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)

In the present state of our knowledge it must be concluded that the outstanding anatomic changes directly attributable to acute iron poisoning are in the gastrointestinal tract and the liver. Both seem to be due to the direct action of iron upon living cells. In the stomach and small bowel the changes appear to be due to the corrosive effect of the iron salt whether in solution or in tablet form. And the anion may indeed play the predominant role as demonstrated by the observation of the severe corrosive changes observed when accumulations of ferrous sulfate tablets occur in areas of the stomach or small bowel. That the mucosal barrier to iron is broken down seems incontrovertible. And it is no longer tenable to assume that the severe complications of iron poisoning are due to the local necroses in the gastrointestinal tract. The liver, being the first parenchymal organ encountered by absorbed iron, is involved to a varying degree. The anatomic changes can progress to frank necrosis in severe cases. And even in those where overt histologic damage is not demonstrable, alterations in biochemical function occur. Anatomic changes in other parenchymal organs are probably largely secondary to dehydration, shock, hemorrhage, and infection. But the possibility of disordered enzyme systems here as well must be borne in mind though so far not demonstrated. In severe cases where hemorrhages play so large a role, albeit infrequently, the specific action of iron in interference with coagulation mechanisms is of the utmost importance. The role of therapy with deferoxamine in production of shock is discussed below. In this connection breakdown of the mucosal barrier with release of apoferritin and ferritin as a hypotensive mechanism has also been suggested by Smith.
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PMID:Iron poisoning in children. 122 66

Patients with Hb SC disease were found to have microcytic and hyperchromic red cell indices despite mild reticulocytosis. Iron deficiency anemia was ruled out by the finding of normal serum ferritin levels. In order to determine whether the microcytosis was due to coexistent alpha-thalassemia, restriction endonuclease mapping was performed on genomic DNA extracted from peripheral blood leukocytes. Patients with Hb SC disease had microcytic indices despite the presence of a full complement of four alpha-genes (alpha alpha/alpha alpha), suggesting that the microcytosis may be due to cellular dehydration (or xerocytosis), since the mean corpuscular hemoglobin concentration in Hb SC disease patients was significantly higher than in controls. This possibility was investigated further by the determination of RBC cation content. RBC Na levels were similar in SC and normal red cells. Hb SC RBCs, however, had significantly reduced K levels. These findings show that RBC cation content, and thus cell water, is decreased in Hb SC disease. The decreased RBC K level in the presence of normal cellular Na concentration suggests selective K loss that is not due to inhibition of the Na K pump. Ouabain-insensitive K+ efflux was increased to four times normal in SC cells. Cell dehydration was confirmed by the demonstration of increased high-density RBCs on discontinuous Stractan density gradients and by osmotic gradient ektacytometry. Cellular dehydration and its sequelae were worse in CC erythrocytes and milder in AC cells than in Hb SC red cells. Taken together, these data indicate that in Hb SC disease the RBCs are severely dehydrated and typically microcytic and hyperchromic. Hb SC RBCs seem to be dehydrated due to selective K loss. These findings suggest a functional interrelationship between Hb SC, the red cell membrane, and cation regulation.
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PMID:The xerocytosis of Hb SC disease. 294 42

A general method for the ultrastructural localization of intracellular proteins and antigens by immunoferritin techniques has been developed. The method involves direct staining of ultrathin sections of mildly glutaraldehyde-fixed and frozen tissues cut by means of a cryo-ultramicrotome. Bovine pancreatic sections were cut, mounted on grids, and stained with ferritin-rabbit antibovine RNase conjugates. After negative staining with 0.2% phosphotungstic acid, electron micrographs revealed specific labeling of all of the zymogen granules and the cisternae of the rough endoplasmic reticulum. No significant labeling was seen in the nucleus, mitochondria, or cell sap regions. The observation that no significant labeling was found in any region of rat pancreatic sections was consistent with the fact that rat RNase is immunologically non-crossreactive with bovine RNase. In addition, the labeling seen in bovine pancreas was completely absent if the sections were first incubated with free antibody. The method used here avoids prolonged fixation, dehydration, and other harsh chemical or physical treatments, and should extend the usefulness of immunoferritin techniques to the intracellular localization of many protein antigens beyond previously available methods.
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PMID:Immunoferritin localization of intracellular antigens: the use of ultracryotomy to obtain ultrathin sections suitable for direct immunoferritin staining. 412 4

A method is described for performing postembedding staining of protein (immunoglobulin) antigen embedded in styrene-methacrylate resin. Fixation of specimens in a combination of 4% paraformaldehyde and 0.2% picric acid and washing in buffer containing 7% sucrose, followed by abrupt dehydration with absolute acetone in the cold preserved the antigenicity, although in a masked form. The masked antigenicity could be reexposed by treatment with nonspecific protease. Staining with fluorescent-, peroxidase-, or ferritin-labeled antibodies on semi- and ultrathin sections resulted in specific localization of the antigen. We applied this technique to the localization of rabbit immunoglobulin in specimens of renal tissue obtained from rats with anti-glomerular basement membrane nephritis; we also localized human IgG in a renal biopsy specimen. The prerequisites for recovery of antigenicity are such that preservation of tissue structure at the light microscopic level is good, but relatively poor at the electron microscopic level.
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PMID:An approach to postembedding staining of protein (immunoglobulin) antigen embedded in plastic: prerequisites and limitations. 615 34

The preservation and contrast of membranous structures in cultured cells using various postfixation procedures prior to embedding have been investigated. These include routine OsO4, ferrocyanide-reduced OsO4, osmium-thiocarbohydrazide-osmium (OTO), and ferrocyanide-reduced osmium-thiocarbohydrazide-ferrocyanide-reduced osmium (R-OTO). With standard ethanol-Epon dehydration/embedding techniques, a dramatic improvement in both membrane contrast and preservation of bilayer membrane structure was achieved using preembedding OTO in cultured cells. R-OTO yielded similar enhanced preservation and contrast of membranes. Both of these methods also resulted in an increase in the contrast of diaminobenzidine reaction product from horseradish peroxidase activity, and of lipid droplets and lipoprotein particles. However, R-OTO did not cause the same increase in the density of proteinaceous elements as was seen with the OTO method. Ferrocyanide-reduced osmium alone showed significant advantages for quantitation of immunocytochemistry using ferritin labels with bismuth subnitrate counterstain. These methods should have general usefulness for the preservation of lipid-containing structures in cultured cells.
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PMID:The use of osmium-thiocarbohydrazide-osmium (OTO) and ferrocyanide-reduced osmium methods to enhance membrane contrast and preservation in cultured cells. 632 74

Lowicryl K4M (K4M) was recently introduced as an embedding medium for immunocytochemistry at the electron microscope level (BL Armbruster, E Carlemalm, R Chiovetti, RM Garavito, JA Hobot, E Kellenberger, W Villiger (1982):J Microsc 126:77 and E Carlemalm, M Garavito, W Villiger (1982):J Microsc 126:123). While earlier protocols of fixation and embedding required 4-6 days, the present method has reduced the processing time by accelerating both dehydration of tissues and polymerization of K4M so that tissues can be prepared for sectioning within 4 hr. The immunocytochemical labeling density was quantitated in order to determine relative antigen preservation in tissues embedded by the accelerated protocol as compared to slower K4M embedding techniques and to tissues embedded in glutaraldehyde-cross-linked bovine serum albumin (BSA). Thin sections of Bufo marinus kidney were labeled with rabbit antibody to Na+,K+ATPase alpha chain catalytic subunit isolated from B. marinus kidney microsomes (M Girardet, K Geering, JM Frantes, D Geser, BC Rossier, JP Kraehenbuhl, C Bron (1981):Biochemistry 20:6684). B. marinus retinas were labeled with rabbit anti-opsin. After fixation in paraformaldehyde(3%)-glutaraldehyde(3%), tissues were washed in buffer, dehydrated in 50, 75, and 90% dimethyl-formamide (DMF, 10 min each); K4M:DMF, 1:2 (15 min); K4M:DMF, 1:1, (20 min); K4M (25 min); K4M (30 min) at room temperature and transferred in fresh K4M to BEEM capsules for exposure to ultraviolet light (GE 15 watt, Black-lite, 10 cm, 45 min or less) at 4 degrees C. Thin sections were labeled successively with antibody, biotinylated sheep anti-rabbit F(ab')2 and avidin-ferritin. Ferritin labeling densities were determined by point counting. High labeling densities were observed with both antibodies, equaling or exceeding levels of labeling by slower protocols or embedment in BSA.
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PMID:Rapid embedding of tissues in Lowicryl K4M for immunoelectron microscopy. 643 66

Birds have evolved alternate physiologic strategies to contend with dehydration, starvation, malnutrition, and reproduction. Basic anatomic and functional differences between birds and mammals impact clinical chemistry values and their evaluation. Interpretation of the results of standard biochemical analyses, including BUN, alanine aminotransferase, aspartate aminotransferase, creatine kinase, gamma glutamyltransferase, bilirubin, ammonia, alkaline phosphatase, cholesterol, bile acids, glucose, albumin, globulins, calcium, phosphorus, prealbumin (transthyretin), fibrinogen, iron, and ferritin, is reviewed and discussed in relation to these physiological differences. The use and interpretation of alternative analytes appropriate for avian species, such as uric acid, biliverdin, glutamate dehydrogenase, and galactose clearance, also are reviewed. Normal avian urine and appropriate use of urinalysis, an integral part of laboratory diagnosis in mammalian species that frequently is omitted from avian diagnostic protocols, is discussed.
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PMID:Clinical chemistry of companion avian species: a review. 1218 2

A paucity of literature exists with regard to research on nutrition for the pediatric athlete. This lack of research makes the development of specific nutritional recommendations for young athletes problematic. This issue is made difficult by the macro- and micronutrient intake required for growth and development in conjunction with that required for sports. Exogenous carbohydrate drinks could be considered for the young athlete engaged in both endurance exercise and high-intensity exercise. Monitoring of the energy intake during resistance training in the pediatric athlete needs to be considered, as there is evidence to suggest that energy deficits may occur. If decrements in exercise performance are noted, then serum ferritin and hemoglobin concentrations should be monitored, as nonanemic iron deficiency is prevalent in the pediatric athlete. The pediatric athlete exercising in the heat is susceptible to voluntary dehydration and evidence exists to suggest that a carbohydrate-electrolyte drink will abolish this phenomenon.
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PMID:Nutrition for the pediatric athlete. 1523 Dec 24

This study was performed to examine the effect of diurnal normobaric hypoxia on hematological parameters. Eleven healthy male volunteers were randomly selected to be in either the hypoxic group (n=6) or the control group (n=5). The hypoxic group was exposed to 8 h of normobaric hypoxia in hypoxic tent systems that elicited a target peripheral O(2) saturation of 81+/-2% on three consecutive days. The control group spent three consecutive 8-h days in modified tent systems that delivered normoxic air into the tent. Venous blood samples were collected before the exposure (days -5, 0), after each day of the exposure (days 1, 2, 3), and for 3 weeks after the exposure (days 7, 10, 13, 17, 24). Serum erythropoietin concentration significantly increased from 9.1+/-3.3 U.L(-1) to 30.7+/-8.6 U.L(-1) in the hypoxic group. Although there were significant increases in hematocrit (4%), hemoglobin concentration (5%), red blood cell count (4%) on day 7 in the hypoxic group, these observations were likely due to dehydration or biological variation over time. There was no significant change in early erythropoietic markers (reticulocyte counts or serum ferritin concentration), which provided inconclusive evidence of accelerated erythroid differentiation and proliferation. The results suggest that the degree of hypoxia was sufficient to stimulate increased erythropoietin production and release. However, the duration of hypoxic exposure was insufficient to propagate the erythropoietic cascade.
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PMID:Diurnal normobaric moderate hypoxia raises serum erythropoietin concentration but does not stimulate accelerated erythrocyte production. 1716 62

An emerging nanofabrication technology is to synthesize nanoscale inorganic materials with narrow size distribution using biological systems, which are size-constrained, fairly robust, and easily removable. Apoferritin, a spherical and hollow protein complex, was subjected to atomic layer deposition of TiO(2). The growth of TiO(2) on the protein surface was investigated as a function of the precursor exposure and purge length. Thermal pretreatment and osmotic dehydration lead to controllable deposition both on the outer surface and within the inner cavity of apoferritin. Depending on the experimental conditions, either hollow spherical nanoparticles or core-shell nanoparticles comprising TiO(2) were identified.
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PMID:Titania nanostructures fabricated by atomic layer deposition using spherical protein cages. 1992 35


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