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)

Many G1-phase-specific mRNAs have been identified from various normal or transformed cells based on serum induction and re-entry into the cell cycle from quiescence. However, these mRNAs may not represent some important genes expressed during G1 phase in continuously cycling cells. The eukaryotic cell cycle possesses two cdk (cyclin-dependent kinase) dependent regulatory gates through which cells pass during late G1 phase and G2 phase of each cycle. Subtractive hybridization was employed to synthesize a high R0t fraction cDNA library enriched in sequences expressed during G1 phase prior to passage through the G1-phase gate. To prepare G1-phase cells from continuously cycling cell populations, G1-phase HeLa cells were collected by centrifugal elutriation and highly synchronous S phase cells were obtained by double thymidine block followed by centrifugal elutriation. A G1-phase subtractive cDNA library was prepared by subtracting G1-phase cDNA with a 10-fold excess of S-phase mRNA. Single-stranded, G1-phase cDNAs were isolated by oligo(dA) chromatography. The library was screened with a high R0t fraction subtractive probe population. Following two rounds of screening, 20 positive clones were obtained. Northern blot analysis indicated that six of these clones were enhanced in expression level during G1 phase when compared with S phase. Nucleotide sequence comparison of each clone with the GenBank data base revealed that hG1.11 was highly homologous (99%) to the apoferritin light chain gene and clones hG1.6, hG1.10, hG1.17, and hG1.18 represented new G1-phase-enriched members of four human ribosomal protein gene families (71-95% homology). The last clone, hG1.1, encoded a highly charged polypeptide not previously identified. Additional study of these G1-phase-enriched mRNAs will be required to determine their role in cell cycle progression and the G1-phase gateway through which cells transit as they proceed through the cell cycle.
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PMID:Molecular cloning of G1 phase mRNAs from a subtractive G1 phase cDNA library. 812 53

For the diagnosis of bone metastasis in breast cancer patients during systemic treatment serum tumor markers, including carbohydrate antigens 15-3 (CA 15-3) and 19-9 (CA 19-9), cancer antigen 125 (CA 125), alpha-fetoprotein (AFP), carcinoembryonic antigen (CEA), beta-2 microglobulin (BMG), ferritin, and tissue polypeptide antigen (determined by the M3 monoclonal antibody, TPS) were measured in 22 patients with known bone metastases and in 30 patients without documented metastases. The most useful single marker was CA 15-3. By stepwise discriminant analysis, it was found that 90% of the patients could be diagnosed truly by using the markers CA 15-3, BMG and ferritin. It is concluded that monitoring with combinations of tumor markers at regular intervals increases the diagnostic efficiency.
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PMID:Serum tumor markers for detection of bone metastasis in breast cancer patients. 820 73

The polypeptide shell of the ferritin molecule has been imaged in water by atomic force microscopy (AFM). The central dip and the quaternary structure could be observed on the surface of the ferritin molecule anchored inhomogeneously in two dimensions. These structures observed in the AFM images are quite similar to the electron density map near the top of the apoferritin viewed down from a 4-fold axis structure reported previously (S. H. Banyard, D. K. Stammers, and P. M. Harrison, 1978. Nature (Lond.). 271:282-284). It has been achieved by introducing a "self-screening effect" of the surface charges of the AFM sample (S. Ohnishi, M. Hara, T. Furuno, and H. Sasabe. 1992. Biophys. J. 63:1425-1431) and the specially sharpened stylus of AFM cantilever.
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PMID:Direct visualization of polypeptide shell of ferritin molecule by atomic force microscopy. 821 88

Mengo virus infection of mouse L-cells results in induction of the synthesis of a cellular protein-containing particle, 12 nm in diameter, which was designated U (Boege et al. (1987) Virology 159, 358-367). We have purified the U-particle from virus-infected cells by a series of chromatographic steps and found it to be composed of two polypeptide species (MW 23,000 and 25,000), present in a ratio of approximately 7:3. Neither of these polypeptides is measurably glycosylated or phosphorylated and the U-particle contains no detectable nucleic acid. Several amino acid sequences obtained from CNBr fragments of the U-polypeptides identified them as the H- and L-chains of mouse apoferritin. This finding was supported by immunoblotting and electron microscopy. In terms of function, the U-particle/apoferritin effectively inhibits the translation of mRNAs in reticulocyte lysates. These experiments indicate that apoferritin may perform important functions in eukaryotic cells in addition to iron storage. Finally, we propose mechanisms to explain how Mengo virus infection could specifically induce the synthesis of apoferritin and how increasing amounts of cytoplasmic apoferritin could facilitate virus replication.
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PMID:The cellular U-particle, whose synthesis is induced by mengovirus infection, is homologous to apoferritin. 825 85

Ferritin, an iron-storing protein, was isolated from disease-involved and -uninvolved regions of spleen biopsies obtained from patients with Hodgkin's disease (HD). Ferritin from all human spleen biopsies showed a major band of polypeptide of M(r) around 20 kDa in 1D-SDS-PAGE analysis. The corresponding bands for horse spleen ferritin and apoferritin (Sigma) were at a slightly lower M(r) level. In isoelectrofocusing (IEF) studies, the pI values of human spleen ferritin from the uninvolved and involved regions were 4.55 and 4.14, respectively. These were more acidic than that of horse spleen ferritin (4.79). Human spleen ferritin from the involved region also differed from that of the uninvolved region in the pattern of CNBr-generated peptide maps in 1D-SDS-PAGE. These results suggest that the presence of Hodgkin's disease in human spleen is associated with some physiochemical changes in the tissue ferritin.
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PMID:Characterization of ferritin from spleens of patients with Hodgkin's disease (HD). 835 Sep 46

The iron storage protein, ferritin, in plants can occur in multiple molecular forms that, until now, were proposed to be derived from degradation of a single mature polypeptide subunit (2,7,17), which is assembled into the holoprotein and functions in plastids. We have carried out some definitive experiments with the diploid legume, Vigna unguiculata (cowpeas), which show that there are functioning genes for three different ferritin subunits in the developing leaves. Unique segments of mRNAs which code for subunits with substantially different mature sequences were detected by PCR. Separate genes for each subunit were found by showing that each gene contained a unique intron. Thus, multiple molecular forms of ferritin can arise through differential expression of a family of genes in plants.
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PMID:Functional genes found for three different plant ferritin subunits in the legume, Vigna unguiculata. 848 87

The serum concentration of the cell proliferation marker TPS (Tissue Polypeptide-Specific Antigen) was compared with 7 different common tumor markers (CEA, CA 12-5, CA 19-9, CA 15-3, ferritin, AFP and beta 2-Microglobulin) in order to assess its practical value in the management of breast cancer. The new monoclonal TPS assay utilizing the specific epitope M3 is used to monitor cell multiplication in cancer patients. The values are not related to tumor burden but rather reflect the tumor proliferation rate. In our study no association was found between the TPS values and the age of the patients and histologic tumor types. Significant correlation was observed between the TPS values and the menopausal status of the patient. The regression analyses between TPS and the other markers did not reveal a correlation. Association between the TPS values and the CA 15-3 was not found. However, strong correlation between CA 15-3 and four other markers was observed. Therefore, it was concluded that TPS can provide additional information when used in combination with CA 15-3.
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PMID:The value of TPS in breast cancer. 854 1

Properties of the L- and H-type polypeptide subunits forming ferritin 24-mer molecules in mice were investigated, using the products of in vitro transcription and translation from the two cloned genes, and recombinant ferritin molecules (H24L0 or H0L24) produced by transformation in Escherichia coli. Several different conditions for analytical electrophoresis reproducibly show that the relative migration position of the two mouse ferritin subunits is reversed from that reported for ferritin H- and L-subunits in all other mammals; since mouse and human H-polypeptides almost co-migrate, this unusual relative mobility is due largely to novel properties of the murine L-subunit. This unusual electrophoretic property of the mouse L-subunit has led to conflicting reports about the subunit composition of natural mouse ferritin. Here, we show that the single major electrophoretic band given by liver ferritin purified from mice having a short-term iron overload matches that produced by the genetically defined L-polypeptide and that some bona fide H-subunits are also detected. In conclusion, it is reasonable to assume that, when mouse ferritin samples will be analyzed under the same conditions as those described here, the slower species will correspond to the L-type subunit. However, when dealing with ferritin from species other than human or mouse, it should be kept in mind that upon electrophoretic analysis of ferritin polypeptide, the designation of an electrophoretic band as being H- or L-type subunits will be very uncertain without corroboration from genetic, immunological, or amino acid sequencing data.
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PMID:Novel properties of L-type polypeptide subunits in mouse ferritin molecules. 862 71

Monkey liver ferritin was isolated and purified along with human liver ferritin and their physicochemical and immunological characteristics were compared. The apparent molecular weight of monkey liver ferritin was estimated to be 430 kDa as against 450 kDa of human liver ferritin. Both ferritins appeared to be made up of a 22.5 kDa polypeptide under denaturing conditions and the proteins contained neutral sugar (wt/wt) of 2.0% (monkey) and 2.4% (human). By immunoblots both human and monkey liver ferritins showed appreciable cross-reactivity with the polyclonal antibodies raised against either proteins. Monkey liver ferritin, however, was not recognised by the human monoclonal antibody. The amino acid composition of both ferritins was more or less similar. Isoelectric focusing indicated that monkey liver ferritin showed microheterogeneity with three bands at pI 5.4, 5.5 and 5.6, whereas human liver ferritin showed a single band at pI 5.6 confirming the relative acidic nature of monkey liver ferritin.
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PMID:Isolation and characterization of monkey liver ferritin. 874 33

As a consequence of elevated expression rates, the intracellular aggregation of polypeptide chains is commonly observed in E. coli. Although wild-type human ferritin, a polymeric iron storage protein, accumulates in the soluble form at high level in the bacterial cytoplasmic fraction, some amino acid substitutions in an exposed loop direct the synthesis of a highly insoluble product. We found that two mechanisms can lead to the aggregation of ferritin. While some mutations prevent ferritin polymerisation, others cause the precipitation of molecules in the assembled state.
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PMID:Loop mutations affect ferritin solubility causing non-native aggregation of subunits or precipitation of fully assembled polymers. 883 Jun 64


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