissue specific distributions, to form shell-like protein structures within which thousands of iron atoms are stored as a soluble inorganic ferric iron core. In-vitro (or in cell free systems), the mechanisms of iron(II) oxidation and formation of the mineral core have been extensively investigated, although it is still unclear how iron is loaded into the protein in-vivo. In contrast, there is a

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Rogers, JT. "Ferritin translation by interleukin-6: the role of sequences upstream of the start codons of the heavy and light subunit genes." Blood 87, no. 6 (1996): 2525–37. http://dx.doi.org/10.1182/blood.v87.6.2525.bloodjournal8762525.

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Interleukin-1beta (IL-1beta) elevates H- and L-ferritin subunit synthesis in both human hepatoma cells (HepG2) and primary human umbilical vein endothelial cells. Ferritin induction is greater than the increase in total HepG2 protein synthesis in response to IL-1. IL-6 causes a moderate increase in L-subunit synthesis. The levels of the mRNAs for the ferritin H-subunits (H-mRNA) and light subunits (L-mRNA) remain unchanged, indicating that expression of the iron storage protein, ferritin, is regulated by translational mechanisms during inflammation. We have found a translational enhancer regio

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Percy, Maire E., Sharon J. Bauer, Susan Rainey, Donald R. C. McLachlan, Madhu S. Dhar, and Jayant G. Joshi. "Localization of a new ferritin heavy chain sequence present in human brain mRNA to chromosome 11." Genome 38, no. 3 (1995): 450–57. http://dx.doi.org/10.1139/g95-059.

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Two types of ferritin heavy (H) chain clones have been isolated from cDNA libraries of human fetal and adult brain: one corresponds to the ferritin H chain mRNA that is abundant in liver and is called "liver-like" brain cDNA; the other contains an additional 279 nucleotide (nt) sequence in the 3′untranslated region and is called brain ferritin H chain cDNA. To map the 279-nt sequence, polymerase chain reaction (PCR) amplification was carried out using DNA from rodent × human hybrid cell lines containing single human chromosomes as templates, and oligomeric primers homologous to the 3′end of th

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Xie, Changchuan, Na Zhang, Huamin Zhou, et al. "Distinct Roles of Basal Steady-State and Induced H-Ferritin in Tumor Necrosis Factor-Induced Death in L929 Cells." Molecular and Cellular Biology 25, no. 15 (2005): 6673–81. http://dx.doi.org/10.1128/mcb.25.15.6673-6681.2005.

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ABSTRACT Tumor necrosis factor (TNF) alpha is a cytokine capable of inducing caspase-dependent (apoptotic) cell death in some cells and caspase-independent (necrosis-like) cell death in others. Here, using a mutagenesis screen for genes critical in TNF-induced death in L929 cells, we have found that H-ferritin deficiency is responsible for TNF resistance in a mutant line and that, upon treatment with TNF, this line fails to elevate levels of labile iron pool (LIP), critical for TNF-induced reactive oxygen species (ROS) production and ROS-dependent cell death. Since we found that TNF-induced LI

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Yeh, K. Y., X. Alvarez-Hernandez, J. Glass, and M. Yeh. "Rat intestinal and hepatic ferritin subunit expression during development and after dietary iron feeding." American Journal of Physiology-Gastrointestinal and Liver Physiology 270, no. 3 (1996): G498—G505. http://dx.doi.org/10.1152/ajpgi.1996.270.3.g498.

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Ferritin consists of 24 heavy (H) and light (L) subunits in varying proportions in different tissues and plays a significant role in iron metabolism. We studied rat ferritin subunit expression in the duodenum and liver during early life, when a cycle of iron depletion and repletion occurs. In both tissues, ferritin contents decreased to low levels from day 3 to day 12. The ferritin on day 3 had an H/L mRNA ration of 0.9 and an H/L subunit ratio of 0.6. The decrease of tissue ferritin levels, but not mRNA, on day 12 suggests translational repression consistent with iron depletion. In the duoden

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Chen, Thomas T., Li Li, Dong-Hui Chung, et al. "TIM-2 is expressed on B cells and in liver and kidney and is a receptor for H-ferritin endocytosis." Journal of Experimental Medicine 202, no. 7 (2005): 955–65. http://dx.doi.org/10.1084/jem.20042433.

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T cell immunoglobulin-domain and mucin-domain (TIM) proteins constitute a receptor family that was identified first on kidney and liver cells; recently it was also shown to be expressed on T cells. TIM-1 and -3 receptors denote different subsets of T cells and have distinct regulatory effects on T cell function. Ferritin is a spherical protein complex that is formed by 24 subunits of H- and L-ferritin. Ferritin stores iron atoms intracellularly, but it also circulates. H-ferritin, but not L-ferritin, shows saturable binding to subsets of human T and B cells, and its expression is increased in

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Holmes, David. "Novel protective role of H-Ferritin." Nature Reviews Nephrology 9, no. 11 (2013): 625. http://dx.doi.org/10.1038/nrneph.2013.193.

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Pujol Carrión, Nuria, and Maria Ángeles de la Torre-Ruiz. "Heterologous Expression of Either Human or Soya Bean Ferritins in Budding Yeast Reveals Common Functions Protecting Against Oxidative Agents and Counteracting Double-Strand Break Accumulation." Biomolecules 15, no. 3 (2025): 447. https://doi.org/10.3390/biom15030447.

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Ferritins are globular proteins that, upon self-assembly in nanocages, are capable of bio-safely storing huge concentrations of bioavailable iron. They are present in most cell types and organisms; one of the exceptions is yeast. Heterologous expression of either human or vegetal ferritins in Saccharomyces cerevisiae revealed new and unknown functions for soya bean ferritins; validated this model by confirming previously characterized functions in human ferritins and also demonstrated that, like human H chain, vegetal H1, and H2 chains also shown a tendency to localize in the nucleus when expr

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SURGULADZE, Nodar, Stephanie PATTON, Anna COZZI, Michael G. FRIED, and James R. CONNOR. "Characterization of nuclear ferritin and mechanism of translocation." Biochemical Journal 388, no. 3 (2005): 731–40. http://dx.doi.org/10.1042/bj20041853.

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Ferritin, normally considered a cytoplasmic iron-storage protein, is also found in cell nuclei. It is an established fact that H-ferritin is the major form of nuclear ferritin, but little is known about the roles of ferritin in nuclei or about the mechanisms that control its appearance within the nuclear volume. In the present study, we show that, for human SW1088 astrocytoma cells, the nuclear and cytoplasmic forms of H-ferritin are products of the same mRNA. Histochemical and biochemical evidence is presented showing that ferritin is distributed non-randomly within the nuclear volume and tha

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Lucignano, Rosanna, Alessandro Pratesi, Paola Imbimbo, et al. "Evaluation of Auranofin Loading within Ferritin Nanocages." International Journal of Molecular Sciences 23, no. 22 (2022): 14162. http://dx.doi.org/10.3390/ijms232214162.

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Auranofin (AF), a gold(I) compound that is currently used for the treatment of rheumatoid arthritis and is in clinical trials for its promising anticancer activity, was encapsulated within the human H-chain and the horse spleen ferritin nanocages using the alkaline disassembly/reassembly protocol. The aim of the work was to highlight possible differences in their drug loading capacity and efficacy. The drug-loaded ferritins were characterized via UV-vis absorption spectroscopy and inductively coupled plasma-atomic emission spectroscopy to assess AF encapsulation and to define the exact amount

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Salkov, V. N., D. N. Voronkov, and V. S. Sukhorukov. "Quantitative changes in ferritin-containing glia in the structures of the substantia nigra in aging and Parkinson’s disease." CLINICAL AND EXPERIMENTAL MORPHOLOGY 13, no. 2 (2024): 20–25. http://dx.doi.org/10.31088/cem2024.13.2.20-25.

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Introduction. Iron accumulates in the substantia nigra (SN) in aging and Parkinson’s disease (PD). However, there is a distinct lack of information about the changes in the metabolism of ferritin–an iron-binding protein in nigral cells–in aging and PD. The aim of the study was to quantify the changes in the number of H- and L-ferritin glia in the SN structures in aging and PD. Materials and methods. We examined autopsies of PD patients (5 cases), mature and elderly people (6 cases), as well as senile people (5 cases). Immunohistochemistry and light microscopy were used to study the location of

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Levi, S., S. J. Yewdall, P. M. Harrison, et al. "Evidence of H- and L-chains have co-operative roles in the iron-uptake mechanism of human ferritin." Biochemical Journal 288, no. 2 (1992): 591–96. http://dx.doi.org/10.1042/bj2880591.

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The ability to incorporate iron in vitro was studied in homopolymers of human ferritin L-chain, human ferritin H-chain and its variants and in homopolymer mixtures. The H-chain variants carried amino acid substitutions in the ferroxidase centre and/or in carboxy residues on the cavity surface. Iron incorporation was examined by gel electrophoresis of the reaction products by staining for iron and protein. It was found that inactivation of the ferroxidase centre combined with the substitution of four carboxy groups on the cavity abolished the ability of H-chain ferritin to incorporate iron. Com

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de, Turris Valeria, Trabuco Matilde Cardoso, Giovanna Peruzzi, et al. "Humanized archaeal ferritin as a tool for cell targeted delivery." nanoscale 9, no. 2 (2017): 647–55. https://doi.org/10.5281/zenodo.2527178.

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Human ferritins have been extensively studied to be used as nanocarriers for diverse applications and could represent a convenient alternative for targeted delivery of anticancer drugs and imaging agents. However, the most relevant limitation to their applications is the need for highly acidic experimental conditions during the initial steps of particle/cargo assembly, a process that could affect both drug stability and the complete reassembly of the ferritin cage. To overcome this issue the unique assembly of <em>Archaeoglobus fulgidus</em> ferritin was genetically engineered by changing a su

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Moglia, Italo, Margarita Santiago, Simon Guerrero, Mónica Soler, Alvaro Olivera-Nappa, and Marcelo J. Kogan. "Enhanced Cellular Uptake of H-Chain Human Ferritin Containing Gold Nanoparticles." Pharmaceutics 13, no. 11 (2021): 1966. http://dx.doi.org/10.3390/pharmaceutics13111966.

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Gold nanoparticles (AuNP) capped with biocompatible layers have functional optical, chemical, and biological properties as theranostic agents in biomedicine. The ferritin protein containing in situ synthesized AuNPs has been successfully used as an effective and completely biocompatible nanocarrier for AuNPs in human cell lines and animal experiments in vivo. Ferritin can be uptaken by different cell types through receptor-mediated endocytosis. Despite these advantages, few efforts have been made to evaluate the toxicity and cellular internalization of AuNP-containing ferritin nanocages. In th

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Enko, Dietmar, Helga Wagner, Gernot Kriegshäuser, et al. "Iron status determination in individuals with Helicobacter pylori infection: conventional vs. new laboratory biomarkers." Clinical Chemistry and Laboratory Medicine (CCLM) 57, no. 7 (2019): 982–89. http://dx.doi.org/10.1515/cclm-2018-1182.

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Abstract Background Helicobacter pylori has been associated with iron deficiency (ID). This study is aimed at investigating ID with conventional (ferritin, transferrin saturation [TSAT]) and new biomarkers (soluble transferrin receptor [sTfR], sTfR/log ferritin, reticulocyte hemoglobin content [CHr], hepcidin-25) in patients sub-grouped by the presence or absence of H. pylori infection. Methods In total, 200 consecutive outpatients, who were referred for the H. pylori 13C-urea breath test (13C-UBT), underwent blood testing for ID. Additionally, Thomas-plot (TP)-analyses (sTfR/log ferritin, CHr

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Levi, Sonia, Maddalena Ripamonti, Marko Dardi, Anna Cozzi, and Paolo Santambrogio. "Mitochondrial Ferritin: Its Role in Physiological and Pathological Conditions." Cells 10, no. 8 (2021): 1969. http://dx.doi.org/10.3390/cells10081969.

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In 2001, a new type of human ferritin was identified by searching for homologous sequences to H-ferritin in the human genome. After the demonstration that this ferritin is located specifically in the mitochondrion, it was called mitochondrial ferritin. Studies on the properties of this new type of ferritin have been limited by its very high homology with the cytosolic H-ferritin, which is expressed at higher levels in cells. This great similarity made it difficult to obtain specific antibodies against the mitochondrial ferritin devoid of cross-reactivity with cytosolic ferritin. Thus, the know

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LEVI, Sonia, Paolo SANTAMBROGIO, Barbara CORSI, Anna COZZI, and Paolo AROSIO. "Evidence that residues exposed on the three-fold channels have active roles in the mechanism of ferritin iron incorporation." Biochemical Journal 317, no. 2 (1996): 467–73. http://dx.doi.org/10.1042/bj3170467.

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Iron is thought to enter the ferritin cavity via the three-fold channel, which is lined in its narrowest part by the residues Asp-131 and Glu-134. We describe here variants of human ferritins with active and inactive ferroxidase centres having Asp-131 and Glu-134 substituted with Ala and Ala or with Ile and Phe respectively. The two types of substitution had similar effects on ferritin functionality: (i) they decreased the amount of iron incorporated from Fe(II) solutions and decreased ferroxidase activity by about 50%; (ii) they inhibited iron incorporation from Fe(III) citrate in the presenc

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Gray, Christian P., Paolo Arosio, and Peter Hersey. "Heavy chain ferritin activates regulatory T cells by induction of changes in dendritic cells." Blood 99, no. 9 (2002): 3326–34. http://dx.doi.org/10.1182/blood.v99.9.3326.

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Abstract Heavy chain ferritin (H-ferritin) is a component of the iron-binding protein, ferritin. We have previously shown that H-ferritin inhibits anti-CD3–stimulated lymphocyte proliferation and that this was due to increased production of interleukin-10 (IL-10). In the present study we have shown that induction of IL-10 production was due to effects of H-ferritin on adherent antigen-presenting cells (APCs) in blood and monocyte-derived dendritic cells (MoDCs). IL-10 was produced by a subpopulation of CD4 T cells, which expressed the CD25 component of the IL-2 receptor and the CTLA-4 receptor

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Stevens, P. W., J. B. Dodgson, and J. D. Engel. "Structure and expression of the chicken ferritin H-subunit gene." Molecular and Cellular Biology 7, no. 5 (1987): 1751–58. http://dx.doi.org/10.1128/mcb.7.5.1751-1758.1987.

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Although the genomes of many species contain multiple copies of ferritin heavy (H)- and light (L)-chain sequences, the chicken genome contains only a single copy of the H-subunit gene. The primary transcription unit of this gene is 4.6 kilobase pairs and contains four exons which are posttranscriptionally spliced to generate a mature transcript of 869 nucleotides. Chicken and human ferritin H-subunit genomic loci are organized with similar exon-intron boundaries. They exhibit approximately 85% nucleotide identity in coding regions, which yield proteins 93% identical in amino acid sequence. We

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