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)

An immunoperoxidase staining technique was used for detecting three major iron-binding proteins (transferrin, ferritin, and lactoferrin) in routine histological paraffin sections of human tissue. Transferrin was found mainly in hepatocytes, a variety of epithelial and myoepithelial cells, renal tubular cells, and histiocytes. Ferritin was most readily found in histiocytes and liver cells, with weaker reactions seen in epithelial cells. Lactoferrin was found in lactating breast tissue, bronchial glands, polymorphs, and gastric and duodenal epithelial cells. The technique is potentially valuable for investigating abnormal iron states.
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PMID:Distribution of transferrin, ferritin, and lactoferrin in human tissues. 34 12

Antibodies from a cow with an experimentally induced infection of the Pawhuska isolate of bovine anaplasmosis were conjugated with ferritin and used to label antigenic sites in preparations of parasitized erythrocytes. Intact erythrocytes did not label on the extracellular surface. Ferritin-conjugated antibody did not pass through the intact erythrocyte to label the parasite, probably due to the large molecular size of the antibody. Damage to erythrocytic plasmalemma and inclusion body in the hemolyzed erythrocytes and complement-fixation antigen allowed labeling of anaplasmal inclusion structures. The positively labeled structures were outer surface of the pellicle, chromatin of the initial body, and inclusion appendage. Unlabeled structures included inner organismic membrane of the initial body, inclusion membrane, fibrillar protoplasmic network of the initial body, and small electron-dense bodies derived from the initial body.
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PMID:Ultrastructural localization of anaplasmal antigens (Pawhuska isolate) with ferritin-conjugated antibody. 35 35

Kinetic studies on the uptake and elimination of ferritin and ferritin-protein conjugates in the rat glomerular mesangium are reported. Ferritin was prepared from horse spleens and conjugates were prepared using either human IgG or albumin. The degree of mesangial uptake was dose dependent and a competitive effect with the reticuloendothelial system was observed. Maximal mesangial fluorescence occurred at a lower dosage with conjugate than with native ferritin. In addition, conjugate persisted for months within the mesangium as compared to a matter of days in the case of ferritin alone. The disappearance of native ferritin from the mesangium paralleled that seen in the circulation. Conjugate, however, disappeared far more rapidly from the circulation than from the mesangium. At a point in time when the mesangium still contained conjugate but the blood was negative, rabbit antiserum to ferritin was injected and was observed to deposit in the mesangium. This demonstrated the accessibility of mesangially sequestered antigen to circulating antibody. This system provides a model for long term studies on the effect of immune reactions occurring in the mesangium.
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PMID:Comparison of the handling of ferritin and ferritin-protein conjugates by the glomerular mesangium: kinetic studies in the rat. 36 34

Strains representing each of the five serologically distinct types of group B Streptococcus and variant strain 090R, which is devoid of type-specific polysaccharide, were studied by electron microscopy after incubation with various ferritin-conjugated antibodies. Ferritin-conjugated types Ia, II and III antibodies localized on homologous cells in a pattern that defines the capsular location of the type Ia, II, and III polysaccharide antigen. Type Ib and Ic cells have surface antigens to which ferritin-labeled antibodies to both capsular polysaccharide and a common surface protein attach.
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PMID:Electron microscopic definition of surface antigens of group B Streptococcus. 37 41

Ferritin is an iron storage protein of high-molecular weight which is primarily present in the liver, spleen, and bone marrow. A very sensitive immunoradiometric assay has been developed which permits determination of serum concentrations in normal persons and in patients with a variety of different disorders. In normal subjects, the serum ferritin concentration correlates very well with total body iron stores as measured by phlebotomy. The serum ferritin concentration is reduced in patients with iron-deficient anemia and is significantly higher in patients who are anemic for other reasons. Subject areas discussed in this review include the details of the immunoradiometric procedure, the sensitivity and accuracy of the assay, factors influencing the assay, values characteristic of a variety of clinical disorders, and the utility of the assay in clinical medicine and public health.
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PMID:Serum ferritin assay. 40 69

Kidney extract and synthetic angiotensin II were injected into bilaterally nephrectomized rats in dosages capable of raising the mean arterial pressure by about 20 mmHg. Changes in ultrastructure and permeability for ferritin molecules were then examined in capillaries located in muscularis layer of the intestinal walls. Kidney extract with a high renin content was obtained from the renal cortex of rats by means of stepwise centrifugation methods. Animals injected with saline served as controls. In rats receiving kidney extract tissue edema was observed in the spaces around the blood and lymphatic capillaries. In these spaces ferritin molecules accumulated in high concentration indicating plasma protein leakage. Ferritin molecules within the endothelium were restricted within plasmalemmal vesicles, but were not found within interendothelial junctions or within the cytoplasmic matrix. Morphometric analysis of vesicular transport in the endothelial cells revealed a significant increase in labeling rate for the vesicles with ferritin molecules. These results suggest that the kidney extract contains substance(s) which increase capillary permeability for plasma proteins at least via increased vesicular transport, resulting in tissue edema.
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PMID:Increased capillary permeability in muscularis layer of rat intestine caused by kidney extract. 41 15

Spontaneously breathing mice were exposed to an aerosol of iron oxide for 3 hours. Participation of the tracheal and bronchial epithelium in the uptake of iron oxide was noted immediately following the exposure and at 1 day, 4 days, and 7 days postexposure. Observations with the electron microscope revealed that iron oxide was pinocytosed and converted to ferritin and hemosiderin in all epithelial cell types except mucous cells. Iron content increased over time and approximately 50% of the nonmucous cells contained hemosiderin by 4 days postexposure. Ferritin and hemosiderin, but not iron oxide, were noted in connective tissue cells in the submucosa beneath the airway epithelium. Soluble iron and/or ferritin produced in the airway epithelial layer was transported to the submucosa, but normal epithelium prevented the penetration of deposited iron oxide particles to the connective tissue compartment.
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PMID:Uptake of iron aerosols by mouse airway epithelium. 43 Oct 45

The immunochemical method has been proposed to indicate the adenin compounds in isolated myofibrils of striated muscle. Adenosine--containing antigen was prepared by coupling adenosine with bovine serum albumin (adenosine--BSA). Antibodies against adenosine--BSA were labelled by ferritin. The sites of the antigen antibody reaction were marked by localization of ferritin molecules. Ferritin antibodies were found to concentrate in the following sarcomere sites: M and Z bands, N-lines and terminal cisternae of sarcoplasmic reticulum near the Z-bands.
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PMID:[Localization of adenine components in chick myofibrils by the ferritin antibody technic]. 43 20

Lysosomal fraction of renal cortical extract, which showed high renin activity, and equipressor dosis of synthetic angiotensin II amide were administered into one-hour nephrectomized rats. Sixty minutes after the sustained elevation of 20 mmHg in mean arterial pressure by each pressor substance, the rats were sacrificed and the intraperitoneal organs were fixed. Five minutes prior to the administration of each pressor substance ferritin solution, as a test substance for vascular permeability, was intravenously injected. Medial changes in the arterioles in the intestinal submucosa were observed by electron microscopy. In angiotensin II group early lytic lesions of the muscle cells were limited to the single muscle cells. Ferritin particles were rarely found in the media. In lysosomal fraction group the lytic lesions were more advanced. Some regions of the media exhibited focal loss of smooth muscle cells manifesting focal medial necrosis. Ferritin particles were distrubuted in some areas of the necrotic media. The results suggested that the kidney extract with high renin content contained substance(s) to produce both medial necrosis and plasma insudation into the media of the arterioles.
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PMID:Acute arteriolar lesions of rat intestine caused by kidney extract. 44 11

We report our evaluation of a commercially available procedure and reagents for determination of ferritin in serum by enzyme-labeled immunosorbent assay (ELISA). Results by our procedure and the "Fer Iron" (Ramco Labs) procedure shows a degree of association (r) of 0.95 and a regression equation of y = 1.03x - 33. Similarly, our procedure compared to the "Gamma Dab" (Clinical Assays) ferritin procedure shows a degree of association of 0.98 and a regression equation of y = 0.93x - 11. Between-day standard deviations were 6 and 22 micrograms/L (n = 24 and 20) for ferritin concentrations of 20 and 300 micrograms/L, respectively. Ferritin values showed no correlation with total iron concentration, but show a broad inverse relationship with iron-binding capacities. The favorable correlation with existing procedures and the speed of the analysis commend the use of ELISA for measurement of ferritin in serum.
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PMID:Enzyme-labeled immunosorbent assay for serum ferritin: method evaluation and comparison with two radioassays. 45 88


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