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Journal articles on the topic 'H-ferritina'

Author: Grafiati

Published: 9 March 2023

Last updated: 31 July 2025

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1

Chuliber, Fernando, Roxana Vanden Ryn, Marina Sol López, et al. "Dímero D y Ferritina, al ingreso Hospitalario, se asociaron a signos de alarma en Dengue y al desarrollo de neumonía en COVID-19. Escenario de doble circulación viral." Revista Bioquímica y Patología Clínica 86, no. 2 (2022): 23–29. http://dx.doi.org/10.62073/bypc.v86i2.196.

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Introducción: COVID-19 y dengue comparten síntomas iniciales (fiebre, cefalea) que desafian el diagnóstico en escenarios de doble circulación viral. Objetivo: Evaluar biomarcadores como ferritina y dímero D (DD), al ingreso hospitalario, y su asociación con la evolución clínica de los pacientes. Métodos: Se realizó un estudio retrospectivo de una cohorte de pacientes adultos consecutivos que consultaron por síntomas compatibles con COVID-19 (marzo-junio 2020). Fueron incluidos los pacientes con dengue o COVID-19. El laboratorio al ingreso consistió en: dímero D (DD) (VIDAS); proteína C reactiv

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2

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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3

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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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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6

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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10

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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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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12

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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13

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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14

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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15

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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and L Monteiro Rodrigues, eds, Catarina Rosado. "Proceedings - CBIOS Science Sessions 2020." Biomedical and Biopharmaceutical Research Journal 17, no. 2 (2020): 1–7. http://dx.doi.org/10.19277/bbr.17.2.245.

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Science Sessions 2020 Catarina Rosado and L Monteiro Rodrigues, eds. Vinicius Cuña, Universidade Lusófona de Humanidades e Tecnologias `````````````````````````````````` p.2 Oxygen Ozone Therapy - Tool in Veterinary Medicine Oxigênio Ozônio Terapia - Ferramenta na Medicina Veterinária Elisabete Silva, Faculdade de Ciências da Universidade de Lisboa p.2 Eco-friendly mon-biocide-releasing antifouling coatings for biofouling prevention Revestimentos antivegetativos monocidas amigos do ambiente para a prevenção de biofouling Amélia Pilar Rauter, Centro de Química Estrutural, Faculdade de Ciências;

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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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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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Kwon, Mun-Gyeong, Ji-Min Jeong, Ju-Won Kim, and Chan-Il Park. "Molecular cloning and expression analysis of a ferritin H subunit from rock bream, Oplegnathus fasciatus." Journal of fish pathology 26, no. 3 (2013): 295–301. http://dx.doi.org/10.7847/jfp.2013.26.3.295.

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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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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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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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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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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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Massover, William H., Sonia Levi, Alessandra Luzzago, Paola Tateo, and Paolo Arosio. "Ultrastructure of Two Mutants in the H-Subunit of Recombinant Human Ferritin: Ordered Arrays Indicate Altered Surface Properties." Proceedings, annual meeting, Electron Microscopy Society of America 48, no. 1 (1990): 288–89. http://dx.doi.org/10.1017/s0424820100180197.

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Two major types of polypeptide subunits, H and L, coassemble (n = 24) as heteropolymers to form molecules of the iron-storage protein, ferritin [1]. The significance of the H-type subunits for molecular structure and function remains unclear. The present study has examined the ultrastructure of recombinant human ferritins which are homopolymers of wild-type or mutant H-subunits [2]. Both mutations change the aminoacid sequence along the outer surface of the molecule; 9Cd has a single substitution of glycine for the lysine at position 86, and Ml has a duplication of 18 aminoacids [2].Recombinan

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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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Collawn, James F., Henry Donato, and Wayne W. Fish. "Evidence that H-enriched human placental ferritin is structurally similar to L-enriched ferritins of other tissues." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 871, no. 3 (1986): 235–42. http://dx.doi.org/10.1016/0167-4838(86)90204-9.

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Scindia, Yogesh, Ewa Wlazlo, Elizabeth Ghias, et al. "Therapeutic Benefit of Regulating Iron Metabolism in Spontaneous Lupus Nephritis." Journal of Immunology 204, no. 1_Supplement (2020): 236.7. http://dx.doi.org/10.4049/jimmunol.204.supp.236.7.

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Abstract Background Lupus nephritis (LN) is an end-organ complication of Systemic lupus erythematosus and is more common in premenopausal women. Hepcidin, the master regulator of iron homeostasis, modulates inflammation and is negatively regulated by estrogen. Therefore, we hypothesized that exogenous hepcidin may reduce the severity and delay the onset of LN. Methods Pre-nephritic 8-week-old or nephritic 16-week-old MRL/lpr female mice were injected Hepcidin (50ug, i.p) or vehicle twice a week and markers of renal injury and inflammation were examined at 18 and 20 weeks of age. The direct eff

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Waidner, Barbara, Stefan Greiner, Stefan Odenbreit, et al. "Essential Role of Ferritin Pfr in Helicobacter pylori Iron Metabolism and Gastric Colonization." Infection and Immunity 70, no. 7 (2002): 3923–29. http://dx.doi.org/10.1128/iai.70.7.3923-3929.2002.

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ABSTRACT The reactivity of the essential element iron necessitates a concerted expression of ferritins, which mediate iron storage in a nonreactive state. Here we have further established the role of the Helicobacter pylori ferritin Pfr in iron metabolism and gastric colonization. Iron stored in Pfr enabled H. pylori to multiply under severe iron starvation and protected the bacteria from acid-amplified iron toxicity, as inactivation of the pfr gene restricted growth of H. pylori under these conditions. The lowered total iron content in the pfr mutant, which is probably caused by decreased iro

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SANTAMBROGIO, Paolo, Sonia LEVI, Anna COZZI, Barbara CORSI, and Paolo AROSIO. "Evidence that the specificity of iron incorporation into homopolymers of human ferritin L- and H-chains is conferred by the nucleation and ferroxidase centres." Biochemical Journal 314, no. 1 (1996): 139–44. http://dx.doi.org/10.1042/bj3140139.

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Mammalian ferritins are iron-storage proteins made of 24 subunits of two types: the H- and L-chains. L-chains, in contrast with H-chains, lack detectable ferroxidase activity. When ferritins were subjected to iron loading in vitro with increments near the saturation limit of 4000 Fe atoms per molecule, the homopolymers of human H-chains formed insoluble aggregates, caused by non-specific iron hydrolysis, whereas the homopolymers of L-chains remained soluble and incorporated most of the available iron. To analyse the molecular reasons for the difference, Glu-57 and Glu-60, which are conserved a

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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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Levi, Sonia, Domenico Girelli, Federica Perrone, et al. "Analysis of Ferritins in Lymphoblastoid Cell Lines and in the Lens of Subjects With Hereditary Hyperferritinemia-Cataract Syndrome." Blood 91, no. 11 (1998): 4180–87. http://dx.doi.org/10.1182/blood.v91.11.4180.

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Abstract Hereditary hyperferritinemia-cataract syndrome (HHCS) is an autosomal and dominant disease caused by heterogeneous mutations in the iron responsive element (IRE) of the 5′ untranslated flanking region of ferritin L-chain mRNA, which reduce the binding to the trans iron regulatory proteins and make L-chain synthesis constitutively upregulated. In the several families identified so far, the serum and tissue L-ferritin levels are fivefold to 20-fold higher than in nonaffected control subjects, iron metabolism is apparently normal, and the only relevant clinical symptom is early onset, bi

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Levi, Sonia, Domenico Girelli, Federica Perrone, et al. "Analysis of Ferritins in Lymphoblastoid Cell Lines and in the Lens of Subjects With Hereditary Hyperferritinemia-Cataract Syndrome." Blood 91, no. 11 (1998): 4180–87. http://dx.doi.org/10.1182/blood.v91.11.4180.411k38_4180_4187.

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Hereditary hyperferritinemia-cataract syndrome (HHCS) is an autosomal and dominant disease caused by heterogeneous mutations in the iron responsive element (IRE) of the 5′ untranslated flanking region of ferritin L-chain mRNA, which reduce the binding to the trans iron regulatory proteins and make L-chain synthesis constitutively upregulated. In the several families identified so far, the serum and tissue L-ferritin levels are fivefold to 20-fold higher than in nonaffected control subjects, iron metabolism is apparently normal, and the only relevant clinical symptom is early onset, bilateral c

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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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Langlois, Michel R., Marie-Elise Martin, Johan R. Boelaert, et al. "The Haptoglobin 2-2 Phenotype Affects Serum Markers of Iron Status in Healthy Males." Clinical Chemistry 46, no. 10 (2000): 1619–25. http://dx.doi.org/10.1093/clinchem/46.10.1619.

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Abstract Background: Human iron status is influenced by environmental and genetic factors. We hypothesized that the genetic polymorphism of haptoglobin (Hp), a hemoglobin-binding plasma protein, could affect iron status. Methods: Reference values of serum iron status markers were compared according to Hp phenotypes (Hp 1-1, Hp 2-1, Hp 2-2; determined by starch gel electrophoresis) in 717 healthy adults. Iron storage was investigated in peripheral blood monocyte-macrophages by measuring cytosolic L- and H-ferritins and by in vitro uptake of radiolabeled (125I) hemoglobin-haptoglobin complexes.

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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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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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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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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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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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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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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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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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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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Bradley, Justin M., Dimitri A. Svistunenko, Jacob Pullin, et al. "Reaction of O2with a diiron protein generates a mixed-valent Fe2+/Fe3+center and peroxide." Proceedings of the National Academy of Sciences 116, no. 6 (2019): 2058–67. http://dx.doi.org/10.1073/pnas.1809913116.

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The gene encoding the cyanobacterial ferritinSynFtn is up-regulated in response to copper stress. Here, we show that, whileSynFtn does not interact directly with copper, it is highly unusual in several ways. First, its catalytic diiron ferroxidase center is unlike those of all other characterized prokaryotic ferritins and instead resembles an animal H-chain ferritin center. Second, as demonstrated by kinetic, spectroscopic, and high-resolution X-ray crystallographic data, reaction of O2with the di-Fe2+center results in a direct, one-electron oxidation to a mixed-valent Fe2+/Fe3+form. Iron–O2ch

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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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