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)

High quality of secondary electron (SE) images, taken at useful magnifications of 100,000 to 200,000, require new signal generation and collection methods and new metal coating procedures. High quality is defined as the condition under which image contrast describes accurately the topographic features of the specimen in a size range that approximates the beam diameter. Such high resolution contrasts are produced by the SE (SE-I) generated by a small electron probe on the specimen surface. Tobacco mosiac virus and ferritin molecules deposited on bulk substrates were introduced as test specimens to check the image quality obtained. The SE-I signal contrast could be imaged when SE (SE-III), produced by backscattered electrons (BSE) at the pole piece of the final lens, were eliminated with an electron absorption device attached to the pole piece. This signal collection procedure will be referred to as "Secondary Electron-I Image" (SE-I image) mode. In addition to the SE-III, BSE generate SE-II in the specimen itself. On specimens deposited on bulk gold or platinum, and coated with the same metals SE-II produced a microroughness contrast that limited particle resolution in the SE-I image mode to approximately 10 nm. Reduction of SE-II and enrichment of the signal in SE-I was achieved by using continuous fine crystalline coatings of tantalum, niobium and chromium. By applying these metals in films of approximately 2.0 nm thickness, the SE-I contrast generation was found to be indepedent of the atomic number of the metal. Edge sharpness was improved when the specimens were coated with low atomic number metals. Under these conditions, the quality of images obtained in SE-I image mode equals that of images obtained in TEM from identically coated specimens and was limited only by the size of the topographic details, beam diameter and beam current.
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PMID:Conditions required for high quality high magnification images in secondary electron-I scanning electron microscopy. 718 36

The rat liver after extrahepatic biliary obstruction was studied by SEM and TEM in correlation with basic histochemical techniques. Cholestasis was verified by serological methods. The biochemical data (increase in serum bilirubin values, a gradual lowering of the albumin fraction), in agreement with the ultrastructural results of a sparse RER, suggested a gradual decrease of the protein synthetic activity of the hepatocyte. SEM and TEM revealed numerous fat-storing cells, closely associated with patches of connective fibrils in the subendothelial spaces. Further ultrastructural observations demonstrated: a) a proliferation of the intrahepatic biliary tree (ductular proliferation, including newly formed ducts with sacculation and diverticuli); b) an increased number of canaliculo-ductular junctions and, c) an increase in the length of the bile canalicular network due to its tortuous course, pocketing and side branching. The occurrence of an intact cytoplasmic barrier separating the bile canalicular lumen from the Disse's space together with the results obtained by retrograde infusion of ferritin into the biliary tree suggested that the regurgitation pathway by ductular reabsorption and by transhepatocytic transport is the best documented and most acceptable, at least in the rat.
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PMID:A scanning and transmission electron microscopic study of experimental extrahepatic cholestasis in the rat. 733 53

In situ functional assay of each ferritin molecule in single-layer 2D arrays for horse spleen apoferritin and recombinant horse L- and human H-apoferritins was conducted by observing the iron-cores formed in the arrays by TEM. The study of the time-course, pH-dependence, and temperature-dependence of the function confirmed the iron-core formation to be due to the native function of apoferritins in array. Dark-field TEM imaging revealed that there was crystallinity in the cores in the array of recombinant human H-apoferritin. This iron-core formation was perfectly preserved in the array even after 3 months of storage at room temperature and low humidity. Moreover, about 50% of the function was found to remain in the array after it was exposed to 150 degrees C in vacuum for 1 hr.
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PMID:Single molecular functional assay of ferritin arrays. 920 35

With rare exceptions, virtually all studied organisms from Archaea to man are dependent on iron for survival. Despite the ubiquitous distribution and abundance of iron in the biosphere, iron-dependent life must contend with the paradoxical hazards of iron deficiency and iron overload, each with its serious or fatal consequences. Homeostatic mechanisms regulating the absorption, transport, storage and mobilization of cellular iron are therefore of critical importance in iron metabolism, and a rich biology and chemistry underlie all of these mechanisms. A coherent understanding of that biology and chemistry is now rapidly emerging. In this review we will emphasize discoveries of the past decade, which have brought a revolution to the understanding of the molecular events in iron metabolism. Of central importance has been the discovery of new proteins carrying out functions previously suspected but not understood or, more interestingly, unsuspected and surprising. Parallel discoveries have delineated regulatory mechanisms controlling the expression of proteins long known--the transferrin receptor and ferritin--as well as proteins new to the scene of iron metabolism and its homeostatic control. These proteins include the iron regulatory proteins (IRPs 1 and 2), a variety of ferrireductases in yeast an mammalian cells, membrane transporters (DMT1 and ferroportin 1), a multicopper ferroxidase involved in iron export from cells (hephaestin), and regulators of mitochondrial iron balance (frataxin and MFT). Experimental models, making use of organisms from yeast through the zebrafish to rodents have asserted their power in elucidating normal iron metabolism, as well as its genetic disorders and their underlying molecular defects. Iron absorption, previously poorly understood, is now a fruitful subject for research and well on its way to detailed elucidation. The long-sought hemochromatosis gene has been found, and active research is underway to determine how its aberrant functioning results in disease that is easily controlled but lethal when untreated. A surprising connection between iron metabolism and Friedreich's ataxia has been uncovered. It is no exaggeration to say that the new understanding of iron metabolism in health and disease has been explosive, and that what is past is likely to be prologue to what is ahead.
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PMID:Chemistry and biology of eukaryotic iron metabolism. 1147 Feb 29

Recently, Quintana and others published the results of TEM investigations of ferritin cores extracted from the brain tissue of patients suffering from progressive supranuclear palsy (PSP) and Alzheimer's disease (AD). These ferrihydrite (fFe2O3.9H2O) cores from the iron storage protein ferritin were found to contain a ferrous (Fe2+) iron-bearing biomineral with cubic structure similar to the magnetite standards which were measured. This is a highly important result as magnetic and electron microscopy analysis has demonstrated the presence of magnetite (Fe3O4) and maghemite (gammaFe2O3) in human brain tissue.
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PMID:On the structural form of iron in ferritin cores associated with progressive supranuclear palsy and Alzheimer's disease. 1087 42

A large number of different proteins or protein domains have been investigated as possible scaffolds to engineer antibody-like molecules. We have previously shown that the TEM-1 beta-lactamase can accommodate insertions of random sequences in two loops surrounding its active site without compromising its activity. From the libraries that were generated, active enzymes binding with high affinities to monoclonal antibodies raised against prostate-specific antigen, a protein unrelated to beta-lactamase, could be isolated. Antibody binding was shown to affect markedly the enzyme activity. As a consequence, these enzymes have the potential to be used as signaling molecules in direct or competitive homogeneous immunoassay. Preliminary results showed that beta-lactamase clones binding to streptavidin could also be isolated, indicating that some enzymes in the libraries have the ability to recognize proteins other than antibodies. In this paper, we show that, in addition to beta-lactamases binding to streptavidin, beta-lactamase clones binding to horse spleen ferritin and beta-galactosidase could be isolated. Affinity maturation of a clone binding to ferritin allowed obtaining beta-lactamases with affinities comprised between 10 and 20 nM (Kd) for the protein. Contrary to what was observed for beta-lactamases issued from selections on antibodies, enzyme complexation induced only a modest effect on enzyme activity, in the three cases studied. This kind of enzyme could prove useful in replacement of enzyme-conjugated antibodies in enzyme-linked immunosorbant assays (ELISA) or in other applications that use antibodies conjugated to an enzyme.
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PMID:TEM-1 beta-lactamase as a scaffold for protein recognition and assay. 1202 49

The dissociation of apoferritin into subunits at pH 2 followed by its re-formation at pH 8.5 in the presence of hexacyanoferrate(III) gave rise to a solution containing hexacyanoferrate(III) trapped within the apoferritin and hexacyanoferrate(III) outside it. The addition of Fe(II) to the dialyzed solution resulted in the appearance of the characteristic Prussian blue color. The UV-vis spectrum of this solution showed a broad band centered at 710 nm, and the IR spectrum contained a broad-medium band at 2083 cm(-1). Both features are consistent with the charge-transfer band and the C[bond]N stretching mode in the Fe(II)[bond]CN[bond]Fe(III) fragment of PB. TEM images of the obtained Prussian blue solution showed discrete spherical electron dense iron particles with an average size of about 5 nm. This represents a new route for preparing metallic nanoparticles that offers control over the size and protection against aggregation. Moreover, the fact that the particles are obtained by reaction of hexacyanoferrate(III) and iron(II) building blocks opens up the possibility of obtaining not only homo- but also heterobimetallic nanoparticles.
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PMID:Nanoparticles of Prussian blue ferritin: a new route for obtaining nanomaterials. 1457 62

This paper reports novel findings of an investigation of the formation of water-soluble iron oxide nanoparticles from iron-storage protein ferritin. The strategy couples thermal removal of the protein shell on a planar substrate and subsequent sonication in aqueous solution under controlled temperature. Advantages of using ferritin as a precursor include well-defined core size, core composition, water-solubility and processibility. The formation of the nanoparticles was characterized using TEM, UV-Vis and FTIR techniques. Iron oxide nanoparticles in the size range of 5-20 nm diameters were produced. In addition to thermal treatment conditions, the sonication temperature of the nanoparticles in water was found to play an important role in determining the resulting particle size. This simple and effective route has important implications to the design of composite nanoparticles for potential magnetic, catalytic, biomedical sensing and other nanotechnological applications.
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PMID:Formation of water-soluble iron oxide nanoparticles derived from iron storage protein. 1557 Sep 48

Nanoparticles of iron phosphate, iron arsenate, iron molybdate, and iron vanadate were synthesized within the 8 nm interior of ferritin. The synthesis involved reacting Fe(II) with ferritin in a buffered solution at pH 7.4 in the presence of phosphate, arsenate, vanadate, or molybdate. O2 was used as the oxidant to deposit the Fe(III) mineral inside ferritin. The rate of iron incorporation into ferritin was stimulated when oxo-anions were present. The simultaneous deposition of both iron and the oxo-anion was confirmed by elemental analysis and energy-dispersive X-ray analysis. The ferritin samples containing iron and one of the oxo-anions possessed different UV/vis spectra depending on the anion used during mineral formation. TEM analysis showed mineral cores with approximately 8 nm mineral particles consistent with the formation of mineral phases inside ferritin.
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PMID:Nanophase iron phosphate, iron arsenate, iron vanadate, and iron molybdate minerals synthesized within the protein cage of ferritin. 1584 28

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


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