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Query: UNIPROT:P02794 (ferritin)
 17,525 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In order to identify the function and location of phosphate associated with the iron core of horse spleen ferritin (HoSF), the phosphate content of native HoSF was altered by two procedures. Adjustment of pH from 7.0 to 10.0 irreversibly released 53% of the phosphate and 10% of the iron, while lowering the pH to 5.0 reversibly released 43% of the phosphate and 35% of the iron. Reversible release of 85% of the initial phosphate (but little iron release) also occurs upon reduction with methyl viologen (MV) or dithionite. Most of the phosphate is released in the early stages of reduction of the iron core, suggesting that the phosphate resides primarily on the mineral core surface. Reduction followed by chelation altered both the iron and phosphate content of the HoSF mineral cores. HoSF iron cores first reconstituted in the absence of phosphate and then incubated with added phosphate did not bind phosphate. However, when HoSF was first reconstituted in the absence of phosphate and then equilibrated anaerobically with both Fe2+ and phosphate, then phosphate was incorporated in amounts similar to native HoSF. Fe2+ binding to native, phosphate altered, and reconstituted HoSF in the presence and absence of phosphate clearly showed that Fe2+ binding to the mineral core depends on the presence of core-bound phosphate. Fe2+ binding to phosphate-depleted mineral cores or to cores reconstituted with 621, 2158, and 3013 Fe/HoSF core in the absence of phosphate bound only eight Fe2+ per entire ferritin molecule, clearly showing that Fe2+ has no measurable affinity for the phosphate-free, reconstituted mineral core.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Role of phosphate in Fe2+ binding to horse spleen holoferritin. 843 49

A study was performed to elucidate the mechanisms of charge-based immune complex nephritis. A chronological observation after induction of nephritis was made by immunoelectron microscopy to clarify whether antigen (Ag) remains in association with antibody (Ab) and C3 during the translocation through the glomerular basement membrane (GBM). Fifteen minutes after intrarenal perfusion with cationized ferritin (pI > 10.0) as Ag, followed by injection of rabbit anti-ferritin Ab, deposition of subendothelial Ag-Ab-C3 complexes was observed. Between 2 hours and 1 day, a large number of Ag in close association with Ab was noted in the lamina densa, but only a small amount of C3 was detectable. During this time Ag and Ab in the subendothelial region gradually decreased. However, C3 reappeared in the subepithelial region together with the Ag-Ab complex after 1 day, and the subendothelial C3 significantly decreased. At 2 hours and day 1, the distributions of Ag and Ab in the GBM were similar in immersion-fixed kidneys regardless of the preperfusion with phosphate-buffered saline. On the other hand, the passage of Ag across the lamina densa was delayed in the experimental rats as compared with the controls. Significant albuminuria also appeared on day 1. Despite the general concept that Ab binding to cationized Ag results in low avidity immune complex, cationized Ag translocated across the GBM in close association with Ab. The complement was activated biphasically in the subendothelial and in the subepithelial space. The subendothelial complement activation may have contributed to the translocation of immune complex.
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PMID:Intraglomerular basement membrane translocation of immune complex (IC) in the development of passive in situ IC nephritis of rats. 845 43

The core of mammalian ferritin is known to contain varying amounts of phosphate as well as iron. This study examined the variations in phosphate found in ferritins from horse spleen, rat liver, and bovine liver. The amount of phosphate varied inversely with the amount of iron present in the core. Theoretical extrapolation showed that in the absence of phosphate approximately 4400 atoms of iron could be incorporated into ferritin. Reconstitution of ferritin with iron and ceruloplasmin followed by prolonged incubation with phosphate produced cores similar to native ferritin in terms of iron to phosphate ratios and rates of iron release. However, ferritin reconstituted in the presence of phosphate differed markedly from native ferritins. The data suggest that phosphate is an integral part of mammalian ferritin cores and influences both core formation and the ease by which iron is released from ferritin.
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PMID:Relationship between iron and phosphate in mammalian ferritins. 851 27

Ferritin in plants is a nuclear-encoded, multisubunit protein found in plastids; an N-terminal transit peptide targets the protein to the plastid, but the site for formation of the ferritin Fe mineral is unknown. In biology, ferritin is required to concentrate Fe to levels needed by cells (approximately 10(-7) M), far above the solubility of the free ion (10(-18) M); the protein directs the reversible phase transition of the hydrated metal ion in solution to hydrated Fe-oxo mineral. Low phosphate characterizes the solid-phase Fe mineral in the center of ferritin of the cytosolic animal ferritin, but high phosphate is the hallmark of Fe mineral in prokaryotic ferritin and plant (pea [Pisum sativum L.] seed) ferritin. Earlier studies using x-ray absorption spectroscopy showed that high concentrations of phosphate present during ferritin mineralization in vivo altered the local structure of Fe in the ferritin mineral so that it mimicked the prokaryotic type, whether the protein was from animals or bacteria. The use of x-ray absorption spectroscopy to analyze the Fe environment in pea-seed ferritin now shows that the natural ferritin mineral in plants has an Fe-P interaction at 3.26A, similar to that of bacterial ferritin; phosphate also prevented formation of the longer Fe-Fe interactions at 3.5A found in animal ferritins or in pea-seed ferritin reconstituted without phosphate. Such results indicate that ferritin mineralization occurs in the plastid, where the phosphate content is higher; a corollary is the existence of a plastid Fe uptake system to allow the concentration of Fe in the ferritin mineral.
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PMID:Formation of the ferritin iron mineral occurs in plastids. 855 14

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 and exposed on the cavity of L-chains, were substituted with His, as in H-chains. The double substitution made the L-homopolymers as sensitive as the H-homopolymers to the iron-induced aggregation, whereas the opposite substitution in the H-chain increased homopolymer resistance to the aggregation only marginally. Millimolar concentrations of citrate and phosphate increased iron incorporation in H-homopolymers by reducing non-specific iron hydrolysis, but inhibited that in L-homopolymers by sequestering available iron. The data indicate that the specific iron incorporation into L-homopolymers is mainly due to the iron-nucleation capacity of Glu-57, Glu-60 and other carboxyl groups exposed on the cavity; in contrast, the specificity of iron incorporation into H-homopolymers is related to its ferroxidase activity, which determines rapid Fe(III) accumulation inside the cavity. The finding that ferroxidase centres are essential for the incorporation of iron in the presence of likely candidates of cellular iron transport, such as phosphate and citrate, confirms their importance in ferritin function in vivo.
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PMID:Evidence that the specificity of iron incorporation into homopolymers of human ferritin L- and H-chains is conferred by the nucleation and ferroxidase centres. 866 Feb 74

Forty patients with chronic renal failure (CRF) were enrolled into the study, none of whom had peptic ulcer disease, amyloidosis, a previous abdominal operation, diabetes mellitus or other factors that could influence gastric emptying. Twenty of the 40 patients had been receiving regular haemodialysis (HD) for at least 1 year prior to the study. Twelve of the 40 patients had upper gastrointestinal symptoms/signs (GI Sx). Radionuclide-labelled solid meals were used to calculate gastric emptying time (GET). Twenty-five normal volunteers comprised the control group. Of the 40 patients, 35 (88%) had an abnormal GET. The incidence of an abnormal GET in HD and non-HD patients was 95 and 80%, respectively; the incidence of an abnormal GET in patients with and without upper GI Sx was 83 and 89%, respectively. These differences in the incidence of an abnormal GET among the HD and non-HD patients, as well as in the patients with and without upper GI Sx, were not statistically significant. There were no significant differences between the normal and abnormal GET patients for any of the following clinical parameters and conditions: dialyser-specific proportionality constant x time/urea distribution volume (KT/V), protein catabolic rate (PCR), ferritin, serum blood urea nitrogen, creatinine, calcium ion, phosphate, intact parathyroid hormone, albumin, uric acid, haemoglobin, triglyceride and cholesterol, total dialysis time, creatinine clearance and daily urine protein. We conclude that in Chinese patients with CRF, both dialysed and undialysed, an abnormal GET is common. The pathogenesis seems to be multifactorial. The presence of abdominal symptoms cannot foretell an abnormal GET.
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PMID:Delayed gastric emptying in patients with chronic renal failure. 877 42

This study describes the application of aqueous two-phase partition using polyethylene glycol (PEG)-potassium phosphate systems for the direct recovery of proteins, and aggregates thereof, from mammalian brain tissue homogenates. Investigation of established methodologies for the purification of prion proteins (PrP) from bovine brain affected with transmissible spongiform encephalopathy (BSE) has identified an alternative purification regime based on aqueous two-phase partition. This circumvents energy-intensive and rate-limiting unit operations of ultracentrifugation conventionally used for isolation of PrP. Selectivity of various PEG-phosphate systems varied inversely with polymer molecular mass. The maximum protein recovery from bovine brain extracts was obtained with systems containing PEG 300. Manipulation of the aqueous environment, to back-extract protein product from the PEG-rich top phase into the phosphate-rich lower phase, enabled integration of ATPS with conventional hydrophobic interaction chromatography (HIC) which selectively removes obdurate contaminating proteins (i.e. ferritin).
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PMID:Aqueous two-phase partition of complex protein feedstocks derived from brain tissue homogenates. 879 85

The adsorption of ferritin from phosphate-buffered saline (PBS) onto gold has been examined using a quartz crystal microbalance (QCM), surface plasmon resonance (SPR), X-ray photoelectron spectroscopy (XPS), and atomic force microscopy (AFM). Application of these techniques allows elucidation of the surface coverage and layer thickness of ferritin on gold. The kinetics of ferritin adsorption onto gold were investigated by monitoring the resonant frequency shift of a QCM. Adsorption isotherms for ferritin in PBS and in air have been measured by QCM. These isotherms suggest less than monolayer coverage of ferritin on gold. A layer thickness of 4.8 ± 0.2 nm was calculated for the dry ferritin film from QCM data. Measurements of the shift in the reflectivity of light at a fixed angle close to the SPR plasmon resonance were also used to follow the kinetics of ferritin adsorption. Full SPR curves were measured in PBS solution and air and were used to determine the effective thickness of the ferritin layer in both environments. The ferritin layer on gold from SPR data was found to be twice as thick when measured in PBS as it was for a dry film. This difference in thickness is attributed to shrinkage of ferritin with drying. Angle-resolved XPS measurements on a dry ferritin film (preadsorbed on gold) yield a ferritin thickness of 4.7 ± 0.5 nm, a value in good agreement with those determined from QCM and SPR. QCM, SPR, and XPS all yield a surface coverage of 6.3 ± 0.7 mg m-2 for dry ferritin layers on gold. AFM enabled examination of the topography of ferritin adsorbed on gold on the nanometer scale and confirmed that ferritin forms an incomplete monolayer. In all cases, ferritin was found to be irreversibly adsorbed to gold and to form a stable protein layer, thus making it well suited as a biological receptor layer for immunosensing applications.
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PMID:Characterization of Ferritin Adsorption onto Gold 905 16

Hemoglobin (Hb) induces heme oxygenase-1 (HO-1), which catalyzes the breakdown of heme to bilirubin, and ferritin. Rats pretreated with Hb have been shown to survive lethal doses of lipopolysaccharide (LPS; see L. Otterbein, S. L. Sylvester, and A. M. Choi. Am. J. Respir. Cell Mol. Biol. 13: 595-601, 1995). The physiological basis of this increased survival and the mechanism(s) involved in the protection against LPS by Hb are unknown. Here we investigated 1) the effects of Hb on the hemodynamic and biochemical parameters of LPS-induced tissue injury and 2) the mechanism(s) by which Hb conferred protection against shock and tissue injury. Hb-treated rats maintained normal mean arterial blood pressure, whereas control rats experienced cardiovascular collapse after a lethal dose of LPS. Hepatic and renal functions, peripheral white blood cells, serum lactate dehydrogenase, and phosphate also remained normal after LPS in Hb-treated rats. Hb also attenuated LPS-induced neutrophil alveolitis and tumor necrosis factor-alpha levels. Pretreatment with both desferoxamine, which, like ferritin, can bind iron, and with exogenous apoferritin failed to protect against LPS. In contrast, treatment with Hb plus desferoxamine, which induced HO-1 but not ferritin, did protect against LPS. Treatment with iron-dextran, which induced ferritin but not HO-1, did not protect against LPS. We conclude that Hb pretreatment reduces the inflammatory and physiological consequences of LPS and that the Hb-induced protection against LPS is dependent on HO-1 and not ferritin induction.
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PMID:Mechanism of hemoglobin-induced protection against endotoxemia in rats: a ferritin-independent pathway. 912 78

Ferritin is the main intracellular iron storage protein. Ferritin iron may be released by many reducing agents including ascorbate. In this work we report ferritin to catalyze the oxidation of ascorbate. The kinetics of this process were studied in detail in phosphate buffer (pH 7.40), at 37 degrees C by using the Clark electrode technique and ESR. The catalytic effect of ferritin manifested itself as the increase both in the rate of oxygen uptake and steady-state concentration of the ascorbate radical. The ferritin catalytic activity was found to be modified by iron chelators, EDTA. Desferal (DFO) as well as by ferrozine (FRZ) which is widely used in kinetic studies on ferritin iron release thanks to the formation of a coloured complex with Fe(II). While EDTA promotes the catalytic action of ferritin, DFO and FRZ diminished it. From the comparison of the kinetics of ascorbate oxidation obtained in the current work and data on the kinetics of ferritin iron release reported by Boyer and McCleary ((1987) Free Rad. Biol. Med. 3, 389-395), we conclude that iron bound to ferritin rather than the iron released is likely responsible for ferritin catalytic action. In addition, it has been concluded that the use of FRZ as an analytical reagent in kinetic studies of reductive ferritin iron release requires taking into account the competitive character of the formation of the Fe(II)-FRZ complex.
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PMID:Iron bound to ferritin catalyzes ascorbate oxidation: effects of chelating agents. 913 40


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