Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P02794 (ferritin)
 17,525 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Etching techniques to prepare ultra-thin sections for immunoelectron microscopy have incorporated a variety of reagents to expose antigenic sites. In this paper involving 2 techniques for surface etching prior to immunoelectron microscopy, radio frequency glow discharge ( RFGD ) and solid-phase lactoperoxidase-glucose oxidase beads ( Enzymobeads ) are compared to conventional peroxide etching techniques. Measuring such parameters as intensity of granule disposition and titers of antibody resulting in detectable staining. RFGD and Enzymobeads were both superior to the conventional peroxide methodology. Non-specific absorption by ferritin under the conditions utilized was not a problem with Enzymobeads or RFGD method. In addition, RFGD may be useful in situations where peroxide susceptible antigens are under study.
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PMID:Radio frequency glow discharge and solid-phase lactoperoxidase-glucose oxidase beads as methods for etching ultra-thin plastic sections for immunoelectron microscopy. 620 97

Merocyanine 540 (MC540)-mediated photodynamic action is a novel approach for purging tumor cells from autologous remission bone marrow explants. The purpose of this study was to evaluate the effects of hemin (ferriprotoporphyrin IX), a potential source of pro-oxidant iron in bone marrow, on in vitro photodynamic inactivation of leukemia cells. Murine L1210 cells exhibited a progressive loss of clonogenicity when irradiated with broad-band visible light in the presence of MC540. Hemin had strikingly different effects on photokilling, depending on its contact time with cells, eliciting a sizable decrease in resistance after short-term (30-min) contact but a marked increase in resistance after long-term (24-h) contact. Similar trends were observed when cells were challenged with glucose/glucose oxidase, indicating that the responses apply to more than one type of oxidative stress. Immunoblot analyses revealed that the levels of inducible heme oxygenase (HO-1) and ferritin heavy (H) chain were substantially elevated 24 h after hemin addition. HO-1 increased relatively rapidly and maximized within 4 h after adding hemin, whereas H-ferritin increased more slowly in parallel with the development of hyperresistance, maximizing after 24-36 h. Desferrioxamine, an avid iron chelator, had no effect on HO-1 induction but inhibited both ferritin induction and the increase in cell resistance, suggesting that HO-mediated release of iron from hemin was necessary for triggering these responses. Spleen apoferritin was taken up by L1210 cells and strongly inhibited photokilling, further implicating ferritin involvement in hyperresistance. Photokilling was accompanied by free radical-mediated lipid peroxidation (thiobarbituric acid reactivity), which could be suppressed substantially by 24-h hemin preincubation. A plausible explanation for the long-term effects of hemin is that excess H-ferritin generated as a result of iron-regulatory protein deactivation sequesters toxic iron, which might otherwise catalyze damaging lipid peroxidation. Chronic oxidative release of hemin from bone marrow erythroid cells could compromise the efficacy of photopurging by making tumor cells more tolerant to photooxidative insult.
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PMID:Hyperresistance of leukemia cells to photodynamic inactivation after long-term exposure to hemin. 884 Sep 77

Hemin (ferriprotoporphyrin IX), the oxidized prosthetic group of hemoglobin, is a source of potentially cytotoxic iron, but in chronic low doses can induce cytoprotection against iron-stimulated oxidative stress. The latter property of hemin has been examined, using murine L1210 cells and three different oxidant generating systems: (i) glucose/glucose oxidase, (ii) near-ultraviolet irradiation, and (iii) dye-mediated photodynamic action. Cells treated with the lipophilic iron donor ferric-8-hydroxyquinoline, Fe(HQ)2 (1 microM, 30 min) were found to be more sensitive to oxidative killing than nontreated controls. However, cells challenged after long-term (20-24 h) exposure to hemin (10 microM) were substantially more resistant than controls and were sensitized far less by Fe(HQ)2. Immunoblot analyses of 24-h hemin-treated cells indicated that the ferritin heavy (H) subunit was elevated 12- to 15-fold, whereas the light (L) subunit was essentially unchanged. Experiments carried out with 55Fe(HQ)2 showed that iron uptake capacity of cells was greatly enhanced after hemin treatment. More specifically, hemin-stimulated cells were found to contain approximately 9 times more immunoprecipitable ferritin iron after incubation with saturating levels (4-5 microM) of 55Fe(HQ)2 and approximately 3 times more iron per ferritin molecule compared with nonstimulated controls. The nonferritin iron content of the latter was estimated to be approximately 40 times greater than that of the former following low-level (0.5 microM) 55Fe(HQ)2 treatment. These results are consistent with the idea that induced ferritin, enriched in H-chain, sequesters redox active iron rapidly and copiously, thereby enhancing cellular resistance to oxidants.
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PMID:Elevated ferritin production, iron containment, and oxidant resistance in hemin-treated leukemia cells. 932 93

Human HL-60 cells exhibited a strong hyperresistance to the lethal effects of photodynamic activity (singlet oxygen) or glucose oxidase activity (hydrogen peroxide) 16-20 h after being exposed to hemin (ferriprotoporphyrin IX). Hyperresistance was accompanied by the overproduction of immunodetectable ferritin, predominantly the heavy (H) subunit, which exhibits ferroxidase activity. Cells that had been enriched in apoferritin via pinocytotic uptake showed similar hyperresistance to both types of oxidative challenge. On the other hand, preincubating cells with hemin in the presence of a phosphorothioate-linked antisense oligodeoxynucleotide against H-ferritin mRNA resulted in a strong diminution in both hyperresistance and H-ferritin induction. No effects were seen when a scrambled order oligodeoxynucleotide of the same base composition was used, confirming that the antisense oligomer had specifically inhibited H-ferritin translation. These results indicate that induced ferritin played a crucial role in the observed cytological responses. Enhanced oxidant resistance is attributed to the ability of this ferritin to rapidly sequester and incapacitate redox-active iron.
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PMID:Hemin-enhanced resistance of human leukemia cells to oxidative killing: antisense determination of ferritin involvement. 952 13

Hemin (ferriprotoporphyrin IX), the oxidized prosthetic group of hemoglobin, is a potential source of prooxidant iron in heavily vascularized tumors. We have evaluated hemin's effects on photodynamic inactivation of bovine artery endothelial cells, using a partially purified oligomeric fraction of hematoporphyrin derivative (HPD-A) as the sensitizing agent. Confluent cells in 5% serum/RPMI medium showed a progressive loss of thiazolyl blue (MTT)-detectable viability when irradiated with broadband visible light in the presence of HPD-A. Cells pretreated with desferrioxamine (DFO) were substantially less sensitive to photokilling, implying that non-heme iron plays a role in cytotoxic activity. Hemin (10-20 microM) had remarkably different effects on photokilling, depending on the time interval between adding it to cells and exposing them to photodynamic action. For example, cells were more sensitive when photostressed immediately after 1 h hemin treatment and washing but much more resistant when photostressed 23 h later. Similar responses were observed when cells were challenged with glucose oxidase. Immunoblot analysis following hemin treatment revealed a progressive induction of the heavy (H) subunit of ferritin that paralleled the development of hyperresistance. After incubation with saturating levels of the synthetic iron donor [55Fe]ferric-8-hydroxyquinoline, hemin-stimulated cells contained about four times more immunoprecipitable ferritin 55Fe than controls. This is consistent with the notion that sequestration of toxic iron as a result of induction of H-chain-enriched ferritin is a key factor in hyperresistance. Inflammatory injury in tumor vasculatures could expose endothelial and neoplastic cells to chronic hemoglobin-derived iron. Consequent upregulation of ferritin could impact negatively on the efficacy of photodynamic therapy and other oxidant-based cancer therapies.
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PMID:Delayed hyperresistance of endothelial cells to photodynamic inactivation after contact with hemin. 972 13

Chronic granulomatous disease (CGD) is an inherited primary immunodeficiency characterized by phagocytes devoid of a functioning nicotinamide adenine dinucleotide phosphate (NADPH) oxidase. The failure of CGD phagocytes to produce reactive oxygen species (ROS) results in a marked increase in the susceptibility of affected patients to life-threatening bacterial and fungal infections. This study investigated whether loading of CGD phagocytes with glucose oxidase (GO)-containing liposomes (GOLs) could restore cellular production of bactericidal ROS (eg, H2O2 and HOCl) in vitro. Results indicate that GO encapsulated in liposomes enabled NADPH oxidase-deficient phagocytes to use H2O2 for the production of highly bactericidal HOCl. The intracellular colocalization of bacteria and liposomes (or liposome-derived ferritin) was demonstrated by confocal laser microscopy and electron microscopy. After uptake of GOLs (approximately 0.2 U/mL at 1 mM total lipid concentration, size approximately 180 nm), CGD granulocytes produced HOCl levels comparable to those of normal phagocytes. Remarkably, after treatment with GOLs, CGD phagocytes killed Staphylococcus aureus as efficiently as normal granulocytes. Moreover, treated cells retained sufficient motility toward chemotactic stimuli as measured by chemotaxis assay. Side effects were evaluated by measuring the H2O2 concentrations and the production of methemoglobin in whole blood. These studies revealed that H2O2 produced by GOLs was degraded immediately by the antioxidative capacity of whole blood. Elevated methemoglobin levels were observed only after application of extremely high amounts of GOLs (2 U/mL). In summary, the application of negatively charged GOLs might provide a novel effective approach in the treatment of patients with CGD at high risk for life-threatening infections.
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PMID:Reconstitution of bactericidal activity in chronic granulomatous disease cells by glucose-oxidase-containing liposomes. 1169 96

The cardiotoxicity induced by the anticancer anthracycline doxorubicin (DOX) is attributed to reactions between iron and reactive oxygen species (ROS) that lead to oxidative damage. We found that DOX forms ROS in H9c2 cardiomyocytes, as shown by dichlorodihydrofluorescein oxidation and the expression of stress-responsive genes such as catalase or aldose reductase. DOX also increased ferritin levels in these cells, particularly the H subunit. A considerable increase in ferritin mRNA levels showed that DOX acted at transcriptional level, but an additional potential mechanism was identified as the down-regulation of iron regulatory protein-2, post-transcriptional inhibitor of ferritin synthesis. Pretreatment with DOX protected H9c2 cells against the damage induced by subsequent exposure to ferric ammonium citrate, and experiments with (55)Fe revealed that the protection was due to the deposition of iron in ferritin. Cytoprotection was also observed when DOX was replaced by glucose/glucose oxidase, a source of H(2)O(2), thus suggesting that DOX increases ferritin synthesis through the action of ROS. This concept was supported by three more lines of evidence. (i) DOX-induced ferritin synthesis was blocked by N-acetylcysteine, a scavenger of ROS. (ii) Mitoxantrone, a ROS-forming analogue, similarly induced ferritin expression and protected the cells against iron toxicity. (iii) 5-Iminodaunorubicin, an analogue lacking ROS-forming activity, did not induce ferritin synthesis or protect the cells against iron toxicity. These results characterize a paradoxically beneficial link between anthracycline-derived ROS, increased ferritin synthesis, and resistance to iron-mediated damage. The role of iron and ROS in anthracycline-induced cardiotoxicity may, therefore, be more complex than previously believed.
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PMID:Doxorubicin paradoxically protects cardiomyocytes against iron-mediated toxicity: role of reactive oxygen species and ferritin. 1473 95

Gold nanowire array has been proven to be efficient support matrixes for the immobilization of hemoglobin (Hb). The vertically oriented nanowire array provides an ordered well-defined 3D structure with nanowire density approximately 5 x 10(8)cm(2). The adsorption of ferritin onto the nanowire surface was visualized by transmission electron microscopy. When Hb was adsorbed, UV-vis absorption and Fourier transform infrared (FT-IR) spectra show no obvious denaturation of Hb in the nanowire array. The Hb-modified nanowire array exerted direct electron transfer and gave a well-defined, nearly reversible redox couple with formal potential of -0.225 V. The quantity of electroactive Hb varied with the changing of the morphology of the electrode and found to increase with the increasing of the nanowire length. Comparisons of voltammetric and quartz crystal microbalance measurements show that 70% of the Hb molecules adsorbed are electroactive when the length of the nanowire was 2 microm. Both of the Hb-modified nanowire array and the unmodified nanowire array demonstrate good electrocatalytic reduction ability for hydrogen peroxide. With the adsorption of glucose oxidase onto the bare nanowire surface, sensitive and selective glucose biosensors can be fabricated.
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PMID:Direct electrochemistry of hemoglobin in gold nanowire array. 1758 54

Studies in humans and animals have suggested negative interactions of iron and zinc during their intestinal absorption. Further, zinc seems to prevent iron-induced oxidative damage in rats, which was hypothesized to be through the modulation of the intracellular iron signaling pathway. The aim of this study was, therefore, to understand the effects of zinc on oxidant-induced iron signaling and cell death in human enterocyte-like Caco-2 cells. We demonstrate that zinc decreases glucose/glucose oxidase (H(2)O(2)-generating system)-induced iron uptake and inhibits iron-regulatory protein 1 activation and divalent metal ion transporter 1 expression. There was also a concomitant decrease in oxidant-induced intracellular labile iron and restoration of ferritin and metallothionein expression. Further, zinc enhanced the Bcl-2/Bax ratio and reduced caspase-3 activity, leading to inhibition of apoptosis. Interestingly, bathophenanthroline disulfonic acid, an extracellular iron chelator, emulated the effects of zinc except for the reduced ferritin levels. These results suggest that zinc inhibits apoptosis by reducing oxidant-induced iron signaling in Caco-2 cells.
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PMID:Zinc inhibits oxidative stress-induced iron signaling and apoptosis in Caco-2 cells. 2009 49

Herein, we report a novel glucose oxidase (GOD)-doped magnetic silica nanostructure and its possible application in the clinical immunoassays. The doped nanostructures were initially synthesized using the reverse micelle method, and ferritin antibodies (anti-Ft) were then labeled to the surface of the nanostructures, which were employed as signal antibodies for ultrasensitive detection of ferritin (Ft) in the sandwich-type electrochemical enzyme immunoassays. The doped nanostructures were characterized using transmission electron microscopy (TEM), UV-vis absorption spectrometry and vibrating sample magnetometer (VSM). The advantages of the doped nanostructures as labels were investigated in comparison with the conventional label method. Under the optimal conditions, the nanostructures-based immunoassay toward ferritin standards displays a wide dynamic range from 0.1 to 400 ng mL(-1) with a low detection limit of 10 pg mL(-1) ferritin (at 3sigma), which is three-fold higher in the sensitivity than that of directly using GOD-labeled antibodies. The assay results for clinical serum samples with the developed method received in excellent accordance with results obtained from the referenced standard enzyme-linked immunosorbent assay (ELISA) method.
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PMID:Glucose oxidase-doped magnetic silica nanostrutures as labels for localized signal amplification of electrochemical immunosensors. 2064 57


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