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

We have investigated the importance of several clinical and laboratory parameters on the development of acquired cystic kidney disease (ACKD) as detected by ultrasonography in 19 patients who had received dialysis therapy for at least three years. We were particularly interested on the possible effect of the serum levels of oxalate and silicon, which can produce tubular obstruction, and that of vanadium, which can affect cell proliferation. The severity of ACKD increased with the duration of dialysis and was greater in men than in women. Positive correlations were observed between the grades of ACKD and the levels of hemoglobin, hematocrit, and parathyroid hormone, while there was a negative correlation between ACKD and serum ferritin levels. The serum levels of oxalate, silicon, and vanadium, pre- and postdialysis, were markedly and significantly higher than those in normal controls, but there was no significant correlation between these levels and the duration of dialysis therapy or severity of ACKD. The pre- and postdialysis levels of vanadium were not significantly different, while the levels of oxalate and silicon were significantly lower in the postdialysis samples. No significant correlations were detected between ACKD and age of the patients, blood pressure, protein catabolic rate, efficiency of dialysis index, or the serum levels of iron, sodium, potassium, calcium, phosphorus, aluminum, and beta 2-microglobulin.
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PMID:Oxalate, silicon and vanadium in acquired cystic kidney disease. 201 15

Foamy alveolar macrophages (FAM) are observed in lungs injured by Bleomycin (BLM), but their relation to pulmonary fibrosis is not clearly understood. We purified FAM from BLM-instilled rat lungs by density gradient centrifugation on Percoll, and studied the effect of FAM on pulmonary fibrosis. The cells lavaged from the rat lungs 14 days after the administration of BLM (B) or saline (S), were applied on Percoll. After centrifugation, the cells layered on each interface were collected and named as SI, SII, SIII, and BI, BII, BIII in order of gravity. The BI layer included 8.5% of unfractionated cells (U). These BI cells were viable (88%), significantly larger than the others, nonspecific esterase positive cells, and included much ferritin and lysozyme, and were morphologically identified as alveolar macrophages (AM). Therefore, we called the BI cells FAM. We estimated the capacity of FAM (2.5 X 10(5] to synthesize DNA (3H-thymidine uptake) and RNA (3H-uridine uptake), and the activities of silica-stimulated FAM to cause proliferation of mouse thymocytes (IL-1 activity) and rat lung fibroblasts (FP activity), and to produce PGE2. FAM has a lower mitogenic activity but did not have been protein synthetic activity as compared with the others. Silica-stimulated FAM released less IL-1 than BII or BIII, and induced less fibroblast growth than BII, but induced as much as BIII, possibly because of the increased capacity of BIII cells to produce PGE2, which is known to inhibit fibroblast growth. In this way, FAM were considered to be "already activated" rather than "highly activated" cells, but the presence of FAM suggested that smaller or denser AM might receive bleomycin stimulation and release fibrogenic mediators (IL-1 or MDGF) into the alveolar spaces during FAM formation, and that AM might participate in the fibrogenic responses.
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PMID:[The effect of foamy alveolar macrophages presented in bleomycin-injured rat lungs in pulmonary fibrosis]. 247 35

We describe the use of a magnetic sector spectrometer positioned below the projection chamber of an electron microscope for energy filtered transmission imaging. The spectrometer used has circular pole face edges and is corrected for second order aberrations. A round EM lens is placed after the sector to form a real image of the virtual achromatic image produced by the spectrometer. A slit placed in the dispersion plane allows the passage of electrons in a selected energy range. The filtered image is projected onto a transmission phosphor and acquired with a silicon intensified TV camera and stored in digital form on computer disk. Filtered images are taken at two energies, one immediately preceding (pre-edge) and one on the characteristic energy loss (edge). To obtain images showing the distribution of elements, background subtraction is performed by either subtraction or division of edge and pre-edge images. The optical properties of the imaging system are described and the results are illustrated by energy filtered images of single ferritin molecules (Fe M2,3 and C k), the phosphorus distribution in ribosomes (PL2,3) and the localization of calcium in muscle (Ca L2, 3). The major advantage of the system, compared to other energy filtered imaging methods, is that it can be readily adapted to existing high vacuum microscopes without the necessity of modifying the column to insert a spectrometer.
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PMID:Applications of energy filtered imaging in biology. 663 70

A sharp tip with high aspect ratio is required for imaging biological macromolecules by atomic force microscopy (AFM). A tip with the end radius of curvature less than 3 nm has been reproducibly fabricated by means of electron beam deposition (EBD) in a field-emission scanning electron microscope. Two-dimensional protein arrays of ferritin and catalase, prepared at air/water interface and transferred onto silicon wafer, could be imaged both in air and in water by AFM using this sharp EBD-tip in contact mode. The negative staining preparation conventionally used in the transmission electron microscopy of protein was applied and shown to be quite effective in fixing the protein arrays for the AFM imaging in air. Individual molecules of ferritin and catalase were visible in the two-dimensional arrays. Also, imaging in water of these protein arrays presented molecular images clearer than in air, due probably to the absence of the adhesion force and the resulting weak lateral force during scanning. These images convince us of the capability of this supertip for AFM studies of biological molecules under aqueous conditions.
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PMID:Imaging two-dimensional arrays of soluble proteins by atomic force microscopy in contact mode using a sharp supertip. 949 89

A signal registration strategy from micropatterned immunosensors that converts antigen-antibody binding reactions into electrochemical signals was demonstrated. An array-type micropatterned gold electrode on a silicon wafer was fabricated, containing two electrode geometries of rectangular (100 microm x 500 microm) and circular (r. 50 microm) types, exhibiting electrochemical characteristics of bulk and micro-electrodes, respectively. Ferritin was employed as a model analyte for immunosensing because it has an advantageous molecular structure for functionalization to the sensing interface, and is regarded as a general marker protein for tumors and cancer recurrence. With the fabricated and ferritin-functionalized immunosensors, biospecific interactions were performed with antiferritin antiserum and secondary antibody samples, followed by electrochemical signaling via an immunoprecipitation reaction by the label enzyme. Under the optimized affinity-surface construction steps and reaction conditions, both types of microfabricated electrodes exhibited well-defined calibration results as a function of the protein concentration in antiserum samples. Furthermore, circular-type micropatterned immunoelectrodes exhibited voltammetric characteristics of microelectrodes, which is advantageous in terms of sensor operation under a fixed potential and low signal drift during the signaling reaction compared with the bulk-type electrodes. The results support that the employed signaling method with the proposed immunosensor configuration is fit for sensor miniaturization and integration to future biomicrosystems.
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PMID:Ferritin immunosensing on microfabricated electrodes based on the integration of immunoprecipitation and electrochemical signaling reactions. 1547 31

Cavities formed by proteins have been utilized as the reaction chamber for the fabrication of a range of inorganic nanoparticles, providing control of the size of particles by limiting growth and preventing agglomeration. In crystal form, proteins construct molecular arrays that can provide regularly arranged sites for nanoparticles. Here we report the fabrication of nanometric iron and indium particles using ferritin, an iron-storage protein. The indium nanoparticles thus formed have uniform spherical shape with diameter of 6.6 +/- 0.5 nm, while the iron nanoparticles are somewhat irregular in shape (5.8 +/- 1.0 nm). Regular two-dimensional arrays of these nanoparticles are successfully produced by crystallizing ferritin molecules on a water-air interface using the denatured protein film method. The lattice constant of these nanoparticle arrays is 13 nm with hexagonal packing, and arrays of more than 1 microm in area can be obtained by transfer onto silicon wafer.
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PMID:Self-organized inorganic nanoparticle arrays on protein lattices. 1588 8

We demonstrated the fabrication of size-controlled two-dimensional iron oxide nanodots derived from the heat treatment of ferritin molecules self-immobilized on modified silicon surfaces. Ferritin molecules were immobilized onto 3-aminopropyltrimethoxysilane (3-APMS)-modified silicon surfaces by electrostatic interactions between negatively charged amino acids of ferritin molecules and amino terminal functional groups of 3-APMS. Heat treatments were performed at 400 degrees C for 60 min to fabricate two-dimensional nanodots based on ferritin cores. XPS and FT-IR results clearly indicate that ferritin shells were composed of amino acids and 3-APMS modifiers on silicon surfaces were eliminated by heat treatment. Nanodots on substrate surfaces corresponded to iron oxides. The size of nanodots was tunable in the range of 0-5 (+/-0.75) nm by in situ reactions of iron ion chelators with ferritin molecules immobilized on substrates before heat treatment.
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PMID:Size control for two-dimensional iron oxide nanodots derived from biological molecules. 1655 58

We report herein the fabrication of ferritin-embedded self-supporting silica nanofilms via a simple spin-coating process. Ferritin was employed as a template molecule, and solutions of ferritin and silica were spread on a polymer-coated silicon substrate, in this order. After dissolving the polymer underlayer by simply immersing ethanol, a centimeter-sized self-supporting nanofilm of ferritin/silica composite with a thickness of 15 nm was successfully transferred onto an alumina membrane without the film breaking. Ozone and hydrochloric acid solution treatment removed the template ferritin molecules from the composite film to produce corresponding transmembrane nanoholes. The reported method is very simple, and the fabrication of a protein-embedded self-supporting nanofilm enables the design of biomembrane-mimetic devices.
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PMID:Embedding of individual ferritin molecules in large, self-supporting silica nanofilms. 1732 67

A patterned two-dimensional hexagonally ordered array of ferritin molecules, the outer surfaces of which had been genetically modified by titanium (Ti) specific binding peptides (minT1-LF), was realized in a self-assembling manner on a hexagonal Ti thin film island made on a silicon substrate. The optimum degree of order was realized at the pH with the maximum selectivity of minT1-LF adsorption on the Ti surface with respect to the silicon dioxide (SiO2) surface. Quartz crystal microbalance (QCM) measurement revealed that minT1-LF adsorbed onto the Ti surface strongly and irreversibly, but adsorbed onto the silicon dioxide surface weakly and reversibly. It was suggested that the concentration of minT1-LF on the Ti pattern promotes hexagonal close-packed ordering and axis aligning.
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PMID:Hexagonal close-packed array formed by selective adsorption onto hexagonal patterns. 1922 85

Individual water-soluble molecules of the protein ferritin have been imaged on a silicon surface in pure water at room temperature with the atomic force microscope (AFM). The ferritin molecules formed an ordered monolayer by binding to a charged polypeptide monolayer of poly-1-benzyl-L-histidine (PBLH) spread at the air-water interface. The film, fully wetted with water, was horizontally transferred onto an alkylated silicon wafer for AFM imagings. The hexagonal arrangement of ferritin molecules was imaged with high reproducibility on the whole surface of the film, since the forces between cantilever and the sample could be kept sufficiently smaller than 10(-10) N, mainly due to a "self-screening effect" of the surface charges of the ferritin-PBLH layer. This is the first observation of two-dimensional ordered arrays of water-soluble protein molecules directly confirmed by AFM with molecular resolution.
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PMID:Imaging the ordered arrays of water-soluble protein ferritin with the atomic force microscope. 1943 59


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