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)

The authors reported on a three month long EPREX (human recombinant erythropoietin) therapy of 5 hemodialysis patients for the treatment of their anemia. The drug was administered in bolus form 2 or 3 times a week after dialysis in a dose of 50 to 150 IU/bodyweight increased gradually in every (or every second) week. Hgb ad Htk values were determined once a week while erythrocyte, leukocyte, thrombocyte and reticulocyte count once a month. Serum iron, TIBC, serum ferritin, BUN, serum creatinine, urea, serum ions, liver function assays, serum lipids and amylase were also established. Hgb, Htk levels and reticulocyte count have significantly increased in the 4th week of treatment already, severe anemia ceased with improved appetite, general condition and physical strength. Serum urea and LDH levels significantly increased while SGOT decreased. No significant change in leukocyte and thrombocyte count, serum Na, K, Ca, P, Cl, BUN, creatinine, total protein level, serum albumin, bilirubin, alkaline phosphatase, GGT, GPT, amylase and blood sugar as well as serum lipid level were observed. No adverse reactions occurred during the treatment. After the three gradually decreased and within 6 weeks they had to be transfused again. In three patients the need for transfusion has significantly grown after the treatment. The authors consider EPREX a highly efficient drug in the treatment of anemia in dialysis patients.
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PMID:[Recombinant human erythropoietin in the therapy of anemia in hemodialyzed patients]. 223 36

The interactions between dialyzable transfer factor and antigens have been studied. Incubation of transfer factor-containing dialysates from ferritin-sensitized mice or ferritin-coated plastic surfaces removed the antigen-sensitizing activity; incubations of the same preparations on cytochrome c-coated surfaces did not. Similar results were obtained when cytochrome c-transfer factor was studied. Incubation on cytochrome c-coated surfaces removed the activity, but incubation on ferritin-coated surfaces did not. Specific transfer factor activities could be recovered by elution with 8 M urea or acetonitrile. The finding of interactions between transfer factor and antigens provides evidence for a molecular basis of the specificity of the immunologic effects of transfer factor. This technique may also enable us to obtain amounts of specific material that are adequate for chemical analysis.
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PMID:Murine transfer factor. III. Specific interactions between transfer factor and antigen. 241 95

Three monoclonal antibodies against human liver ferritin were selected to study antigenic determinants (epitopes) of human isoferritins. These monoclonal antibodies were found to form immunoprecipitin lines with ferritin in double diffusion tests (Ouchterlony), indicating multiple epitopes on a single ferritin molecule. The antibodies revealed high species specificity as well. Monoclonal antibodies MA301 and MA311 appeared to recognize different epitopes, since they did not inhibit each other in competitive enzyme-linked immunosorbent assay (ELISA). However, MA309 recognized both epitopes for MA301 and MA311 with similar competitive inhibition. These epitopes were not detectable when ferritin was treated with 8M urea (pH 2.5) and were detectable upon reconstruction by dialysis against 2 M urea (pH 7.2), suggesting that these monoclonals recognize epitopes in the tertiary structure of the ferritin molecule. As a matter of fact, these monoclonals react preferentially with intact ferritin molecule and only negligibly with subunits. Isoelectric focusing patterns of human ferritins demonstrated that liver, spleen, placenta, and hepatoma cells (Li-7) transplanted in nude mice contained basic isoferritins, whereas HeLa cells (carcinoma), Wa cells (EB virus-transformed B cells), and Raji cells (Burkitt's lymphoma) contained acidic isoferritins. Human heart ferritin displayed a somewhat intermediate pattern between liver and HeLa ferritins. In spite of the heterogeneous population of human isoferritins, the dissociation constants (Kd) of the three monoclonal antibodies to liver, HeLa, and heart isoferritins were quite similar.
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PMID:Common epitopes in human isoferritins characterized by murine monoclonal antibodies. 242 Jul 86

The authors studied the in vitro permeability of different fragments of the rabbit's peritoneum to urea, inulin, horseradish peroxidase, and ferritin. Parietal peritoneum has a lower permeability to middle and large molecules than visceral peritoneum. In addition the local anesthetic, bupivacaine had a different effect on the mesothelial permeability of visceral peritoneum than on that of parietal peritoneum.
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PMID:Permeability of different parts of the peritoneal mesothelium to solutes: an in vitro study. 248

The iron-storage protein ferritin was found to be associated with highly purified coated vesicles (CV) from chicken liver. Chicken liver ferritin was morphologically similar to ferritin from horse spleen and could be isolated using a specific anti-ferritin monoclonal antibody. This antibody recognized a 240 X 10(3) Mr form of chicken ferritin but not the 22 X 10(3) Mr ferritin subunit after protein transfer to nitrocellulose. CV purified by controlled-pore glass-bead chromatography also contained ferritin when assayed by monoclonal anti-ferritin antibody using a sensitive enzyme-linked assay. Ferritin remained associated with CV even after re-chromatography. Ferritin particles were observed to be associated with CV by electron microscopy. CV-associated ferritin could be quantitatively removed from CV by treatment of the CV with 0.5 M-Tris-HC1 + 2M-urea at pH 8.5, conditions that also lead to dissociation of the clathrin lattice. Triton X-100 detergent treatment did not affect the association of ferritin with CV. These results indicate that purified CV from chicken liver contain ferritin in association with the clathrin lattice. The possible functional significance of this association is discussed.
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PMID:Coated vesicles from chicken liver bind ferritin. 277 20

Three hundred and seventy-three female and 213 male nonalcoholic subjects, aged 60-100 y, who had participated in a nutritional status survey of elderly people in the Boston area were grouped according to usual alcohol intake: 0-4, 5-14, or 15+ g/d. The age- and sex-adjusted mean intake of calories, fat, protein, carbohydrate, and 10 micronutrients and the mean levels of 14 nutrient and 22 nonnutrient biochemical indices were compared for the three categories of alcohol intake. The mean micronutrient intakes were also adjusted for total caloric intake and the mean nutrient biochemical concentrations were also adjusted for the corresponding nutrient intakes. The results suggest that caloric intake and blood concentrations of retinol, iron, ferritin, HDL cholesterol, AST, and ALT increased with increasing alcohol intake whereas folate and phosphorus intakes and blood measures of riboflavin, copper, zinc, urea nitrogen, and creatinine decreased with increasing alcohol intake.
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PMID:Moderate alcohol intake and nutritional status in nonalcoholic elderly subjects. 280 94

To examine the mechanism by which prostaglandin E2 (PGE2) inhibits the development of apoferritin (HAF)-induced immune complex glomerulonephritis (ICGN), weekly determinations of glomerular histologic conditions, blood urea nitrogen (BUN), total immunoglobulin levels, anti-HAF antibody, peripheral blood and splenic T cell subsets, and splenic suppressor cell activity were compared between mice receiving HAF and mice additionally treated with PGE2. PGE2 therapy prevented the development of glomerular hypercellularity and the increase in BUN concentration. Administration of PGE2 reduced anti-HAF IgG levels, but total IgM and IgG1, IgG2a, and IgG2b levels were unchanged. Mice receiving HAF alone demonstrated serial reductions in phenotypically identified peripheral blood pan-T cells and suppressor-cytotoxic T cells. PGE2-treated mice maintained normal levels of peripheral blood T cell subsets. Significant reductions in splenic total T cells and suppressor-cytotoxic cells occurred in mice receiving HAF as compared with normal mice. This reduction was offset by an increase in splenic B cells. PGE2 therapy prevented the decrease in splenic T cells at week 1, but not at week 4. Nonspecific suppressor cell activity, as measured by the ability of spleen cells from experimental mice to suppress a mixed lymphocyte reaction (MLR) or to suppress MLR-induced polyclonal IgG synthesis, was not different between the two groups. We conclude that prevention of HAF-ICGN by PGE2 is associated with a reduction in nephritogenic antibody production without an alteration in total immunoglobulin synthesis or the generation of nonspecific suppressor T cells. Changes in the percent of peripheral blood and splenic T cells and B cells may represent an effect of PGE2 on antigen-stimulated B cell proliferation.
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PMID:Serial changes in humoral and cellular immunity induced by prostaglandin E2 treatment of murine immune complex glomerulonephritis. 293 13

Several polycations added to the luminal solution were found to inhibit the vasopressin (ADH)-induced water flow in toad urinary bladder but not the ADH-induced increase in sodium transport or in urea permeability. Ultrastructural studies were conducted to evaluate the uptake of cationized ferritin. It was found that endocytosis of cationized ferritin by luminal cells was strikingly enhanced on exposure to ADH; this increased endocytosis was concomitant with inhibition of transepithelial ADH-induced water flow. Various maneuvers preventing endocytosis were also found to counteract the polycation-induced inhibition of the ADH effect. It is suggested that polycations are endocytosed in vesicles whose walls contain the water channels but not the urea or sodium channels.
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PMID:Polycations reduce vasopressin-induced water flow by endocytic removal of water channels. 301 Jul 30

Proteodermatan sulfate was isolated from the skin of human, female breast in 6-M urea and proteolytic inhibitors at 70 degrees C and purified on Sephacryl S-200. It was composed of 55% protein and 45% dermatan sulfate, displayed one protein and carbohydrate-stainable band on agarose-polyacrylamide gels, yielded dermatan sulfate after digestion by papain, and its calculated E0.1% 1 cm, 280 nm was 16.2. Its mucopolysaccharide portion was digested by chondroitinase ABC but not by chondroitinase AC. This proteoglycan was used to immunize rabbits. Double diffusion of antiserum against the antigen or its core protein resulted in one precipitation band. Antiserum did not cross-react with bovine collagen type I, human fibronectin, dermatan sulfate, hyaluronic acid, heparin, heparan sulfate or the chondroitin sulfates by double diffusion. The antiserum titer determined by radioimmunoassay was 1:16,000. This assay was not affected by a 40-fold excess of dermatan sulfate. Purified IgG molecules were apparently associated with collagen in human breast mid-dermis as demonstrated by indirect immunoelectron microscopy with ferritin-labeled goat antirabbit IgG. The results indicate that rabbit anti-human, anti-proteodermatan sulfate IgG is highly specific for the core protein of dermatan sulfate and confirm the hypothesis that in vivo proteodermatan sulfate is closely associated with collagen.
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PMID:Immunoelectron microscopy of proteodermatan sulfate in human mid-dermis. 315 40

Three purported means by which large solutes may penetrate the blood-brain barrier are: permeabilized tight junctions; vesicular transport; or channel formation across cerebral blood vessels. The role of vesicular transport has been questioned, in part, because many cytoplasmic vesicles are induced by aldehyde fixation. Cryofixation reduces this artefact and was used to see structural changes in frog cerebral endothelium made permeable to plasma solutes after perivascular exposure to hyperosmotic (3 M) urea, or injury with a cold probe (-50 degrees C). Some control and experimental frogs were made hypothermic so as to inhibit endocytosis and autolytic changes. The brains of some untreated controls were immerse-fixed in aldehydes. Other controls and all other brains of normothermic or hypothermic animals were rapidly frozen, then substituted with acetone-fixative. The interendothelial tight junctions separate partially or completely, after hyperosmotic exposure, in one third of the junctions. Blood-borne ferritin and Evans blue pass through some of the patent junctions. Junctional opening is caused by cell shrinkage, because the perimeter/area ratio of individual endothelial cells in the hyperosmotic group is significantly greater than in the control, due to a decreased area. Large 0.08-0.32-micron-wide invaginations or pits of the endothelial cell membrane characterize both cryofixed and aldehyde-fixed vessels. The pits often appear as isolated vesicles in the cytoplasm, but serial sections reveal that many communicate with either the capillary lumen or subendothelial space. No series of pits opened onto both lumen and space to form a transendothelial channel. The number of vesicles in aldehyde-fixed specimens is about 4 times greater (P less than 0.01) and in the cold injured, cryofixed brain capillary, about two times greater (P less than 0.01), than in the cryofixed control. Hyperosmotic exposure does not increase the number of pits. The permeabilization of anuran cerebral endothelium by hyperosmotic treatment or cold injury is thus by means of an intercellular rather than a transcellular route.
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PMID:Cerebral vessels cryofixed after hyperosmosis or cold injury in normothermic and hypothermic frogs. 325 81


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