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PubMed1997

Iron acquisition from transferrin and lactoferrin by Pseudomonas aeruginosa pyoverdin.

Growth of Pseudomonas aeruginosa ATCC 15692 was promoted when the strain was cultured in an iron-depleted succinate medium, supplemented with transferrin at 30%, 60% and 100% and lactoferrin at 60% and 100% iron-saturation. No significant differences between cell growth and pyoverdin production were observed when transferrin iron saturation was increased from 30% to 100%; however, cell growth and pyoverdin production were strongly dependent on lactoferrin iron saturation. Lower lactoferrin iron saturation (< 30%) resulted in more pyoverdin production and reduced cell growth. Incubation of pyoverdin (1.0 microM) with 10.0 microM transferrin (30%, 60% and 100% iron-saturated) or lactoferrin (60% and 100% iron-saturated) led to quenching of pyoverdin fluorescence. Also, 24 h incubation of pyoverdin (20.0 microM) with these two proteins (20.0 microM, 30%, 60% and 100% iron-saturated transferrin and 60% and 100% iron-saturated lactoferrin) at 25 degrees C resulted in increased absorbance at 460 nm. Both the fluorescence quenching and absorbance increases were iron-saturation-dependent. Taken together, these results support the conclusion that at physiological pH, P. aeruginosa pyoverdin can acquire from partially iron-saturated transferrin or lactoferrin.

Fluorescence↗
PubMed2001

The crystal and molecular structures of diferric porcine and rabbit serum transferrins at resolutions of 2.15 and 2.60 A, respectively.

The serum transferrins are monomeric proteins with a molecular mass of around 80 kDa and are responsible for the transport of iron in vertebrates. The three-dimensional structures of diferric porcine and rabbit serum transferrin have been refined against X-ray diffraction data extending to 2.15 and 2.60 A, respectively. Data for both proteins were collected using synchrotron radiation at temperatures of 277 K. The porcine protein crystallizes in the space group C2, with unit-cell parameters a = 223.8, b = 44.9, c = 78.9 A, beta = 105.4 degrees with one molecule in the asymmetric unit. The structure was solved by molecular-replacement methods using rabbit serum transferrin as the search model. The structure was refined using REFMAC, with a final residual of 13.8% (R(free) = 18.2% for a 5% data sample) for all data to 2.15 A. The final model comprises 5254 protein atoms, two Fe(3+) cations and two CO(3)(2-) anions, one N-acetyl glucosamine moiety and 494 water molecules. The rabbit protein crystallizes in space group P4(3)2(1)2, with unit-cell parameters a = 127.2, c = 144.9 A and one molecule per asymmetric unit. The structure was solved using the method of multiple isomorphous replacement and refined using REFMAC to give a final residual of 18.6% (R(free) = 22.2% for a 5% data sample) for all data to 2.60 A. The final model comprises 5216 protein atoms, two Fe(3+) cations and two CO(3)(2-) anions, a Cl(-) anion and 206 solvent molecules; there is no clear indication of the carbohydrate moiety attached to Asn490 (rabbit serum numbering). Both molecules adopt a bilobal structure typical for members of the transferrin family. Each of the structurally homologous lobes contains two dissimilar domains with a single iron-binding site buried within the interdomain cleft. The porcine serum protein lacks an interdomain disulfide bridge close to the connecting peptide between the lobes, but this seems to have little effect on the overall orientation of the lobes. The N-lobes of both proteins possess lysine residues, one from each of the two domains, that lie in close proximity to one another to form the so-called dilysine trigger. The more acid-labile release of iron from serum transferrins than from lactoferrins is discussed.

Animals↗
PubMed1986

A new transferrin allele in sheep.

An electrophoretic variant of sheep transferrin, TfL, has been described. Transferrin L has been shown to be controlled by a single codominant allele, TfL, at the Tf locus. Transferrin L is electrophoretically distinguishable from the very similar transferrin TfKCzech. The value of gradient polyacrylamide gel electrophoresis for transferrin phenotyping in sheep is discussed.

Alleles↗
PubMed1975

Differences between human Fe1-transferrin molecules.

Two molecular forms of Fe1-transferrin molecule can be demonstrated by anion-exchange chromatography on columns of DEAE-cellulose, pH 7.90. It is believed that co-ordination of each metal-binding site by ferric ions induces dissimilar changes in molecular conformation in the region of the binding sites which, in the case of one site, results in the molecule behaving as a weaker anion during anion-exchange chromatography. If so, this could be entirely in accord with current views that the two binding sites of transferrin do not share equal properties of iron exchange with cells. At physiological levels of transferrin iron-saturation, it is likely that two populations of Fe1-transferrin molecules form the bulk of the iron-transferrin complex.

Binding Sites↗
PubMed1977

The role of iron in the regulation of hepatic transferrin synthesis.

The role of iron supply in the regulation of hepatic transferrin synthesis by the isolated perfused rat liver was studied using nutritional iron deficiency as the experimental model. The increased transferrin release encountered in iron deficiency could be equated with enhanced de novo synthesis as evidenced by the inhibitory effects of cycloheximide and measurements of intrahepatic protein pools before and after perfusion. Refeeding with iron, sufficient to restore plasma iron and hepatic ferritin iron but before correction of anaemia, promoted a reduction towards normal in the transferrin synthetic rate. This effect was not produced by transfusional correction of the anaemia, suggesting a specific response to iron supply. Phenobarbitone treatment, which produced a marked fall in hepatic ferritin iron concentration but no change in haemoglobin or plasma iron concentrations, promoted a specific enhancement of transferrin synthesis in both control and iron deficient livers. The concentration of liver iron stores appears to be a major regulatory factor in the control of hepatic transferrin synthesis.

Animals↗
PubMed1977

Transferrin receptors in developing murine erythroid cells.

Techniques of cell separation were used to isolate murine erythroid cells at different stages of maturation. The number of transferrin receptors in these cell populations was assayed by measuring binding of 125I-labelled transferrin. Nearly 23 times as many receptors were found in the least mature cells, chiefly pronormoblasts, as in reticulocytes. Iron transport, determined by measurement of the rate of 59Fe uptake from 59Fe-labelled transferrin, was proportional to the number of receptors at all stages of differentiation. Electron microscope radioautographic studies of the interaction of 125I-labelled transferrin with erythroid precursor cells demonstrated that 15-33% of cell associated transferrin was intracellular in erythroid precursors.

Animals↗
PubMed1979

Modulation of transferrin receptors in bone marrow cells by changes in lipid fluidity.

The hypothesis that modulation of transferrin receptors during haematopoiesis is mediated by changes in the lipid fluidity of the cell membranes was tested in this study with bone marrow cells. Binding conditions were first established, under which internalization of fluorescently-labelled transferrin was reduced to a minimum during the binding assays. Cholesterol depletion, which was achieved by a mild physiological treatment, and which increased the membrane-lipid fluidity, resulted in a substantial increase in the average number of the available transferrin receptors per bone marrow cell. Cholesterol enrichment mediated a converse effect. These findings correlate well with the changes observed in the availability of transferrin receptors and membrane microviscosity during differentiation of erythroid cells. In line with the notion of passive modulation, it is proposed that the transferrin receptor is a cross-membrane protein with a substantial portion facing the cytoplasm.

Animals↗
PubMed1980

Evidence for the functional heterogeneity of the two sites of transferrin in vitro.

A recently developed crossed immunoelectrophoretic method for displaying and quantitating the four possible molecular species of transferrin has been utilized to assess the relative effectiveness of each site of rabbit and human diferric transferrin in providing iron to rabbit reticulocytes. The site which appears to reside in the N-terminal half of the rabbit protein was found to be at least 5 times more effective than its counterpart. However, both sites may serve as iron donors in monoferric as well as diferric rabbit transferrins. It is also possible that iron may be removed from rabbit transferrin in pairwise as well as sequential fashion. In human diferric transferrin, the site in the C-terminal domain functions as the better iron donor for rabbit reticulocytes.

Animals↗
PubMed1986

Fluorescence probe measurement of the pH of the transferrin microenvironment during iron uptake by rat bone marrow erythroid cells.

Fluorescence probe measurements of the transferrin micro-environment during iron uptake by rat erythroid cells revealed that part of the transferrin is taken up in an acidic environment. The pH of this intracellular transferrin environment is 5.7. When rat erythroid cell precursors are incubated with diferric transferrin then in the incubation medium monoferric transferrins TfNFe and TfFeC appear. In view of the known instability of TfNFe at acidic pH, TfNFe cannot arise after endocytosis of Tf2Fe in acid vesicles at pH below 6.0. The results support the existence of a mechanism other than endocytosis in the iron uptake process in rat erythroid cells.

Animals↗
PubMed1986

Intracellular forms of iron during transferrin iron uptake by mitogen-stimulated human lymphocytes.

Transferrin receptors expressed by mitogen stimulated human lymphocytes mediate the uptake of transferrin iron into haem, ferritin and a non-haem, non-ferritin component. In spite of different rates of iron uptake by cells from different individuals, the proportional incorporation of 59Fe into these components was similar, suggesting that there was an obligatory relationship between the different forms of iron in the cells. By 3 h over 60% of the iron taken up was incorporated into ferritin while less than 10% was found in haem. Initially (10 min) non-haem, non-ferritin iron comprised 70% of total iron and this diminished to 30% by 3 h. At 10 min 80% of iron in the non-haem, non-ferritin component was retained by anti-transferrin affinity columns indicating it was transferrin-bound. The proportion retained fell to reach a steady state level of 50% by 60 min. These results indicate that 10-20% of the iron in the cells was not recognized as transferrin, ferritin or haem iron. The finding that iron incorporation into this unidentified pool reached equilibrium while that into haem and ferritin increased suggests the iron may act as a precursor for functional and storage compounds.

Chromatography, Affinity↗
PubMed2005

Carbohydrate-deficient isoforms of transferrin (%CDT) and sialic acid (SA) in iron-deficiency anemia.

This study has investigated the serum levels of carbohydrate-deficient isoforms of transferrin (CDT) and sialic acid (SA) in iron-deficiency anemia (IDA). Blood samples were collected from 60 women with IDA and from 20 healthy controls. CDT was estimated by anion-exchange chromatography on minicolumns followed by photometric detection of transferrin and was expressed as a percentage of total transferrin (%CDT). SA was measured by an enzymatic method. There was no difference in the mean level of %CDT between patients with IDA (2.26%) and control patients (2.05%). SA increased significantly from control level 0.61 to 0.69 g/l in anemic patients. We concluded that elevated concentration of total transferrin in IDA did not change the relative value of low sialylated isoforms (%CDT) and the increase of total SA level in the sera of anemic patients is not related to the increase of total transferrin.

Adult↗
PubMed1993

Effect of transferrin concentration on bacterial growth in human ascitic fluid from cirrhotic and neoplastic patients.

Cirrhotic patients with ascites have an unusually high frequency of development of spontaneous bacterial peritonitis. Iron availability is a key factor in bacterial growth and the ability of the host to limit it is associated with resistance to infection. The present study was undertaken to evaluate the influence of iron and transferrin on bacterial growth in ascitic fluid from 25 biopsy-proven cirrhotic and nine neoplastic carcinomatous patients. No significant differences were found when comparing total ascitic fluid iron between the two groups but ascitic fluid transferrin concentration was significantly lower in cirrhotic (29.26 mg dl-1 SD 29.58) than neoplastic (96.57 mg dl-1 SD 76.01) patients. Moreover, a significant negative correlation was found between bacterial growth and transferrin concentration in ascitic fluid (P = 0.039). When the iron concentration in ascitic fluid was experimentally elevated (50 micrograms dl-1 or 150 micrograms dl-1) we observed a progressive increase in bacterial growth. If transferrin concentration is simultaneously elevated (250 mg dl-1) this increase does not occur. These findings indicate that the transferrin level is an important factor in the regulation of bacterial growth in ascitic fluid and that the low concentration found in cirrhotic patients could facilitate spontaneous bacterial peritonitis.

Adult↗
PubMed1984

Expression of EGF receptor and transferrin by F9 and PC13 teratocarcinoma cells.

We document the time of appearance and the levels of two markers of differentiation during the formation of embryoid bodies by two embryonal carcinoma (EC) cell lines. Neither of these markers has been described before for EC cells differentiating in aggregate culture, and they further extend the identification and characterization of new cell types. Both F9 and PC13 EC cell lines form embryoid bodies (so-called because they resemble early mouse embryos) with an outer epithelial layer of visceral endoderm cells, after suspension culture in the presence of retinoic acid. However, the two cell lines differ in the procedures needed to initiate the differentiation process. Once floating aggregate cultures have been formed, the time course of the appearance of epidermal growth factor (EGF) receptors and of the secretion of transferrin are similar in both cell lines, although the levels differ. EGF receptors and transferrin are quantified by 125I-EGF binding assays and enzyme-linked immunosorbent assays (ELISA) using specific antibodies, respectively. The expression of EGF receptors increases about two fold while that of transferrin increases up to 40 fold after treating F9 aggregates with retinoic acid. The EGF receptors reach a maximum 4 days after adding retinoic acid and then decline, while transferrin only increases later from a low but detectable level. For PC13 cells, EGF receptors increase tenfold, and transferrin synthetic rate increases 40 fold during the time-course. Interestingly, unstimulated F9 cells in monolayer cultures also express low levels of these markers, while the levels in PC13 EC cells are barely detectable above background.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1980

Uptake of iron from transferrin by isolated rat-liver mitochondria mediated by phosphate compounds.

1. Isolated rat-liver mitochondria accumulate iron from transferrin at neutral pH by a mechanism which is markedly stimulated by small-molecular-weight polyphosphate compounds. The efficiency of the phosphate compounds decreases in the order: pyrophosphate > ATP > GTP > 2,3-bis-(phospho)glycerate > phosphate. 2. The uptake has a very low energy dependence, and it does not depend on the hydrolysis of ATP or the saturation of transferrin, but it increases in parallel to the concentration of iron to reach a saturation level of 800-1200 pmol iron/mg protein. 3. Following a chase with unlabelled transferrin (125I)-labelled transferrin bound to the mitochondria remains constant, whereas the progressive uptake of 59Fe levels off. 4. During reincubation of iron-loaded mitochondria up to 30% of the iron is mobilized in the presence of ascorbate and ATP (or apotransferrin). 5. The results suggest that iron is mobilized from transferrin by the polyphosphate compounds outside the mitochondria in a subsequent reaction.

Adenosine Triphosphate↗
PubMed1989

Lactoferrin-binding sites at the surface of HT29-D4 cells. Comparison with transferrin.

The binding of 125I-lactoferrin to HT29-D4 cells, a clone of HT29 cells, was studied and compared to the binding of 125I-transferrin to the same cells. The binding of the two iron-transport proteins is saturable and reversible suggesting the presence of specific receptors for each protein. Scatchard analysis suggests the existence of binding sites for lactoferrin with the relatively high equilibrium dissociation constant, Kd1 of 408 nM. Additionally, the cell is capable of binding large amounts of lactoferrin with very low affinity, probably in a non-receptor intermediate fashion. The dissociation constant of transferrin and its receptor was calculated 9.29 nM which corresponds well to values found in the literature. In contrast to lactoferrin, the cell was capable of binding only low amounts of transferrin in a non-receptor intermediate fashion. After chemical crosslinking of lactoferrin to the cell surface, the radiolabeled lactoferrin was found in a complex of molecular mass 300 kDa. Crosslinking of transferrin resulted in a complex of much higher molecular mass. These data clearly show a binding site for lactoferrin different from the transferrin receptor. Only if competition experiments were performed with a high molar excess of both ligand proteins did a small percentage of either of the two ligands crossreact with the receptor for the other, possibly due to a structural similarity of the two glycoproteins.

Adenocarcinoma↗
PubMed1989

Effect of glycosylation inhibitors on the structure and function of the murine transferrin receptor.

The murine transferrin receptor is a disulphide-linked dimer with three N-glycosylation sites. We have investigated the structural and functional properties of the transferrin receptor from murine plasmacytoma cells (NS-1 cells) treated with the glycosylation inhibitor, tunicamycin and the glycosylation-processing inhibitors, swainsonine and castanospermine. 1. Tunicamycin (1 microgram/ml) inhibited mannose incorporation in NS-1 cells by greater than 90%, but also inhibited methionine incorporation by up to 50%. Both swainsonine (1 microgram/ml) and castanospermine (50 micrograms/ml) resulted in mannose incorporation greater than 100% of untreated cells and neither drug affected methionine incorporation. 2. Incubation of NS-1 cells with tunicamycin resulted in a shift in the apparent molecular mass of the transferrin receptor from 96 kDa and 94 kDa to approximately 82 kDa. 3. Peptide N-glycosidase F digestion of the receptor from untreated cells resulted in the fully deglycosylated 82 kDa component as well as an 87 kDa component which represents partially deglycosylated receptor resistant to peptide N-glycosidase F digestion. 4. The receptor from swainsonine-treated cells was equally sensitive to peptide N-glycosidase F and endo-beta-N-acetylglucosaminidase H (endo H; resulting in both 87-kDa and 82-kDa components), whereas the receptor from castanospermine-treated cells was only partially sensitive to endo H. 5. Analysis of mannose- and fucose-labelled cellular glycopeptides by concanavalin-A--Sepharose chromatography showed that swainsonine (1 microgram/ml) treatment resulted in approximately 90% inhibition of the synthesis of complex N-glycans and an accumulation of fucosylated hybrid structures. In contrast, castanospermine (100 micrograms/ml) treatment resulted in only partial inhibition (60%) of the synthesis of complex N-glycans. 6. Analysis of the receptor from tunicamycin, swainsonine and castanospermine treated cells under nonreducing conditions showed a single component corresponding to the dimer, indicating that dimerisation of newly synthesised murine receptor is independent of carbohydrate. 7. The non-glycosylated receptor from tunicamycin-treated cells appears to bind transferrin as demonstrated by interaction with transferrin-Sepharose. 8. Surface expression of the receptor was not significantly altered in the presence of either swainsonine or castanospermine as judged by flow cytometry.

Alkaloids↗
PubMed1991

Post-transcriptional regulation of the transferrin receptor and 4F2 antigen heavy chain mRNA during growth activation of spleen cells.

The expression of several cell surface proteins including the transferrin receptor and 4F2 antigen is induced when quiescent cells are activated and proliferate. We have studied this induction in mouse spleen cells after stimulation with 4 beta-phorbol 12-myristate 13-acetate (PMA), the Ca(2+)-ionophore, ionomycin and recombinant interleukin-2 (IL-2). The 4F2 antigen heavy chain and transferrin receptor mRNA were barely detectable in resting cells, but increased 60-fold within 4 h of growth stimulation. The corresponding proteins became measurable at the cell surface after 6 h, prior to the S phase. In run-on transcription assays the transferrin receptor gene was transcribed to almost the same extent in resting and growth-stimulated cell populations and the 4F2 antigen heavy chain gene was induced fivefold. This suggests that post-transcriptional control mechanisms are mainly responsible for the accumulation of the respective mRNA at the onset of cell proliferation. In the case of the transferrin receptor, the induction correlated with an activation of the mRNA-binding iron-regulatory factor which is known to increase the stability of the cytoplasmic transferrin receptor mRNA.

Animals↗
PubMed2005

Bicarbonate inhibits the growth of Staphylococcus epidermidis in platelet concentrates by lowering the level of non-transferrin-bound iron.

BACKGROUND: Platelet concentrates (PCs) contain non-transferrin-bound iron (NTBI) owing to the displacement of iron from plasma-derived transferrin by citrate. NTBI in the PC medium supports the growth of Staphylococcus epidermidis. The possibilities of lowering the level of NTBI have been studied with the aim to inhibit the growth of S. epidermidis in the PC medium. STUDY DESIGN AND METHODS: NTBI in PC supernatants was determined by a chelation method and by the bleomycin-detectable iron assay. Iron binding by transferrin was determined by spectrophotometry. The growth of inoculated S. epidermidis in PC supernatants was monitored by optical density and determination of viable counts. RESULTS: Bicarbonate enhanced in a dose-dependent manner transferrin iron binding in citrate-containing solutions, including citrated plasma and PAS-II. The use of a modified anticoagulant supplemented with bicarbonate effectively lowered the level of NTBI and inhibited bacterial growth in citrated plasma. Supplementation of bicarbonate to the additive solution to increase the ratio of bicarbonate to citrate in a reconstituted PC medium further inhibited bacterial growth. Maintenance of stable pH and bicarbonate level in the reconstituted medium necessitated storage under 5 percent CO(2). CONCLUSIONS: The relatively low bicarbonate level in PC medium promotes iron displacement by citrate from plasma-derived transferrin. The appearance of NTBI can be decreased and iron-dependent bacterial growth can be inhibited by increasing bicarbonate level in citrated plasma and PC medium. To achieve the same beneficial effect in blood banking, other more practical ways to bind NTBI in a harmless form should be developed.

Bicarbonates↗