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

Sendai virus envelopes and human erythrocyte band 3 membrane polypeptides were isolated in detergent solutions and coreconstituted into detergent-free vesicle structurally resembling viral envelopes. Formation of hybrid viral envelope-band 3 vesicles (VB3) was demonstrated by immunoprecipitation of VB3 containing 4,4'-diisothiocyano-2,2'-ditritostilbenedisulfonic acid-labeled band 3 in the presence of antiviral antiserum. The hybrid VB3 vesicles displayed agglutination, fusion, and hemolytic properties similar to those of reconstituted viral envelopes. Incubation of VB3 with Friend erythroleukemic cells resulted in fusion-mediated insertion of viral antigens and of band 3 into the plasma membranes of the recipient cells. The presence of band 3 incorporated into Friend erythroleukemic cells was revealed structurally by electron microscopy after staining with ferritin-conjugated anti-human erythrocyte membrane antiserum. Incorporation of band 3, the putative erythrocyte antion channel, led to a marked and specific stimulation of anion exchange in Friend erythroleukemic cells. The viral-mediated insertion of an isolated membrane protein into viable Friend erythroleukemic cells provides a method for studying membrane protein turnover and for assaying reconstituted membrane components such as carriers or channels.
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PMID:Implantation of the isolated human erythrocyte anion channel into plasma membranes of Friend erythroleukemic cells by use of Sendai virus envelopes. 23 Apr 75

Antisera against purified acetylcholine receptors from the electric tissues of Torpedo californica and of Electrophorus electricus were raised in rabbits. The antisera contain antibodies which bind to both autologous and heterologous receptors in solution as shown by an immunoprecipitation assay. Antibodies in both types of antisera bind specifically to the postjunctional membrane on the innervated surface of the intact electroplax from Electrophorus electric tissue as demonstrated by an indirect immunohistochemical procedure using horseradish peroxidase conjugated to anti-rabbit IgG. Only anti-Electrophorus receptor antisera, however, cause inhibition of the receptor-mediated depolarization of the intact Electrophorus electroplax. The lack of inhibition by anti-Torpedo receptor antibodies, which do bind, suggests that the receptor does not undergo extensive movement during activity. The binding of anti-Torpedo antibodies to receptor-rich vesicles prepared by subcellular fractionation of Torpedo electric tissue was demonstrated by both direct and indirect immunohistochemical methods using ferritin conjugates. These vesicles can be conveniently collected and prepared for electron microscopy on Millipore filters, a procedure requiring only 25 micrograms of membrane protein per filter. In addition, it was possible to visualize the binding of anti-Torpedo receptor antibodies directly, without ferritin. These anti-Torpedo receptor antibodies, however, do not inhibit the binding of acetylcholine or of alpha-neurotoxin to receptor in Torpedo microsacs but do inhibit binding of alpha-neurotoxin to Torpedo receptor in Triton X-100 solution. It is likely that the principal antigenic determinants on receptor are at sites other than the acetylcholine-binding sites and that inhibition of receptor function, when it occurs, may be due to a stabilization by antibody binding of an inactive conformational state.
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PMID:Binding of antibodies to acetylcholine receptors in Electrophorus and Torpedo electroplax membranes. 34 25

Campylobacter jejuni strains were tested for their ability to acquire iron from various iron sources present in humans. Hemin, hemoglobin, hemin-hemopexin, and hemoglobin-haptoglobin stimulated the growth of C. jejuni strains in low-iron medium. Transferrin, lactoferrin, and ferritin were unable to provide iron to the strains tested. Derivatives of the naturally transformable C. jejuni strain 81-176 were isolated on the basis of their inability to use hemin as an iron source. These mutants were also unable to use hemoglobin, hemin-hemopexin, or hemoglobin-haptoglobin as iron sources. Some mutants lacked a 71,000-Da iron-regulated outer membrane protein, while others appeared to retain all of their outer membrane proteins. Growth curves and a recombination experiment that exploited natural transformation were used to further characterize the mutants. A hemolytic activity was shown to be produced by several C. jejuni strains, but it did not appear to be iron regulated.
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PMID:Iron acquisition and hemolysin production by Campylobacter jejuni. 150 Jan 94

The virulence of three avian strains of Pasteurella multocida was evaluated in mice. Strains P-1059I (serotype A:3) and its uncapsulated variant P-1059B and strain 2723 (serotype A:16) were compared. Capsular material thickness after polycationic ferritin labelling of dextrose starch agar (DSA)-grown P. multocida was shown to vary with the strain and was not always related to virulence. Addition of alpha,alpha' bipyridyl (BIP) (160 microM) to the culture medium did not affect capsule production but increased virulence of strains P-1059B and 2723. None of the strains tested showed dermonecrotic activity. Using sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), outer membrane protein (OMP) profiles indicated for strains P-1059I and P-1059B three proteins of 30, 35, and 38 KDa with the 30 KDa protein being the major one. Strain 2723 showed the same OMP profile but the 38 KDa protein was the major one. DSA + BIP-grown strains showed the same OMP profiles. Whole cell profiles were similar for all strains tested. However, addition of BIP to the culture media increased the virulence of strains P-1059B and 2723 and for all strains a 39 KDa protein was induced by the iron chelator. The results indicate that encapsulation may be important for virulence, but other surface components such as OMPs may be required as well.
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PMID:Cell surface characteristics and virulence in mice of Pasteurella multocida. 157 5

The binding of Phaseolus vulgaris (PHA) isolectins L4 and E4 to the brush border membrane of differentiated Caco-2 cells was studied and the impact on cellular metabolism and microvilli was assessed. Computer analysis of the data based on binding experiments with peroxidase conjugated isolectins gave mean (SD) values for maximal binding of 2540 (151).10(-9) M for PHA-L4 and 2104 (140).10(-9) M for PHA-E4 per mg of brush border membrane protein. The dissociation constants for L4 and E4 binding were 4.3 (1.4).10(-6) M and 1.1 (0.8).10(-6) M, respectively. Incubation of differentiated Caco-2 cells for 30 minutes with ferritin conjugated PHA isolectins showed that, as indicated by the number of ferritin particles, PHA-E4 bound to the microvilli to a greater extent than PHA-L4. Ferritin particles were also localised intracellularly over endocytotic invaginations and vesicles. After incubation for 48 hours with PHA-L4 or PHA-E4, the relative incorporation of precursors for DNA, RNA, and (glyco)protein synthesis into the trichloroacetic acid insoluble fraction of the Caco-2 cells was determined. Both isolectins stimulated the incorporation of thymidine and glucosamine, but neither PHA-L4 nor PHA-E4 were able to influence the incorporation of uridine. With respect to fucose, methionine, and N-acetyl mannosamine, the stimulatory effect remained confined to PHA-E4. Since PHA-L4 and PHA-E4 were tested at the same concentrations, PHA-E4 is more effective than PHA-L4. The changes in the uptake of radioactive precursors were lost after heat inactivation of PHA-E4. Compared with control and PHA-L4 incubated Caco-2 cells, the microvilli of PHA-E4 incubated cells were shortened significantly (p less than 0.01).
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PMID:Binding of kidney bean (Phaseolus vulgaris) isolectins to differentiated human colon carcinoma Caco-2 cells and their effect on cellular metabolism. 186 41

The ability of Haemophilus influenzae, H. parainfluenzae and H. paraphrophilus to utilize iron complexes, iron-proteins and exogenous microbial siderophores was evaluated. In a plate bioassay, all three species used not only ferric nitrate but also the iron chelates ferric citrate, ferric nitrilotriacetate and ferric 2,3-dihydroxybenzoate. Each Haemophilus species examined also used haemin, haemoglobin and haem-albumin as iron sources although only H. influenzae could acquire iron from transferrin or from haemoglobin complexed with haptoglobin. None of the haemophili obtained iron from ferritin or lactoferrin or from the microbial siderophores aerobactin or desferrioxamine B. However, the phenolate siderophore enterobactin supplied iron to both H. parainfluenzae and H. paraphrophilus, and DNA isolated from both organisms hybridized with a DNA probe prepared from the Escherichia coli ferric enterobactin receptor gene fepA. In addition, a monospecific polyclonal antiserum raised against the E. coli 81 kDa ferric enterobactin receptor (FepA) recognized an iron-repressible outer membrane protein (OMP) in H. parainfluenzae of between 80 and 82 kDa (depending on the strain). This anti-FepA serum did not cross-react with any of the OMPs of H. paraphrophilus or H. influenzae. The OMPs of each Haemophilus species were also probed with antisera raised against the 74 kDa Cir or 74 kDa IutA (aerobactin receptor) proteins of E. coli. Apart from one H. parainfluenzae strain (NCTC 10665), in which an OMP of about 80 kDa cross-reacted with the anti-IutA sera, no cross-reactivity was observed between Cir, IutA and the OMPs of H. influenzae, H. parainfluenzae or H. paraphrophilus.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Utilization of enterobactin and other exogenous iron sources by Haemophilus influenzae, H. parainfluenzae and H. paraphrophilus. 215 Apr 14

The membrane protein bacteriorhodopsin was imaged in buffer solution at room temperature with the atomic force microscope. Three different substrates were used: mica, silanized glass and lipid bilayers. Single bacteriorhodopsin molecules could be imaged in purple membranes adsorbed to mica. A depression was observed between the bacteriorhodopsin molecules. The two dimensional Fourier transform showed the hexagonal lattice with a lattice constant of 6.21 +/- 0.20 nm which is in agreement with results of electron diffraction experiments. Spots at a resolution of approximately 1.1 nm could be resolved. A protein, cationic ferritin, could be imaged bound to the purple membranes on glass which was silanized with aminopropyltriethoxysilane. This opens the possibility of studying receptor/ligand binding under native conditions. In addition, purple membranes bound to a lipid bilayer were imaged. These images may help in interpreting results of functional studies done with purple membranes adsorbed to black lipid membranes.
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PMID:Imaging the membrane protein bacteriorhodopsin with the atomic force microscope. 227 63

It is established that wild-type cells of Yersinia pestis absorb exogenous hemin or Congo red and thus grow as pigmented colonies at 26 degrees C on media containing these chromatophores (Pgm+). Pgm+ isolated are known to possess a siderophore-independent mechanism of iron-transport (required for growth in iron-deficient medium) which is absent in avirulent Pgm- mutants. Production of the bacteriocin pesticin and linked invasins (Pst+) is an additional defined virulence factor of yersiniae; mutation of Pgm+,Pst- organisms to pesticin-resistance (Pstr) results in concomitant conversion to Pgm-. In this study, autoradiograms of two-dimensional gels of [35S]methionine-labeled outer membranes from Pgm- mutants were compared to those of the Pgm+,Pst+ or Pgm+,Pst- parent. An apparently single predominant peptide present in these preparations (greater than 10% of total membrane protein) existed as a family of iron-modifiable 17.9-kDa molecules focusing down to isoelectric points of about 4.6 and up to 5.89. Expression of eight detectable Pst(+)-specific peptides was not significantly influenced by exogenous iron. Pgm+ yersiniae constitutively produced pigmentation-specific peptide F and five iron-repressible peptides termed IrpA to IrpE. Typical spontaneous mutation to Pgm- resulted in loss of peptide F and IrpB-E. A rare Pgm+,Pstr mutant, selected on Congo red agar containing pesticin, also lost IrpB-E but retained peptide F. This isolate, like Pgm- mutants, failed to grow in iron-deficient medium. Regardless of phenotype, all yersiniae utilized hemin, hemopexin, myoglobin, hemoglobin, and ferritin, but not transferrin or lactoferrin, as sole sources of iron.
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PMID:Outer membrane peptides of Yersinia pestis mediating siderophore-independent assimilation of iron. 253 80

Previous studies documented the abnormal association of heme and heme proteins with the sickle RBC membrane. We have now examined RBC ghosts and inside-out membranes (IOM) for the presence of nonheme iron as detected by its formation of a colored complex with ferrozine. Sickle ghosts have 33.8 +/- 18.2 nmol nonheme iron/mg membrane protein, and sickle IOM have 4.3 +/- 3.0 nmol/mg. In contrast, normal RBC ghosts and IOM have no detectable nonheme iron. The combination of heme and nonheme iron in sickle IOM averages nine times the amount of membrane-associated iron in normal IOM. Kinetics of the ferrozine reaction show that some of this nonheme iron on IOM reacts slowly and is probably in the form of ferritin, but most (72% +/- 18%) reacts rapidly and is in the form of some other biologic chelate. The latter iron compartment is removed by deferoxamine and by treatment of IOM with phospholipase D, which suggests that it represents an abnormal association of iron with polar head groups of aminophospholipids. The biologic feasibility of such a chelate was demonstrated by using an admixture of iron with model liposomes. Even in the presence of tenfold excess adenosine diphosphate, iron partitions readily into phosphatidylserine liposomes; there is no detectable association with phosphatidylcholine liposomes. To examine the bioavailability of membrane iron, we admixed membranes and t-butylhydroperoxide and found that sickle membranes show a tenfold greater peroxidation response than do normal membranes. This is not due simply to a deficiency of vitamin E, and this is profoundly inhibited by deferoxamine. Thus, while thiol oxidation in sickle membranes previously was shown to correlate with heme iron, the present data suggest that lipid peroxidation is related to nonheme iron. In control studies, we did not find this pathologic association of nonferritin, nonheme iron with IOM prepared from sickle trait, high-reticulocyte, postsplenectomy, or iron-overloaded individuals. These data provide additional support for the concept that iron decompartmentalization is a characteristic of sickle RBCs.
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PMID:Nonheme iron in sickle erythrocyte membranes: association with phospholipids and potential role in lipid peroxidation. 316 8

The Golgi apparatus mediates intracellular transport of not only secretory and lysosomal proteins but also membrane proteins. As a typical marker membrane protein for endoplasmic reticulum (ER) of rat hepatocytes, we have selected phenobarbital (PB)-inducible cytochrome P-450 (P-450[PB]) and investigated whether P-450(PB) is transported to the Golgi apparatus or not by combining biochemical and quantitative ferritin immunoelectron microscopic techniques. We found that P-450(PB) was not detectable on the membrane of Golgi cisternae either when P-450 was maximally induced by phenobarbital treatment or when P-450 content in the microsomes rapidly decreased after cessation of the treatment. The P-450 detected biochemically in the Golgi subcellular fraction can be explained by the contamination of the microsomal vesicles derived from fragmented ER membranes to the Golgi fraction. We conclude that when the transfer vesicles are formed by budding on the transitional elements of ER, P-450 is completely excluded from such regions and is not transported to the Golgi apparatus, and only the membrane proteins destined for the Golgi apparatus, plasma membranes, or lysosomes are selectively collected and transported.
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PMID:Is cytochrome P-450 transported from the endoplasmic reticulum to the Golgi apparatus in rat hepatocytes? 405 94


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