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Littérature scientifique sur le sujet « H-ferritina »

Auteur : Grafiati
Publié le 9 mars 2023
Mis à jour le 31 juillet 2025

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Articles de revues sur le sujet "H-ferritina"

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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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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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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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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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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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Thèses sur le sujet "H-ferritina"

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TULLIO, CHIARA. "Development of an effective tumor-targeted contrast agent for magnetic resonance imaging based on Mn/H-ferritin nanocomplexes." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2021. http://hdl.handle.net/10281/307662.

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La risonanza magnetica per immagini è una delle tecniche diagnostiche più sofisticate attualmente utilizzate in clinica. I mezzi di contrasto di contrasto (MC) possono essere somministrati per ottenere una migliore risoluzione delle immagini dei tessuti detectabili, nonché per ridurre il rischio di diagnosi errate causate dalla limitata sensitività di questa tecnica. Attualmente, soltanto alcuni MC a base di gadolinio sono approvati per un utilizzo in ambito clinico. Tuttavia, a causa di alcune problematiche legate alla loro tossicità, la loro somministrazione è consentita soltanto in particol
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DUGAST, ISABELLE. "Genetique moleculaire de l'hemochromatose idiopathique : etude du gene ferritine h du chromosome 6." Rennes 1, 1988. http://www.theses.fr/1988REN10062.

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Recherche d'une forme nouvelle de ferritine, attribuee au chromosome 6, dans la region du locus hi, marquee par les haplotypes hla. Mise en evidence d'un gene de grande taille dont les coupures enzymatiques suggerent la presence possible d'introns. Ce clone permet de decrire un polymorphisme possible du gene ferritine h sur le chromosome 6
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FERREIRA, CHRYSTOPHE. "Etablissement et caracterisation d'un modele de souris deficientes en sous-unite h ferritine." Paris 7, 2000. http://www.theses.fr/2000PA077078.

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La ferritine est une proteine ubiquitaire qui joue un role majeur dans le stockage, la biodisponibilite et la detoxication du fer intracellulaire. Chez les mammiferes, la ferritine est un heteropolymere compose de 2 types de sous-unites, h et l, formant une coque proteique dans laquelle le fer est stocke sous une forme cristalline. Des etudes in vitro sur des proteines recombinantes indiquent que la sous-unite h a une activite ferroxydase permettant une incorporation rapide du metal dans le polymere alors que la sous-unite l catalyse la nucleation du cur ferrique. Afin de preciser in vivo les
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Offermann, Stefanie. ""Shotgun-Kristallisation"- Strukturaufklärung eines Ferritins und einer Glyzerin-Dehydrogenase aus dem Archaeon H. salinarum." Diss., lmu, 2003. http://nbn-resolving.de/urn:nbn:de:bvb:19-9349.

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MAUVIEUX-LELAURE, VALERIE. "Pseudogene h-ferritine du chromosome 6 (locus fthp1) : sequence, localisation, description de deux marqueurs polymorphiques." Rennes 1, 1991. http://www.theses.fr/1991REN10122.

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L'hemochromatose est une maladie hereditaire a transmission autosomique recessive caracterisee par une surcharge tissulaire en fer. L'anomalie genomique en cause a ete localisee sur le bras court du chromosome 6 a moins d'un centimorgan du locus hla-a. La mise en evidence dans cette meme region d'une sequence h-ferritine (la feritine etant une proteine majeure du metabolisme du fer) a constitue le point de depart de notre sujet de recherche. Afin d'isoler et d'etudier cette sequence h-ferritine du chromosome 6, differentes etapes ont ete menees a bien: 1) realisation d'une banque partielle d'a
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YACHOU, ABDELKADER. "Caracterisation de la famille multigenique h ferritine de souris et etude du role de la sous-unite h dans la synthese de l'heme." Paris 7, 1992. http://www.theses.fr/1992PA077298.

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La ferritine, proteine de stockage de fer, est constituee de 24 sous-unites qui sont de deux types h et l. Ces sous-unites sont codees par deux familles multigeniques distinctes. Il a ete suggere qu'un deuxieme gene h existe et serait responsable de l'hemochromatose idiopathique. Le nombre de sequences h est plus reduit dans le genome de souris que dans celui de l'homme. Nous avons crible une banque genomique de souris a l'aide d'une sonde adnc h de souris. Nous avons isole cinq groupes de clones, trois pseudogenes et deux formes allelique d'un seul gene, que nous avons localise, par hybridati
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Sakamoto, Souichiro. "H-Ferritin Is Preferentially Incorporated by Human Erythroid Cells through Transferrin Receptor 1 in a Threshold-Dependent Manner." Kyoto University, 2016. http://hdl.handle.net/2433/215433.

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Koorts, Alida Maria. "Expression of the H-subunit and L-subunit of ferritin in bone marrow macrophages and cells of the erythron during chronic immune stimulation." Thesis, Pretoria : [s.n.], 2009. http://upetd.up.ac.za/thesis/available/etd-03122010-195432/.

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Briand-David, Véronique. "Génétique moléculaire de l'hémochromatose idiopathique approche par le polymorphisme de restriction des gènes des sous-unités H de la ferritine, et des gènes HLA classe 1 /." Grenoble 2 : ANRT, 1988. http://catalogue.bnf.fr/ark:/12148/cb37612408x.

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Briand-David, Véronique. "Genetique moleculaire de l'hemochromatose idiopathique : approche par le polymorphisme de restriction des genes des sous-unites h de la ferritine, et des genes hla de classe i." Rennes 1, 1988. http://www.theses.fr/1988REN10110.

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Chapitres de livres sur le sujet "H-ferritina"

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Marziali, Giovanna, Edvige Perrotti, Ramona Ilari, Eliana M. Coccia, Ugo Testa, and Angela Battistini. "Transcriptional Regulation of the Ferritin H-Chain and Transferrin Receptor in Hematopoietic Cells." In Molecular Biology of Hematopoiesis 6. Springer US, 1999. http://dx.doi.org/10.1007/978-1-4615-4797-6_48.

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Arosio, Paolo, Alberto Albertini, Sonia Levi, et al. "Chemico-Physical and Functional Differences Between H and L Chains of Human Ferritin." In Advances in Experimental Medicine and Biology. Springer US, 1994. http://dx.doi.org/10.1007/978-1-4615-2554-7_2.

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Beaumont, Carole, Richard Jones, Attila Seyhan, and Bernard Grandchamp. "A Hemin-Inducible Enhancer Lies 4.5 Kb Upstream of the Mouse Ferritin H Subunit Gene." In Advances in Experimental Medicine and Biology. Springer US, 1994. http://dx.doi.org/10.1007/978-1-4615-2554-7_23.

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Boumaiza, Mohamed, Samia Rourou, Paolo Arosio, and Mohamed Nejib Marzouki. "The Use of Ferritin as a Carrier of Peptides and Its Application for Hepcidin." In BioMechanics and Functional Tissue Engineering [Working Title]. IntechOpen, 2020. http://dx.doi.org/10.5772/intechopen.94408.

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Hepcidin a 25-amino-acid and highly disulfide bonded hormone, is the central regulator of iron homeostasis. In this chapter we propose ferritin as a peptide carrier to promote the association of the hybrid hepcidin/ferritin nanoparticle with a particular cell or tissue for therapeutic or diagnostic use. Indeed, human ferritin H-chain fused directly (on its 5’end) with camel mature hepcidin was cloned into the pASK-43 plus vector and expressed using BL21 (DE3) pLys E. coli strain. The transformed E.coli produced efficiently hepcidin-ferritin construct (hepcH), consisting of 213 amino acids with
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Kato, Junji, Koshi Fujikawa, and Yoshiro Niitsu. "Ferritin." In Experimental protocols for reactive oxygen and nitrogen species. Oxford University PressOxford, 2000. http://dx.doi.org/10.1093/oso/9780198506683.003.0033.

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Abstract Iron is essential for life and is involved in various physiological functions such as respiration, electron transport, and cell proliferation. Conversely, iron overload, especially free iron, causes cell damage by production of free radicals, oxidation of lipids, and DNA fragmentation. For these reasons, intracellular iron is strictly regulated. Part of that regulation is provided by ferritin, an iron-storage protein that consists of twenty-four L and H subunits. Each molecule of ferritin stores approx. 4500 atoms of iron and thus indirectly regulates free-radical production. Here we
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Actes de conférences sur le sujet "H-ferritina"

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Mazzucchelli, S., M. Truffi, L. Sorrentino, et al. "Olaparib Nanoformulation in H-Ferritin for the Triple Negative Breast Cancer Treatment." In The 3rd World Congress on Recent Advances in Nanotechnology. Avestia Publishing, 2018. http://dx.doi.org/10.11159/nddte18.116.

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Liu, Xiaoli, A. b. Madhankumar, Becky Slagle-Webb, Jonas M. Sheehan, Nodar Surguladze, and James R. Connor. "Abstract 5529: Silencing H-ferritin by siRNA delivered by cationic liposomes increases chemotherapeutic sensitivity for treating malignant tumor." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-5529.

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Mazzucchelli, S., L. Fiandra, M. Bellini, et al. "Abstract P6-12-17: H-ferritin allows nanometronomic treatment of breast cancer with doxorubicin preventing drug resistance and circumventing cardiotoxicity." In Abstracts: Thirty-Ninth Annual CTRC-AACR San Antonio Breast Cancer Symposium; December 6-10, 2016; San Antonio, Texas. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.sabcs16-p6-12-17.

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Ruscitti, P., P. Cipriani, F. Ciccia, et al. "FRI0613 H-ferritin and pro-inflammatory cytokines are increased in the bone marrow of adult patients affected by macrophage activation syndrome." In Annual European Congress of Rheumatology, 14–17 June, 2017. BMJ Publishing Group Ltd and European League Against Rheumatism, 2017. http://dx.doi.org/10.1136/annrheumdis-2017-eular.5420.

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Mazzucchelli, S., F. Andreata, A. Bonizzi, et al. "Abstract P1-20-04: Nanoformulation of doxorubicin inside H- ferritin nanocages allows a cardio-safe combined therapy with trastuzumab: De-escalating cardiotoxicity in HER2-positive breast cancer." In Abstracts: 2018 San Antonio Breast Cancer Symposium; December 4-8, 2018; San Antonio, Texas. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-p1-20-04.

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Mazzucchelli, S., M. Truffi, L. Sorrentino, et al. "Abstract P1-10-13: Olaparib nanoformulation in H-ferritin as a promising option for both BRCA-mutated and sporadic triple negative breast cancer: An in vitro study." In Abstracts: 2017 San Antonio Breast Cancer Symposium; December 5-9, 2017; San Antonio, Texas. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.sabcs17-p1-10-13.

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Greenwood, Michael, Rawan Eid, Nagla Arab, Chamel Khoury, and Paul Young. "Expression of human H ferritin prompts the identification of a hitherto elusive yeast orthologue and enables parsing of distinct iron-induced cell death pathways in Saccharomyces cerevisiae." In 1st Electronic Conference on Molecular Science. MDPI, 2015. http://dx.doi.org/10.3390/ecms-1-b002.

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