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

Ferritin-binding proteins (FBPs) in bovine serum were characterized by ferritin immunoassay, ferritin-binding activity, and immunoblotting. Serum ferritin, but not tissue ferritin, was precipitated by centrifugation at 14000 x g for 30 min, and bovine spleen ferritin added to bovine serum was precipitated by centrifugation at 1650 x g for 20 min. Two FBPs (FBP1 and FBP2) were purified from bovine serum by sequential chromatography on bovine spleen ferritin-Sepharose 4B affinity and Sephacryl S-300 columns. FBP1 separated into 82 kDa- and 26 kDa-bands on SDS-PAGE, while FBP2 separated into 55 kDa- and 26 kDa-bands. FBP1 and FBP2 were identified as IgM and IgG, respectively, by immunoblotting with alkaline phosphatase-labeled antibodies specific for bovine IgM, IgG, and IgA heavy chains. Given these results, we suggest that bovine FBPs are autoantibodies (IgM and IgG) to ferritin and that circulating ferritin exists as an immune complex.
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PMID:Characterization of bovine serum ferritin-binding proteins. 1512 10

Ferritin has been shown as being the principal iron storage in the majority of living organisms. In marine species, ferritin is also involved in high-level accumulation of (210)Po. As part of our work on the investigation of these radionuclides' concentration in natural environment, ferritin was searched at the gene and protein level. Ferritin was purified from the visceral mass of the oyster Crassostrea gigas by ion-exchange chromatography and HPLC. SDS-PAGE revealed one band of 20 kDa. An Expressed Sequence Tag (EST) library was screened and led to the identification of two complementary DNA (cDNA) involved in ferritin subunit expression. The complete coding sequences and the untranslated regions (UTRs) of the two genes were obtained and a 5' Rapid Amplification of cDNA Ends (RACE) was used to obtain the two iron-responsive elements (IREs) with the predicted stem-loop structures usually present in the 5'-UTR of ferritin mRNA. Sequence alignment in amino acid of the two new cDNA showed an identity with Pinctada fucata (85.4-88.3%), Lymnaea stagnalis (79.3-82.2%) and Helix pomatia (79.1-79.1%). The residues responsible for the ferroxidase center, conserved in all vertebrate H-ferritins, are present in the two oyster ferritin subunits. Oyster ferritins do not present the special characteristics of other invertebrate ferritins like insect ferritins but have some functional similarities with the vertebrate H chains ferritin.
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PMID:Crassostrea gigas ferritin: cDNA sequence analysis for two heavy chain type subunits and protein purification. 1531 22

In this work, evidence for the presence of ferritins in plant mitochondria is supplied. Mitochondria were isolated from etiolated pea stems and Arabidopsis thaliana cell cultures. The proteins were separated by SDS/PAGE. A protein, with an apparent molecular mass of approximately 25-26 kDa (corresponding to that of ferritin), was cross-reacted with an antibody raised against pea seed ferritin. The mitochondrial ferritin from pea stems was also purified by immunoprecipitation. The purified protein was analyzed by MALDI-TOF mass spectrometry and the results of both mass finger print and peptide fragmentation by post source decay assign the polypeptide sequence to the pea ferritin (P < 0.05). The mitochondrial localization of ferritin was also confirmed by immunocytochemistry experiments on isolated mitochondria and cross-sections of pea stem cells. The possible role of ferritin in oxidative stress of plant mitochondria is discussed.
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PMID:Evidence for the presence of ferritin in plant mitochondria. 1535 42

The objective of this work was to gain a better understanding of the mechanism of resistance to protein adsorption of surfaces grafted with poly(ethylene oxide) (PEO). A polyurethane-urea was used as a substrate to which PEO was grafted. Grafting was carried out by introducing isocyanate groups into the surface followed by reaction with amino-terminated PEO. Surfaces grafted with PEO of various chain lengths (PUU-NPEO) were prepared and characterized by water contact angle and X-ray photoelectron spectroscopy (XPS). XPS data indicated higher graft densities on the PUU-NPEO surfaces than on analogous surfaces prepared using hydroxy-PEO (PUU-OPEO) as reported previously [J.G. Archambault, J.L. Brash, Colloids Surf. B: Biointerf. 33 (2004) 111-120]. Protein adsorption experiments using radiolabeled myoglobin, concanavalin A, albumin, fibrinogen and ferritin as single proteins in buffer showed that adsorption was reduced on the PEO-grafted surfaces by up to 95% compared to the control. Adsorption decreased with increasing PEO chain length and reached a minimum at a PEO MW of 2000. Adsorption levels on surfaces with 5000 and 2000 MW grafts were similar. There was no clear effect of protein size on resistance to protein adsorption. Adsorption on the PUU-NPEO surfaces was significantly lower than on the corresponding PUU-OPEO surfaces, again suggesting higher graft densities on the former. Adsorption of fibrinogen from plasma was also greatly reduced on the grafted surfaces. From analysis (SDS-PAGE, immunoblotting) of the proteins eluted after plasma exposure, it was found that the grafted surfaces and the unmodified substrate adsorbed the same proteins in roughly the same proportions, suggesting that adsorption to the PEO surfaces occurs on patches of bare substrate. The PEO grafts did not apparently cause differential access to the substrate based on protein size.
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PMID:Protein resistant polyurethane surfaces by chemical grafting of PEO: amino-terminated PEO as grafting reagent. 1554 34

As intracellular iron storage molecules, only hydroxymate type siderophores have been reported in ascomycetes and basidiomycetes. This is the first report documenting the presence of mycoferritin in ascomycetes. The fungus, Aspergillus parasiticus (255), is capable of producing mycoferritin only upon induction with iron in yeast extract sucrose (YES) medium. The same has been purified from Aspergillus sps by application of conventional biochemical techniques. The molecular mass, yield, iron and carbohydrate contents of the HPLC purified protein were 460kDa, 0.012mg/g of wet mycelia, 1.6% and 6.0%, respectively. The iron content was much lower than Mortierella alpina mycoferritin (17%). Native PAGE revealed the presence of trimeric and monomeric forms of ferritin. Subunit analysis by SDS-PAGE showed a single protein subunit of approximately 20kDa suggesting structural simplicity of the apoferritin shell. Variation in amino acid composition was noted upon comparison with ferritins of other species. Interestingly, no phenylalanine could be detected in the mycoferritin of Aspergillus sps. The acidic amino acid content was 1.5-1.6 fold higher than mammalian and fish ferritins. The spectral characteristics (UV/VIS and fluorescence) of mycoferritin were akin to equine spleen ferritin. However, circular dichroic spectra revealed a lower degree of helicity.
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PMID:Purification and characterization of mycoferritin from Aspergillus parasiticus (255). 1583 84

We used two-dimensional SDS-PAGE and microsequencing or peptide mass fingerprinting to identify major proteins in the hemolymph of Anopheles gambiae. We found approximately 280 protein spots in hemolymph and identified 28 spots, representing 26 individual proteins. Most of these proteins have known or predicted functions in immunity, iron transport, or lipid biology. Many of the proteins have been found in hemolymph in other insects but one protein is novel: a new member of the ML family (involved in lipid recognition). Three of the identified proteins increased in spot intensity or appeared de novo following bacterial injection: a phenoloxidase, and two chitinase-like proteins. A subset of proteins decreased following bacterial injections: these included the light and heavy chains of ferritin. Several proteins appeared in hemolymph following any wound or injection. Most of these are metabolic enzymes lacking signal peptides that are likely to be released as a result of damage to muscles and other tissues by injury. The map will provide a useful tool for examining changes in hemolymph proteins following blood feeding and infection by parasites.
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PMID:The hemolymph proteome of Anopheles gambiae. 1594 78

In an attempt to design a targeted drug delivery system to tumors' over-expressing H-ferritin specifically recognized by a monoclonal antibody, AMB8LK, a cationic emulsion - AMB8LK conjugate was prepared. A novel cross-linker molecule bearing maleimide group was synthesized and added to cationic emulsion formulation for AMB8LK Fab' fragment covalent coupling. NMR spectroscopy confirmed the cross-linker synthesis and the preservation of the active maleimide function. SDS gel-electrophoresis results corroborated the formation of the Fab' fragment. Different densities of Fab' fragments (10-200 Fab'/oil droplet) were conjugated to emulsion droplet interface and no changes in the physico-chemical properties were observed ( approximately 120 nm size and zeta potential of approximately +30 mV). The coupling efficiency ranged from 55% to 70% and was visualized by TEM showing gold particles attached to the droplet interface. Cell culture studies demonstrated specific binding to cells as confirmed by the occurrence of the marked reduction in binding when free AMB8LK Mab was incubated before adding the AMB8LK-emulsion conjugate to the cells. The coupling of AMB8LK Fab' fragment to the cationic emulsion increased the cells uptake by 50% as compared to non-conjugated respective cationic emulsion. Appropriate conditions were, thus, identified for coupling AMB8LK Fab' fragment to cationic emulsion without altering the specificity and affinity of the Mab fragment to the tumor antigen.
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PMID:The design and evaluation of a novel targeted drug delivery system using cationic emulsion-antibody conjugates. 1622 21

Plasma ferritin is an important extracellular iron storage molecule, whose concentration increases drastically in cancer and infection. During infection, the pathogen usurps host iron for its survival and pathogenicity; hence, maintenance of the plasma ferritin level during infection is a crucial host defence mechanism. In this study, the horseshoe crab plasma ferritin complex was purified, characterized, and its involvement in innate immune defence was investigated. The plasma ferritin appears as a 21-kDa subunit on SDS-PAGE. Full-length ferritin-H cDNAs (CrFer-H1 and CrFer-H2) were cloned. Analysis of the 5' UTR indicates the existence of a functional iron-response element, suggesting that both the CrFer-H genes may be post-transcriptionally regulated. Northern analysis shows that the CrFer-H is ubiquitously expressed. Within 3 h of lipopolysaccharide challenge, the gene is up-regulated by > 12-fold. In contrast, iron-loading did not result in any significant change. When challenged with Pseudomonas aeruginosa, the plasma ferritin disappeared between 6-48 h and re-appeared thereafter, suggesting that during infection, ferritin may be concealed intracellularly as it withholds iron from the invading pathogen. Taken together, these results provide insights into the importance of plasma ferritin as an evolutionarily conserved molecule for the iron-withholding strategy of innate immunity.
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PMID:The response of ferritin to LPS and acute phase of Pseudomonas infection. 1626 99

Ferritin is a major eukaryotic protein and in humans is the protein of iron storage. A partial gene fragment of ferritin (255 bp) taken from the total RNA of Periserrula leucophryna, was amplified by RT-PCR using oligonucleotide primers designed from the conserved metal binding domain of eukaryotic ferritin and confirmed by DNA sequencing. Using the 32P-labeled partial ferritin cDNA fragment, 28 different clones were obtained by the screening of the P. leucophryna cDNA library prepared in the Uni-ZAP XR vector, sequenced and characterized. The longest clone was named the PLF (Periserrula leucophryna ferritin) gene and the nucleotide and amino acid sequences of this novel gene were deposited in the GenBank databases with accession numbers DQ207752 and ABA55730, respectively. The entire cDNA of PLF clone was 1109 bp (CDS: 129-653), including a coding nucleotide sequence of 525 bp, a 5'-untranslated region of 128 bp, and a 3'-noncoding region of 456 bp. The 5'-UTR contains a putative iron responsive element (IRE) sequence. Ferritin has an open reading frame encoding a polypeptide of 174 amino acids including a hydrophobic signal peptide of 17 amino acids. The predicted molecular weights of the immature and mature ferritin were calculated to be 20.3 kDa and 18.2 kDa, respectively. The region encoding the mature ferritin was subcloned into the pT7-7 expression vector after PCR amplification using the designed primers and included the initiation and termination codons; the recombinant clones were expressed in E. coli BL21(DE3) or E. coli BL21(DE3)pLysE. SDS-PAGE and western blot analysis showed that a ferritin of approximately 18 kDa (mature form) was produced and that by iron staining in native PAGE, it is likely that the recombinant ferritin is correctly folded and assembled into a homopolymer composed of a single subunit.
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PMID:Characterization, cloning and expression of the ferritin gene from the Korean polychaete, Periserrula leucophryna. 1655 18

We sought to explore the relationship between Helicobacter pylori infection and serum ferritin, vitamin B(12), folate, and zinc status among children. Fifty patients aged 5-18 years who underwent upper gastrointestinal endoscopy because of dyspeptic symptoms, were studied, prospectively. Patients were grouped as H. pylori positive (group 1, n=32) or H. pylori negative (group 2, n=18) by histopathologic examination and rapid urease test. Fasting serum ferritin, vitamin B(12), folate, and zinc levels of patients were measured. Both groups were indifferent according to age, gender, height standard deviation score (H(SDS)), and weight standard deviation score (W(SDS)). Serum ferritin levels were 33+/-26 and 50+/-46 ng/mL (P=.098), vitamin B(12) levels were 303+/-135 and 393+/-166 pg/mL (P=.042), folate levels were 9.64+/-3.2 and 9.61+/-2.8 ng/mL (P=.979), and zinc levels were 95+/-48 and 87+/-31 mug/dL (P=.538), in groups 1 and 2, respectively. Ferritin levels of 14 (43.8%) patients in group 1 and 6 (33.3%) patients in group 2 were below the normal range (P=.470). Serum vitamin B(12) levels of 9 children (28%) in group 1 and 2 children (11%) in group 2 were below the normal range (P=.287). The findings of the present study suggest that H. pylori infection has a negative effect on serum ferritin and vitamin B(12) levels in children. This negative effect on vitamin B(12) levels is rather marked in contrast to that on ferritin levels. H. pylori infection has no significant effect on serum folate or zinc levels among children.
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PMID:Serum ferritin, vitamin B(12), folate, and zinc levels in children infected with Helicobacter pylori. 1721 8


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