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)

Small nuclear ribonucleoprotein particles (snRNPs) were identified in nuclear sonicates of Novikoff hepatoma ascites cells and in intact Novikoff hepatoma and PtK2 cells by immunofluorescence and immunoelectron microscopy. Auto-antibodies (anti-Sm and anti-RNP) obtained from patients with systemic lupus erythematosus an autoimmune disease, were used to localize snRNP particles. The Sm antibody is specific for U1, U2, U4, U5 and U6 containing snRNPs. The RNP antibody is specific for only U1 containing snRNPs. Isolated particles, 120 +/- 10 A in diameter, were found to be associated with ferritin-conjugated goat anti-human antibodies coupled to Sm antibodies. In addition, these particles (snRNPs) were occasionally associated with larger particles measuring 230 +/- 10 A in diameter which are presumed to be hnRNP particles. Double label immunofluorescence and immunoelectron microscopy have shown Sm and RNP antibodies to colocalize in PtK2 cells. However, the perinucleolar chromatin and juxtanuclear envelope chromatin was devoid of RNP immunostaining. Therefore, U1 containing snRNPs do not appear to be in these regions. The Sm antibody localizes in a nuclear network including the perinucleolar chromatin and juxtanuclear envelope chromatin. Cells treated with the drug DRB (5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole), which inhibits hnRNA synthesis, show an altered pattern of Sm immunostaining. Such cells contain large clusters of snRNPs which do not extend to the perinucleolar chromatin or perinuclear lamina chromatin. Nuclear matrix preparations maintain an snRNP nuclear network as visualized by Sm immunofluorescence. It is notable that the size and density of the immunostained particles in the nuclear network during interphase, is similar to that of interchromatinic granules.
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PMID:Immunoelectron microscopic localization of snRNPs. 623 Jan 27

1. The iron contents, gel migration rates and isoelectric-focusing patterns of normal liver and hepatocellular carcinoma ferritins from the same patients were compared. 2. Sucrose-density-gradient centrifugation showed that the number of iron atoms per ferritin molecule was decreased to approximately half in carcinoma tissue when compared with normal liver. 3. On electrophoresis, hepatocellular carcinoma ferritin migrates faster and is therefore more negatively charged than normal liver ferritin, thus refuting the general view that the more negatively charged a ferritin molecule the greater its iron content. 4. Comparison of tumour and normal liver ferritin subunit compositions on acid/urea/polyacrylamide gels showed hepatocellular carcinoma ferritin to contain an additional, more negatively charged, subunit to normal liver ferritin. 5. Isoelectric focusing showed that hepatocellular carcinoma tissue contains isoferritins with isoelectric points intermediate between the ranges of normal liver and normal heart isoferritins.
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PMID:A biochemical comparison of normal human liver and hepatocellular carcinoma ferritins. 624 28

Radiolabeled antiferritin IgG will target ferritin-bearing tumors such as hepatoma, lung cancer, and neuroblastoma. In hepatoma 4 of 5 patients have had clinical remission of malignancy following intravenous doses up to 150 mCi of radiolabeled antiferritin IgG. The dosimetry of radiolabeled 131I-antiferritin reveals a 3-day effective half-life, low dose rate isotopic implant of tumors 5 rad/h, 2,000-3,000 rad to the tumor, and a tumor half-life of 7.7 days. The possibilities of this new cancer agent are discussed in regard to isotopes, greater antibody specificity, and methods of evaluation.
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PMID:Antiferritin IgG antibody for isotopic cancer therapy. 625 69

Fixation by periodate/lysine/paraformaldehyde, a method purported to cross-link specifically plasma membrane glycoproteins, was evaluated using Novikoff rat ascites hepatocellular carcinoma cells. Cells were treated with periodate/lysine, periodate/glycine, and periodate/lysine/paraformaldehyde and subsequently reduced with NaB3H4. The glycoproteins labeled with 3H were resolved by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate and visualized by fluorography. The effects of reactant concentrations on 3H-labeling of cellular components, cell viability, and cross-linkage of 3H-labeled proteins were examined. The effect of increasing the localized density of plasma membrane glycoproteins on the extent of cross-linkage by periodate and lysine was investigated using cells in which patching of the plasma membrane glycoproteins had been induced by ferritin-conjugated concanavalin A/rabbit antiferritin antiserum. Also investigated was the periodate-independent to mixtures of periodate and lysine or glycine. Results of these studies did not support a mechanism of cross-linking involving reaction between the free base lysin and aldehyde groups on periodate oxidized carbohydrate residues but suggested a complex interaction between periodate oxidized plasma membrane glycoproteins and polymeric complexes of lysine and formaldehyde.U
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PMID:Evaluation of periodate/lysine/paraformaldehyde fixation as a method for cross-linking plasma membrane glycoproteins. 626 47

Serum ferritin concentrations are elevated in 35% to 100% of patients with hepatocellular carcinoma (HCC). With an immunoperoxidase technique, ferritin was demonstrated in tumor tissue from 32 of 74 (43%) black southern African patients, and from 12 of 19 (63%) American patients with HCC (P greater than 0.1). Ferritin was present in nonneoplastic liver in 82% of African and 100% of American patients (P greater than 0.1). Moderate to large amounts of stainable hepatic storage iron (hemosiderin) were present in 76% of African and 67% of American patients (P greater than 0.1). Fifty-two (70%) African patients had macronodular cirrhosis. In the literature, 80% to 90% of American patients with HCC have cirrhosis. High serum ferritin levels in patients with HCC may be due to ferritin production by the tumor, or related to the associated iron overload and/or cirrhosis.
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PMID:Immunohistochemical ferritin in hepatocellular carcinoma. 632 63

We have cloned a segment of cDNA from human liver coding for an apoferritin subunit, probably an H chain. Sequence comparison with the available protein sequence shows that our clone corresponds to a ferritin subunit present as a minor species in human spleen and placenta, but as major species in HeLa cells. Northern blot analysis shows the existence of only one band of similar size in human liver, HeLa cells, Daudi lymphoma and Hep3B hepatoma cell lines. In contrast, Southern blot analysis provides evidence for a multigene family.
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PMID:Cloning and sequencing of a full length cDNA coding for a human apoferritin H chain: evidence for a multigene family. 632 67

Fifteen nude mice were inoculated with a human neuroblastoma cell line and 14 with a human primary hepatocellular carcinoma cell line. Human ferritins were detected in the sera of the mice which developed tumors. Of 14 mice bearing human neuroblastoma, 12 had human liver-type ferritin (8 to 52 ng/ml) in their sera, and three of these also had HeLa-type ferritin (acidic ferritin) (29 to 40 ng/ml). Of 10 nude mice bearing human primary hepatocellular carcinoma, eight had human liver-type ferritin (10 to 820 ng/ml), and one of these had HeLa-type ferritin at a level of 43 ng/ml. Since the ferritins in the sera of these mice were produced by the human tumor cells, these observations support the hypothesis that the elevated ferritins often found in the serum of patients with cancer are, in part, derived from their tumors.
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PMID:Human ferritins present in the sera of nude mice transplanted with human neuroblastoma or hepatocellular carcinoma. 633 59

Immunochemical and immunocytochemical techniques have been used to characterize viral glycoproteins and endogenous rat leukaemia viruses (RaLV) produced both by Novikoff hepatocellular carcinoma cells and spontaneously transformed Wistar rat embryo cells (WRC). Results from immunocytochemical analysis demonstrated that RaLV produced by Novikoff and WRC cells could be distinguished by their unique patterns of reactivity with xenoantisera raised against virus particles or viral glycoproteins. This differential labelling was unexpected since all the antisera tested had been shown by immunoprecipitation and immunodepletion analysis to be reactive with viral glycoproteins expressed on the cell surface. Since no significant differences in cell surface-associated viral glycoproteins and those shed from the cell surface were detected by pulse iodination analysis, it was concluded that the apparent discrepancy between immunoferritin labelling and immunoprecipitation analysis resulted from differences in antigen accessibility on intact virions caused by structural differences in the viral glycoproteins expressed on Novikoff and WRC cells. This conclusion was supported by results from ferritin-lectin labelling, affinity chromatography and neuraminidase digestion studies which demonstrated differences in the saccharide moieties on both virion and cell surface-associated viral glycoproteins. Further evidence of structural differences was provided by limited digestion with trypsin and V8 protease of the Mr 64 000 (Nov gp64) and Mr 68 000 (WRC gp68) viral glycoproteins immunoprecipitated from Novikoff and WRC cells, respectively, with either monospecific anti-Rauscher murine leukaemia virus anti-gp70 serum or monospecific antiserum against Nov gp64 (anti-gp64). Results from digestion studies showed that all the major cleavage fragments from WRC gp68 were of higher molecular weight than their Nov gp64-derived counterparts. Evidence that Nov gp64 and WRC gp68 both share structural homology with other murine viral gp70s was suggested by results from immunoprecipitation analysis with anti-gp70 and anti-gp64 sera under reducing and non-reducing conditions which demonstrated the presence of an interchain disulphide bond in both glycoproteins and showed that at least some of these molecules exist on the cell surface as disulphide-linked heterodimers of Mr 78 000 and 82 000.
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PMID:Structural differences in envelope glycoproteins associated with rat leukaemia virus produced by Novikoff hepatocellular carcinoma and spontaneously transformed Wistar rat embryo cells. 636 46

The incidence of this mendelian recessive trait is higher than previously estimated. Idiopathic hemochromatosis is associated with certain HLA types. Early diagnosis and institution of a phlebotomy program can produce regression of all manifestations except hepatoma and arthritis. Screening, with determination of transferrin saturation greater than 60 percent, permits diagnosis before signs and symptoms appear. Serum ferritin determination is the best indicator of the course of the disease.
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PMID:Idiopathic hemochromatosis. 663 48

Ferritin is both a normal tissue- and tumor-associated protein. The in vivo localization of 131I-radiolabeled antitumor ferritin and normal IgG antibodies in the H-4-II-E rat hepatoma model was investigated in both tumor and normal tissues over a dose range of 0.67 micrograms to 5 mg of normal and antiferritin IgG and at labeling ratios (microCi 131I per micrograms IgG) of 15:1, 5:1, and 1:10. The total dose from nonpenetrating radiation in rads was calculated and demonstrated a maximum of 2.9 times greater dose deposition (rads) of antiferritin than normal IgG in hepatoma without specific increase in binding in normal tissues. The maximum tumor targeting achieved was dependent on the amount of injected IgG and not on the labeling ratio or procedure. The binding in tumor could be inhibited by unlabeled antiferritin but not by unlabeled normal rabbit IgG and demonstrated the requirement of specificity for tumor binding. Normal tissues did not target with antiferritin. Most normal tissues have a capacity to bind normal and antiferritin IgG nonspecifically that is linear in relationship to the amount of injected IgG. The results demonstrate that 131I-antiferritin selectively targets ferritin-secreting hepatoma over normal tissues and that the amount of targeting is dependent on the amount of antiferritin injected. The physiologic reasons for such selective localization is not known, but the term "biologic window" has been used to describe the differential availability of tumor ferritin for binding.
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PMID:Variables affecting the tumor localization of 131I-antiferritin in experimental hepatoma. 669 55


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