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Query: UNIPROT:P02794 (ferritin)
 17,525 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The lectin receptors of confluently grown hamster BHK, wild type polyoma virus transformed PyBHK, and temperature-sensitive polyoma transformed ts3-PyBHK fibroblasts were investigated using cell agglutination, quantitative (125I)lectin binding, and ferritin-lectin labeling. PyBHK and permissively grown ts3-PyBHK cells agglutinated more strongly with Ricinus communis I agglutinin (RCA-I)compared to BHK and nonpermissively grown ts3-PyBHK, although saturation binding of (125I)RCA-I to these cells at 4 degrees resulted in a twofold difference in lectin-binding sites on BHK and nonpermissively grown ts3-PyBHK cells (1.0-1.3 x 10 7 sites/cell) compared to PyBHK and permissively grown ts3-PyBHK (0.4-0.6 x 10 7 sites/cell). These cells bound equivalent amounts of (125I)concanavalin A (0.8-1 x 10 7 sites/cell) and (125I)wheat germ agglutinin (1-2.2 x 10 7 sites/cell). Under these binding conditions little endocytosis occurred, as judged by the subsequent release of greater than 90% cell-bound (125I)RCA-I by the RCA-I inhibitor lactose and localization of ferritin-RCA-I exclusively to the extracellular plasma membrane surface. However, if the binding is performed at 22 degrees, only 50% of the bound lectin can be removed by lactose, and ferritin-RCA-I is localized inside the cell within endocytotic vesicles. The relative mobility of RCA-I receptors was examined on ts3-PyBHK cells by the ability of ferritin-RCA-I to induce clustering of its receptors at 22 degrees. RCA-I receptors on permissively grown ts3-PyBHK cells appeared to be more mobile than on nonpermissively grown cells. BHK and PyBHK cells were treated with neuraminidase, and the resulting enzyme-treated cells were assayed for lectin agglutinability and quantitative binding of RCA-I, concanavalin A, and wheat germ agglutinin. Neuraminidase treatment resulted in decreased concanavalin A and wheat germ agglutinability and a slight increase in RCA-I agglutinability. The enzyme-treated BHK and PyBHK cells bound less (125I)wheat germ agglutinin (2.8 x 10 6 and 2.2 x 10 6 sites/cell, respectively) and 2.5 and 6.2 times more (125I)RCA-I (2.5-3 x 10 7) and 3.5-4 x 10 7 sites/per cell, respectively). There was no change in the number of concanavalin A binding sites after neuraminidase treatment. The increase in RCA-I binding sites approximated the decrease in wheat germ agglutinin binding sites indicating that the predominant penultimate oligosaccharide residue to sialic acid on these cells is D-Gal.
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PMID:Qualitative and quantitative interactions of lectins with untreated and neuraminidase-treated normal, wild-type, and temperature-sensitive polyoma-transformed fibroblasts. 16 28

An affinity-purified plant lectin from Ricinus communis (RCAII) was shown to exhibit differential toxicity toward SV40-transformed 3T3 fibroblasts grown in vitro. When macromolecular synthesis was examined in SV3T3 and 3T3 cells, RCAII suppressed cell protein synthesis in the transformed line at lower concentrations (1/50 to 1/100) compared to the 3T3 line, and these effects were blocked by the RCAII inhibitors D-galactose or lactose. RNA and DNA synthesis and L-leucine transport were relatively unaffected by RCAII concentrations (greater than 1 mug/ml) that completely suppressed protein synthesis in both cell lines. The RCAII-mediated inhibition of cell protein synthesis required incubation times longer than 60 min, but quantitative cell binding studies with 125-I-RCAII indicated that the lectin binds to maximal levels in approximately 5 to 10 min, even at 4 degrees. During 10-min labeling experiments with 125-I-RCAII (1 mug/ml), it was demonstrated that the cell-bound lectin could be almost quantitatively removed from cells up to an additional 15 min after labeling without subsequent inhibition of protein synthesis. However, longer incubation times (greater than 30 min) after RCAII cell labeling and washing resulted in incomplete removal of cell-bound lectin (less than 20 to 30% of cell-bound lectin could be removed after a 60-min incubation). The longer incubation times (greater than 60 min) also resulted in almost complete inhibition of protein synthesis. Ferritin-conjugated RCAII (ferritin-RCAII) was used to follow the fate of the cell-bound lectin. Ferritin-RCAII bound rapidly (less than 10 min) to SV3T3 cell surfaces and could be blocked from labeling with lactose. After a 10-min incubation at 4 degrees in ferritin-RCAII solutions, the ferritin label was exclusively located at the extracellular surface in a random distribution. After washing and incubation at 37 degrees, the ferritin-RCAII induced clustering of its receptors (15 to 30 min) and eventually induced endocytosis (30 to 60 min). Further incubation (greater than 60 min) resulted in a predominantly intracellular localization of ferritin-RCAII inside endocytotic vesicles and free in the cell cytoplasm. That RCAII acts directly on protein synthesis after cell entry was confirmed with rabbit reticulocyte and mouse Krebs II ascites S30 cell-free protein synthesis system in diameter wit
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PMID:Mechanism of cell entry and toxicity of an affinity- purified lectin from Ricinus communis and its differential effects on normal and virus-transformed fibroblasts. 16 59

The presence of carbohydrate residues on the outer surface of PMN granules has been demonstrated by the use of ricin-conjugated ferritin. The binding of the lectin was inhibited by alpha-lactose. No difference in the binding densities of azurophil or specific granules was observed.
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PMID:Demonstration of ricin-binding sites on the outer face of azurophil and specific granules of rabbit polymorphonuclear leukocytes. 114 75

Mutants of Actinomyces viscosus T14V lacking type 1 or type 2 fimbriae or both were selected by their failure to react with rabbit antibodies against either or both fimbrial antigens. Immunospecific double labeling with iron dextran and ferritin-conjugated antibodies showed two types of fimbriae on individual cells of the parent organism, a single type on mutant strains with type 1+2- and type 1-2+ fimbriae and no labeled or unlabeled fimbriae on a type 1-2- fimbria-deficient strain. The mutational loss of one fimbrial antigen did not appear to affect expression of the other, since bacteria with one or two types of fimbriae bound similar amounts of a monoclonal antibody directed against the fimbrial antigen present on both bacterial phenotypes. The strong adsorption of strains with type 1+2+ or 1+2- fimbriae to saliva-treated hydroxyapatite and weak adsorption of those with type 1-2+ or no fimbriae was consistent with the known involvement of type 1 fimbriae in this attachment process. Similarly, the A. viscosus lectin was clearly associated with the expression of type 2 fimbriae, since only the strains with type 1+2+ or 1-2+ fimbriae participated in lactose-sensitive coaggregations with Streptococcus sanguis 34. Further studies using the fimbria-deficient mutant strains showed that aggregation of A. viscosus T14V in the presence of sialidase-treated human saliva involved both types of fimbriae, whereas neither type was required for the lactose-resistant coaggregation of the organism with certain streptococcal strains.
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PMID:Mutants of Actinomyces viscosus T14V lacking type 1, type 2, or both types of fimbriae. 290 12

Ninety preselected children, aged between 8 and 14 years, living in two rural West African (Gambian) villages, were randomly divided into three groups, matched for age and sex. One group received a placebo (lactose) tablet, one received riboflavin (5 mg) on 5 d every week, which was sufficient to correct an endemic riboflavin deficiency, and one received a multivitamin supplement (Protovit; Hoffmann La Roche), on 5 d every week, together with FeSO4 (200 mg) once weekly, and the supplements were given for 1 year. Neuromuscular tests, including arm tremor and manipulative skills, were performed on three occasions: once just before the introduction of the supplements; again 6 weeks after commencing the supplements; and again 1 year later. Venous blood samples were collected at the same time as the first two sets of neuromuscular tests. These samples were used for haematology and nutrient status indices: plasma ferritin, ascorbic acid, cyanocobalamin and pyridoxal phosphate, and erythrocyte tests for folate status, for riboflavin status (erythrocyte glutathione reductase activation coefficient) and thiamine status (erythrocyte transketolase activation coefficient). The riboflavin in both supplements achieved a clear-cut response in biochemical status, which was dose-dependent. The pyridoxine, ascorbic acid and Fe components of the multivitamin also affected the associated biochemical indices. Although overall the arm tremor and related neuromuscular function tests did not respond significantly to the supplements, significant improvement was seen in the boys for the arm-tremor test in both the supplemented groups.
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PMID:Biochemical indices and neuromuscular function tests in rural Gambian schoolchildren given a riboflavin, or multivitamin plus iron, supplement. 798 90

27 long term monitored coeliac children were assessed. The average length of follow-up was 6.4 years, the average age of the children was 11.5 years (ranging 6.3 to 20.1 years). Of the 11 boys and 16 girls 4 adolescents consume a normal diet, while another 2 are on semistrict diet, all 6 of them without any enteral symptoms. Out of the 15 children aged younger than 13 years 9 are on a strict diet. Semistrict diet has an impact on gliadin antibody levels respectively. Serum ferritin levels of those on a normal diet are significantly lower than those of the control group. Out of the 25 lactose breath tests 7 showed abnormal results, irrelevant both to the strictness of the diet and to gliadin antibody levels. In the view of weight and length percentiles there is no difference at present between those eating normal food and diet. Nevertheless, with regards to the risk of malignancy in coeliac disease the necessity of a strict diet must be stressed. In long term follow-up the levels of gliadin antibodies and of serum ferritin are of pathognostic importance.
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PMID:[Long-term follow up study of children with celiac disease]. 849 86

Bovine lactoferrin binds to a 60 kDa heat shock protein of Helicobacter pylori. Binding ability was related to human immunoglobulin G because bovine lactoferrin binding proteins were isolated by extraction of cell surface associated proteins with distilled water, applied on IgG-Sepharose and nickel sulphate chelate affinity chromatography. Binding was demonstrated by Western blot after purified protein was digested with alpha-chymotrypsin and incubated with peroxidase-labeled bovine lactoferrin. Binding was inhibited by bovine lactoferrin, lactose, rhamnose, galactose, and two iron-containing proteins, ferritin and haptoglobin. Helicobacter pylori binds ferritin and haptoglobin via charge or hydrophobic interactions because this binding was not inhibited by specific and various glycoproteins or carbohydrates. Carbohydrate moieties of bovine lactoferrin molecules seem to be involved in binding because glycoproteins with similar carbohydrate structures strongly inhibited binding. Scatchard plot analysis of the binding of peroxidase-labeled bovine lactoferrin to H. pylori cells yielded a kd 2.88 x 10(-6) M. In addition, binding of H. pylori cells to bovine lactoferrin was enhanced when bacteria treated with pepsin or alpha-chymotrypsin after isolation from iron-restricted and iron-containing media.
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PMID:Cryptic domains of a 60 kDa heat shock protein of Helicobacter pylori bound to bovine lactoferrin. 911 43

Jejunal expression of three brush-border membrane (BBM) enzymes, intestinal alkaline phosphatase (IAP), lactose-phlorizin hydrolase (LPH), and sucrase-isomaltase (SI), and a cytosolic protein, ferritin (Ft), was investigated after transient segmental ischemia-reperfusion (I/R). I/R reduced mucosal IAP, LPH, and SI mRNAs to 36%, 11%, and 38% of normal jejunal levels after 3 h of reperfusion and to 22%, 8%, and 51% of normal jejunal levels after 6 h of reperfusion, respectively. Intriguingly, in the internal control jejunum IAP and LPH mRNAs also decreased significantly. LPH and SI mRNA rapidly recovered to levels significantly higher than those of normal jejunum at 12 h, whereas IAP mRNA levels did not recover until 48 h. Enzyme activity paralleled changes in mRNA levels in the ischemic reperfused jejunum. Electrophoretic mobility shift assays showed that I/R significantly increased SI footprinting 1 (SIF1) binding activity. The mobility of one of the DNA-protein complexes was further retarded in the presence of anti-Cdx-2 antibody, suggesting that either Cdx-2 or a related protein was interacting with the SIF1 sequences. Similar to BBM enzymes, cytosolic Ft mRNA and protein were significantly decreased at 3 and 6 h after I/R. By 12 h, Ft mRNA, but not Ft protein, had increased to higher than normal levels. We conclude that a rapid recovery of BBM mRNAs and enzymes occurs in regenerating mucosa after upper villus damage. The increase of SIF1 binding protein activity after I/R may enhance SI, and perhaps LPH, gene transcription. The expression of Ft is regulated at both pretranslational and translational levels.
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PMID:Expression of intestinal brush-border membrane hydrolases and ferritin after segmental ischemia-reperfusion in rats. 972 71

Biofilm formation by a strain of Streptococcus suis serotype 2 isolated from a case of meningitis in pigs was characterised. Using a polystyrene microtitre plate assay, S. suis 95-8242 produced a dense biofilm when glucose, fructose or sucrose was used as the carbohydrate source, whereas no biofilm formed in the presence of lactose. Polysaccharide production by the biofilm-forming strain was demonstrated by the Congo red agar assay. Transmission electron microscopy revealed that bacterial cells were surrounded by a thick layer of polycationic ferritin-labelled material. S. suis 95-8242 was more resistant to both penicillin G and ampicillin in biofilms than in planktonic cultures on the basis of minimal inhibitory and minimal bactericidal concentrations.
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PMID:Characterisation of biofilm formation by a Streptococcus suis meningitis isolate. 1796 4