Relevant bibliographies by topics / H-ferritina

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers

Academic literature on the topic 'H-ferritina'

Author: Grafiati
Published: 9 March 2023
Last updated: 10 March 2023

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Journal articles on the topic "H-ferritina"

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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 (December 15, 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 subunit; it is cleaved during germination. The amino-acid sequence of pea seed ferritin is aligned with those of other ferritins (49% amino-acid identity with H-chains and 40% with L-chains of human liver ferritin in the aligned region). A three-dimensional model has been constructed by fitting the aligned sequence to the coordinates of human H-chains, with appropriate modifications. A folded conformation with an 11-residue helix is predicted for the N-terminal extension. As in mammalian ferritins, 24 subunits assemble into a hollow shell. In pea seed ferritin, its N-terminal extension is exposed on the outside surface of the shell. Within each pea subunit is a ferroxidase centre resembling those of human ferritin H-chains except for a replacement of Glu-62 by His. The channel at the 4-fold-symmetry axes defined by E-helices, is predicted to be hydrophilic in plant ferritins, whereas it is hydrophobic in mammalian ferritins.
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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 (February 1, 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 study showed that inhibitory action of ferritins on immunoglobulin (Ig) production was caused at an early stage of B-cell differentiation. The cytoplasmic Ig-containing cells decreased in proportion to the reduction of Ig secretion. The evidence that ferritin inhibited Ig synthesis of Epstein-Barr virus-transformed human B-lymphoblastoid cell line also supported the idea that the effect of ferritin was directed toward the antibody-producing B lymphocytes. The molecular analysis showed that the inhibitory effect of ferritin was regulated at the transcriptional level of the Ig generation signal. Our results suggest that H- and L-rich ferritins exert their inhibitory action on the differentiation of B cells maturing into Ig-producing cells.
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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 (February 1, 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 showed that inhibitory action of ferritins on immunoglobulin (Ig) production was caused at an early stage of B-cell differentiation. The cytoplasmic Ig-containing cells decreased in proportion to the reduction of Ig secretion. The evidence that ferritin inhibited Ig synthesis of Epstein-Barr virus-transformed human B-lymphoblastoid cell line also supported the idea that the effect of ferritin was directed toward the antibody-producing B lymphocytes. The molecular analysis showed that the inhibitory effect of ferritin was regulated at the transcriptional level of the Ig generation signal. Our results suggest that H- and L-rich ferritins exert their inhibitory action on the differentiation of B cells maturing into Ig-producing cells.
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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, Carole BEAUMONT, C. Maria PANZERI, Anna COZZI, Romina SANGREGORIO, et al. "Transient overexpression of human H- and L-ferritin chains in COS cells." Biochemical Journal 330, no. 1 (February 15, 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 background, with about 40% of the cells being transfected. Thus ferritin concentration in individual cells was increased up to 1000-fold over controls with no evident signs of toxicity. The exogenous ferritin subunits were correctly assembled into homopolymers, but did not affect either the size or the subunit composition of the endogenous heteropolymeric fraction of ferritin, which remained essentially unchanged in the transfected and non-transfected cells. After 18 h of incubation with [59Fe]ferric-nitrilotriacetate, cellular iron incorporation was similar in the transfected and non-transfected cells and most of the protein-bound radioactivity was associated with ferritin heteropolymers, while H- and L-homopolymers remained iron-free. Cell co-transfection with cDNAs for H- and L-chains produced ferritin heteropolymers that also did not increase cellular iron incorporation. It is concluded that transient transfection of COS cells induces a high level of expression of ferritin subunits that do not co-assemble with the endogenous ferritins and have no evident activity in iron incorporation/metabolism.
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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 (August 15, 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 present on cells expressing the proliferation markers HLA-DR, MLR3, interleukin 2 (IL- 2), and transferrin receptors (Tf-R). In addition, after PHA induction, the time course of the expression of H-ferritin binding sites was similar to those of the above proliferation markers. Ferritin binding sites were observed in lymphocytes at all cell cycle phases, including the early S-phase. H-Ferritin at nanomolar and picomolar concentrations had an inhibitory effect on PHA-induced blastogenesis. We propose that H-ferritin binding sites behave like proliferation markers, with the unusual function of downregulating proliferation.
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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 (August 15, 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 cells expressing the proliferation markers HLA-DR, MLR3, interleukin 2 (IL- 2), and transferrin receptors (Tf-R). In addition, after PHA induction, the time course of the expression of H-ferritin binding sites was similar to those of the above proliferation markers. Ferritin binding sites were observed in lymphocytes at all cell cycle phases, including the early S-phase. H-Ferritin at nanomolar and picomolar concentrations had an inhibitory effect on PHA-induced blastogenesis. We propose that H-ferritin binding sites behave like proliferation markers, with the unusual function of downregulating proliferation.
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Bauminger, E. R., A. Treffry, A. J. Hudson, D. Hechel, N. W. Hodson, S. C. Andrews, S. Levi, 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 (September 15, 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 human H-chain ferritin variant with a substituted tyrosine (rHuHF-Y34F) can act as a donor of Fe(III). Since an Fe(III)-tyrosinate (first identified in bullfrog H-chain ferritin) is absent from variant rHuHF-Y34F, the Fe(III) transferred is not derived from this tyrosinate complex. Mössbauer parameters of the small iron cores formed within Ec-FTN are significantly different from those of mammalian ferritins. Analysis of the spectra suggests that they are derived from both ferrihydrite and non-ferrihydrite components. This provides further evidence that the ferritin protein shell can influence the structure of its iron core.
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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 (October 30, 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 structure, function and regulation of ferritins. An update on the animal models that were used to characterize H, L and mitochondrial ferritins is also provided. The data show that ferritin structure is highly conserved among different phyla. It exerts an important cytoprotective function against oxidative damage and plays a role in innate immunity, where it also contributes to prevent parenchymal tissue from the cytotoxicity of pro-inflammatory agonists released by the activation of the immune response activation. Less clear are the properties of the secretory ferritins expressed by insects and molluscs, which may be important for understanding the role played by serum ferritin in mammals.
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Fargion, S., P. Arosio, AL Fracanzani, V. Cislaghi, S. Levi, A. Cozzi, A. Piperno, and G. Fiorelli. "Characteristics and expression of binding sites specific for ferritin H- chain on human cell lines." Blood 71, no. 3 (March 1, 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 exponential phase of growth and progressively decreased to disappear when cells reached the plateau phase. Treatment of the cells with desferrioxamine increased recombinant H-ferritin binding, while iron had little effect. K562 cells induced to differentiate by hemin failed to bind ferritin H. Ferritin H-chain binding capacity is present on various cell lines such as HL60, lung cancer, and hepatoma cells. Analysis of the binding sites by western blotting showed a peptide with apparent mol wt of about 100 kd.
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Dissertations / Theses on the topic "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 particolari pazienti e con il minimo dosaggio. In questa tesi è riportata la sintesi e la validazione di un nuovo tipo di MC a base di manganese: Mn@HFn-RT. Il manganese è un metallo endogeno paramagnetico in grado di produrre un contrasto positivo simile al gadolinio e con una inferiore tossicità per l’uomo. Ioni di manganese sono stati caricati efficacemente all’interno del guscio di una proteina ricombinante chiamata H-ferritina, che si è dimostrato essere riconosciuta dalle cellule che overesprimono il recettore TfR1, come accade nella maggior parte delle cellule tumorali. Mn@HFn-RT è stato caratterizzato, dimostrando un’eccellente stabilità colloidale, un’ottima relassività ed un buon profilo di sicurezza. Da esperimenti condotti in vitro è stato possibile confermare la capacità di Mn@HFn-RT di raggiungere efficacemente le cellule tumorali, e si è inoltre dimostrata la sua abilità di favorire il riconoscimento di masse tumorali in vivo: infatti, Mn@HFn-RT somministrato con un basso dosaggio di metallo, ha dimostrato una ottima clearance ed è stato in grado di far risaltare una massa di tumore al seno impiantato in topo. Per tali motivi, Mn@HFn-RT può essere considerato un promettente MC per la risonanza magnetica.
Magnetic resonance imaging is one of the most sophisticated diagnostic tools in clinic. Contrast agents (CAs) may be exploited to afford much clearer images of detectable organs and to reduce the risk of misdiagnosis, due to the limited sensitivity of the technique. Actually, only a few gadolinium-based CAs are approved for clinical use. Nevertheless, concerns over their toxicity remain and their administration is approved only under strict control. In the present study it is reported the synthesis and validation of a novel manganese-based CA, Mn@HFn-RT. Manganese is an endogenous paramagnetic metal able to produce a positive contrast like gadolinium, however it is estimated to cause lower toxicity for human body. MN ions have been efficiently loaded inside the shell of a recombinant human protein called H-ferritin that is recognized by cells overexpressing TfR1, including the majority of cancer cell. Mn@HFn-RT was characterized, showing excellent colloidal stability, superior relaxivity and good safety profile. From in vitro experiments it was possible to confirm the ability of Mn@HFn-RT to efficiently target cancer cells and thus favor the detection of the tumor region in a breast cancer in vivo model with very low metal dosages and showing rapid clearance. Mn@HFn-RT looks a promising CA candidate to be developed for MRI.
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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 roles respectifs de ces sous-unites dans le metabolisme du fer, nous avons etabli par recombinaison homologue dans les cellules es une lignee de souris deficientes en sous-unite h ferritine (h-ft). L'etude de ces animaux a permis de preciser la fonction biologique de la proteine : le defaut complet en h-ft conduit a une letalite embryonnaire precoce entre le 4 e m e et le 9 e m e jour de developpement. Ce phenotype confirme l'importance biologique de l'activite ferroxydase de la h-ft et l'absence de redondance fonctionnelle de cette activite. A 9,5 jours de developpement, le gene h-ft est transcrit principalement dans le cur et le cerveau. L'expression precoce et tissus-specifique dans ces organes particulierement sensibles au stress oxydatif suggere un role protecteur de la ferritine vis a vis de ce processus. Les souris heterozygotes ont une quantite de h-ft tissulaire diminuee d'un facteur 2 environ mais ne presentent ni surcharge tissulaire en fer ni perturbation physiopathologique. Cette observation confirme in vivo que quelques sous-unites h dans le polymere suffisent a la fonction de la ferritine. La reduction de la h-ft s'accompagne
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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'adn genomique provenant d'un sujet hemochromatosique (l'adn du sujet normal etant etudie en parallele a boston) en phage lambda l147-1. 2. Isolement d'un clone contenant un insert de 12 kb possedant la sequence h-ferritine cible et sous-clonage de la sequence interessante. 3. Sequencage des sous-clones obtenus. 4. Analyse de la sequence h-ferritine chromosome 6 par comparaison avec l'acdn h-ferritine et avec certains retrogenes h-ferritine deja decrits. 5. Etude de deux marqueurs polymorphiques specifiques du locus fthp1. En conclusion, ce travail a permis d'eliminer l'hypothese d'une identite entre le pseudogene h-ferritine caracterise ici et le gene de l'hemochromatose, de preciser genetiquement la localisation du locus fthp1 et d'apporter certains elements en faveur de l'existence d'un deuxieme gene h-ferritine fonctionnel
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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 hybridation in situ, sur trois chromosomes: 3, 6 et 19. En procedant par la liaison genetique dans des croisements interspecifiques de souris, nous avons localise le gene h sur le chromosome 19. Afin d'etudier le role de la sous-unite h, nous avons realise des transfectants stables de cellules mel, surexprimant cette proteine. Nous avons estime le nombre de copies integrees du gene transfecte et les messagers correspondants, par pcr quantitative, la proteine h par western blot et l'accumulation d'hemoglobine, par dosage colorimetrique. Nos resultats suggerent que la sous-unite h facilite la mobilisation du fer pour la synthese de l'heme
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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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Book chapters on the topic "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, 391–402. Boston, MA: 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, Paolo Santambrogio, Anna Cozzi, Barbara Corsi, Elena Tamborini, Stefania Spada, and Ermanna Rovida. "Chemico-Physical and Functional Differences Between H and L Chains of Human Ferritin." In Advances in Experimental Medicine and Biology, 13–21. Boston, MA: 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, 211–18. Boston, MA: 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 a molecular weight of 24 KDa. The recovered product is a ferritin exposing hepcidin on outer surface. The hepcH monomer was characterized by immunoblotting using a monoclonal antibody specific for human ferritin and a polyclonal antibody specific for hepcidin-25. The results were also confirmed by MALDI-TOF mass spectrometry. The recombinant native human ferritin and the commercial human hepcidin-25 were used as controls in this experiment. The assembly of hepcH, as an heteropolymer molecule, was performed in presence of denatured human ferritin-H and -L chains. After cysteine oxidation of the recombinant nanoparticles, cellular binding assays were performed on mammalian cells such as mouse monocyte–macrophage cell line J774, HepG2 and COS7.
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Conference papers on the topic "H-ferritina"

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Mazzucchelli, S., M. Truffi, L. Sorrentino, M. Bellini, R. Ottria, A. Ravelli, P. Ciuffreda, D. Prosperi, and F. Corsi. "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, M. Truffi, MA Rizzuto, L. Sorrentino, E. Longhi, M. Nebuloni, D. Prosperi, and F. Corsi. "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, P. Di Benedetto, AR Lizzi, V. Liakouli, O. Berardicurti, 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, M. Monieri, M. Bellini, E. Longhi, R. Ottria, 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, M. Bellini, MA Rizzuto, R. Ottria, P. Ciuffreda, D. Prosperi, and F. Corsi. "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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7

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. Basel, Switzerland: MDPI, 2015. http://dx.doi.org/10.3390/ecms-1-b002.

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