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PubMed1990

Site-specific rate constants for iron removal from diferric transferrin by nitrilotris(methylenephosphonic acid) and pyrophosphate.

The kinetics of iron removal from human serum diferric transferrin by nitrilotris(methylenephosphonic acid) (NTP) and pyrophosphate (PPi) have been studied in 0.1 M, pH 7.4, N-(2-hydroxyethyl)piperazine-N'-2-ethanesulfonate buffer at 25 degrees C using urea/polyacrylamide gel electrophoresis. The four microscopic rate constants required for a complete description of iron removal from the two transferrin metal-binding sites have been measured at 100 mM concentrations of NTP and PPi. There is very good agreement between the rate constants determined by electrophoresis in this study and the corresponding rate constants determined spectrophotometrically for monoferric transferrins that have been labeled at the empty binding site with substitutionally inert Co(III). The results validate the use of cobalt-labeled transferrins as models for kinetic studies on iron removal from diferric transferrin.

Cobalt↗

PubMed1978

Binding sites of iron transferrin on rat reticulocytes. Inhibition by specific antibodies.

1. In the process of iron uptake by precursors of the erythrocytes probably more than one membrane component is involved; besides the specific transferrin receptor, another membrane component with a high iron activity after incubation with 59Fe can be isolated. 2. A striking resemblance exists between rat and human reticulocyte components which are involved in the process of iron uptake. 3. Incubation of reticulocytes with Fab fragments of an antibody against the membrane receptor for transferrin causes a concentration-dependent decrease in transferrin binding and iron uptake. 4. The membrane receptor complex isolated is still heterogeneous; analytical ultracentrifugation studies suggest a molecular weight lower than 230,000. 5. Intact immature red cells are necessary for specific binding of transferrin with the receptor followed by iron uptake. This is the only mechanism for iron uptake. 6. Immunofluorescence studies showed that the receptor for transferrin is localized at the outside of the cell membrane.

Anemia↗

PubMed1988

Reduction of diferric transferrin by SV40 transformed pineal cells stimulates Na+/H+ antiport activity.

Transplasmalemma electron transport by HeLa and pineal cells to reduce external ferricyanide is associated with proton release from the cells. Diferric transferrin also acts as an electron acceptor for the transmembrane oxidoreductase. We now show that reduction of external diferric transferrin by RPNA-209-1 SV40 transformed pineal cells is accompanied by proton release from the cells. The stoichiometry of proton release to electron transfer is much greater than would be expected from aniostropic electron flow across the membrane through protonated carriers. The proton release is not stimulated by apotransferrin and the diferric transferrin-stimulated activity is inhibited by apotransferrin. Apotransferrin also inhibits reduction of diferric transferrin by these cells. The proton release is dependent on external sodium ions and is inhibited by amiloride, which indicates that the proton release is mediated by the Na+/H+ antiport and that this antiport is activated by electron transport through the transmembrane dehydrogenase. Growth stimulation by diferric transferrin or other external oxidants can be based in part on activation of the Na+/H+ antiport.

Animals↗

PubMed1988

Membrane transport of non-transferrin-bound iron by reticulocytes.

The transport of non-transferrin-bound iron into rabbit reticulocytes was investigated by incubating the cells in 0.27 M sucrose with iron labelled with 59Fe. In most experiments the iron was maintained in the reduced state, Fe(II), with mercaptoethanol. The iron was taken up by cytosolic, haem and stromal fractions of the cells in greater amounts than transferrin-iron. The uptake was saturable, with a Km value of approx. 0.2 microM and was competitively inhibited by Co2+, Mn2+, Ni2+ and Zn2+. It ceased when the reticulocytes matured into erythrocytes. The uptake was pH and temperature sensitive, the pH optimum being 6.5 and the activation energy for iron transport into the cytosol being approx. 80 kJ/mol. Ferric iron and Fe(II) prepared in the absence of reducing agents could also be transported into the cytosol. Sodium chloride inhibited Fe(II) uptake in a non-competitive manner. Similar degrees of inhibition was found with other salts, suggesting that this effect was due to the ionic strength of the solution. Iron chelators inhibited Fe(II) uptake by the reticulocytes, but varied in their ability to release 59Fe from the cells after it had been taken up. Several lines of evidence showed that the uptake of Fe(II) was not being mediated by transferrin. It is concluded that the reticulocyte can transport non-transferrin-bound iron into the cytosol by a carrier-mediated process and the question is raised whether the same carrier is utilized by transferrin-iron after its release from the protein.

Animals↗

PubMed1989

Covalent modification of serum transferrin with phospholipid and incorporation into liposomal membranes.

A method is described for incorporation of water-soluble proteins into liposomal membranes using covalent protein-phospholipid conjugates in detergent solution. A disulfide derivative of phosphatidylethanolamine containing a reactive N-hydroxysuccinimide ester group is synthesized, and the derivative is reacted with serum transferrin in deoxycholate-containing buffer. Disulfide-linked transferrin-phosphatidylethanolamine conjugates containing up to 6 mol phospholipid/mol protein are prepared. The amphiphilic conjugates have solubility properties very similar to integral membrane proteins. The conjugates self-associate to form protein micelles of narrow size distribution (Stokes radii 6-7 nm), and in the presence of excess phospholipid (egg phosphatidylcholine), they readily incorporate into liposomal membranes upon removal of detergent. Stable incorporation into liposomes requires the introduction of two molecules of phosphatidylethanolamine into the transferrin. Using the disulfide linker to release transferrin from the liposomes, evidence is presented for a function of the phosphatidylethanolamine as an anchor-molecule into the liposomal lipid. Optimal conditions for preparation of homogeneous liposomes with diameters in the range 30-125 nm and with a varying content of transferrin are defined. The liposomes appear well suited for studies on liposome-cell membrane interactions.

Chromatography, Gel↗

PubMed1979

Synthesis and secretion of albumin and transferrin by foetal rat hepatocyte cultures.

Hepatocytes derived from foetal rat liver synthesize and secrete albumin and transferrin when maintained in primary culture. These proteins are produced for at least seven days under the conditions of culture. Studies on hepatocyte cultures derived from 12, 13, 14, 15 and 19-day foetal rats show that the maximal cellular rate of secretion of both proteins increases about 50-fold over this period. The maximal rate of albumin secretion in all cultures is achieved after one day in culture and decreases in hepatocytes from early foetuses after the fourth to sixth day in culture. Transferrin secretion by hepatocytes from 12 to 15 day foetuses increases markedly during the second day of culture and is relatively constant thereafter. In contrast, secretion of transferrin by hepatocytes from 19-day foetuses is constant from the first day of culture. The results show that both albumin and transferrin are synthesized and secreted by the foetal liver as early as the twelfth day of gestation. The increase in the rate of transferrin secretion that occurs during culture of hepatocytes from 12 to 15 day foetuses may reflect the development of a secretory mechanism that is different from that for albumin.

Albumins↗

PubMed1984

Iron uptake from transferrin by isolated hepatocytes: effect of ethanol.

Freshly isolated rat hepatocytes incubated with highly purified 59Fe-labelled diferric 125I-rat transferrin for 90 minutes in the presence of 10 mM ethanol took up significantly less 59Fe than did cells incubated without ethanol, while producing a significantly greater reduction of the pH of the incubation medium. Total transferrin binding was equivalent in both groups, but the molecular ratio of iron:transferrin on cell membranes isolated after 90 minutes was markedly reduced in the presence of ethanol, suggesting increased retention of apotransferrin. These data are compatible with the hypothesis that iron uptake from transferrin by hepatocytes is mediated by a pH dependent transferrin receptor mechanism similar to that in reticulocytes.

Animals↗

PubMed1984

Synthesis of rat transferrin in Escherichia coli containing a recombinant bacteriophage.

Using mRNA from rat liver a cDNA library was constructed in lambda gt11Amp3. Immunochemical screening identified 15 clones producing transferrin. The identity of two clones was confirmed by nucleotide sequencing, which also indicated a presegment rich in hydrophobic amino acids but lack of a prosegment in precursor transferrin. A 920 base pair insert in one clone corresponded to 84% of the N-terminal domain of transferrin, which was synthesized as a hybrid protein with bacterial beta-galactosidase. A 1540 base pair insert in another clone corresponded to the N-terminal plus 50% of the carboxy terminal domain of transferrin. The product of this clone possessed only antigenic properties of transferrin.

Amino Acid Sequence↗

PubMed1989

Change in transferrin receptor distribution in regenerating rat liver.

Partial hepatectomy results in an increase in the ability of the liver cells to bind 125I-labeled transferrin to surface receptors. Scatchard analysis of the binding of transferrin in regenerating rat liver indicates that this increase was due to an increase in the number of transferrin receptors on the cell surface. When we measured total cellular transferrin receptor number, we found that control and regenerating livers had identical amounts of receptor number. The increase in the surface receptor number is apparently due to the translocation of intracellular transferrin receptor to the cell surface.

Animals↗

PubMed1986

Binding of DNA to albumin and transferrin modified by treatment with water-soluble carbodiimides.

N-Acylurea derivatives of albumin and transferrin prepared with the water-soluble carbodiimides N-ethyl-N'-(3-dimethylaminopropyl)carbodiimide and N-ethyl-N'-(3-trimethylpropylammonium)carbodiimide iodide have been found to bind different types of DNA. The two proteins were reacted with varying amounts of carbodiimide in water at pH 5.5 for 36-60 hr at 20 degrees, and then purified. In the case of iron-loaded transferrin, reactions with carbodiimides were in phosphate-buffered saline (pH 7.5) to prevent loss of iron from the protein. [3H]N-Ethyl-N'-(3-trimethylpropylammonium)carbodiimide iodide was used for the determination of covalently attached N-acylurea groups in the modified proteins, and gel electrophoresis for changes in charge and possible aggregation through cross-linking. Binding of DNA to N-acylurea proteins was studied by means of gel electrophoresis and nitrocellulose filter binding. N-Acylurea albumin and N-acylurea transferrin at low concentrations retarded the migration of lambda-Pstl restriction fragments, pBR322 plasmid and M13 mp8 single-stranded DNA on agarose gels, while at higher concentrations of modified protein the N-acylurea protein-DNA complexes were unable to enter the gel. Nitrocellulose filter assays showed that binding pBR322 DNA and calf thymus DNA to N-acylurea proteins is rapid and dependent on protein concentration and the ionic strength of the medium. N-Acylurea albumins prepared with each each of the two carbodiimides gave comparable plots for DNA bound versus protein concentration. On the other hand, binding of DNA by N-acylurea transferrins differed according to the carbodiimide used in the synthesis. N-Acylurea CDI-tkransferrin (prepared with tertiary carbodiimide) was less effective than either of the two N-acylurea albumins in binding DNA. In contrast with these results, N-acylurea Me+-CDI-transferrin (prepared with quaternary carbodiimide) was far more effective in binding DNA and in this respect was similar to the N-acylurea albumins. On the basis of experiments in which N-acylurea protein-DNA complexes were treated with heparin, two types of binding could be distinguished. These were a weak binding occurring in the initial stages of interaction and a tight binding which developed on further incubation of the complexes. These studies show that binding of DNA by N-acylurea proteins is a reversible process dependent on ionic strength; interaction appears to be electrostatic in nature, although other forms of binding might be involved.(ABSTRACT TRUNCATED AT 400 WORDS)

Animals↗

PubMed1984

Prevention of denervation atrophy in muscle: mammalian neurotrophic factor is not transferrin.

Atrophy in a denervated muscle results from the disuse caused by paralysis of the muscle, and from the loss of special neurotrophic substances. Daily injections of proteins extracted from rats' sciatic nerves have been shown to prevent the non-disuse atrophy of rats' muscles denervated for 7 days. The trophic factor from chicken sciatic nerve which stimulates differentiation in aneural chick muscle in vitro has been purified and found to be closely similar to transferrin. We undertook to determine whether the trophic properties of mammalian nerve extract on denervated rats' muscles in vivo were due to the presence of serum transferrin in the extract. Atrophy was measured as the reduction in cross-sectional areas of type IIB fibers in the extensor digitorum longus muscle. Muscles denervated for 7 days and injected daily with 1 of several doses of iron-conjugated rat transferrin exhibited a rate of atrophy equivalent to that in denervated muscles that either were not treated or were injected with saline. Denervated muscles injected with crude extract of rats' sciatic nerves had significantly less atrophy than their controls. Removal of transferrin from the crude extract by immunoaffinity chromatography did not diminish its ameliorative effects on denervated muscle. Therefore, the trophic action of mammalian nerve extract on denervated rats' muscles in vivo is not due to the presence of serum transferrin in the extract.

Animals↗

PubMed1983

Aluminium interaction with 67Ga uptake by human plasma and transferrin.

To investigate the possible uptake of aluminium by plasma proteins, the Group IIIB element gallium (67Ga) was used as an analogue. Gel filtration confirmed that plasma bound 67Ga in the transferrin region, and this effect could be reproduced using pure transferrin. Approximately 75%, of 67Ga could be displaced by 10 mumol/l aluminium in the buffer. Equilibrium dialysis with samples of plasma, transferrin and albumin (BSA), showed that uptake of 67Ga by plasma or transferrin was systematically inhibited by increasing concentration of aluminium in the range found in dialysis fluid while uptake by albumin was negligible. The results suggest that transferrin plays an important role in aluminium uptake during haemodialysis.

Aluminum↗

PubMed1988

Concentration differences in isoforms of transferrin in blood from alcoholics during abuse and abstinence.

At least five different forms of iron-saturated transferrin (Tf) from blood plasma can be separated by isoelectric focusing. These transferrin forms differ in the carbohydrate parts, especially the amount of sialic acid. The increased relative concentration of the form with isoelectric point 5.7 (Tf5.7) has been shown to be a good indicator for liver effects caused by alcohol abuse. However, in alcoholics during abstinence the newly formed transferrin has a higher sialic acid content than most of the transferrin already present in the blood. This indicates that the elevated concentration of Tf5.7 with a low sialic acid content, found in alcoholics is not due to a defect at sialylation, but most probably caused by an impaired uptake of sialic acid-deficient transferrin by the hepatocytes due to membrane dysfunction.

Adult↗

PubMed1984

There is selective accumulation of a growth factor in chicken skeletal muscle. I. Transferrin accumulation in adult anterior latissimus dorsi.

Chick embryo myoblasts in culture will respond to extracts of adult anterior latissimus dorsi muscle with an increase in cell number and an increase in total protein and in myosin heavy chain in fused myotubes. Extracts of adult pectoralis major and of posterior latissimus muscles are only marginally active. The active adult muscle extracts are fractionated by DEAE-cellulose column chromatography and transferrin is identified as the active component based on the following findings: (1) the active fractions are shown to contain an 80K protein that comigrates with chicken transferrin on SDS-PAGE, (2) the active extract from the anterior latissimus dorsi completely replaced embryo extract in the culture medium and supported normal myogenesis, (3) the active extract requires iron for its ability to support myogenesis, (4) the peptide map of the 80K protein is identical to a peptide map of transferrin. Under conditions where the 80K protein is detected in adult anterior latissimus dorsi muscles it is shown that the protein is nevertheless not synthesized in the muscle. These results support the idea that tissues of selective muscles in the adult chicken accumulate transferrin. An accompanying paper shows that transferrin also accumulates in early developmental stages of fast muscle tissue but that accumulation ceases after hatching in these muscles in normal chickens but not in animals of congenic strains with inherited muscular dystrophy.

Aging↗

PubMed1990

Tau fraction of transferrin is present in human aqueous humor and is not unique to cerebrospinal fluid.

In view of the many similarities between the aqueous humor and the cerebrospinal fluid (CSF), we investigated whether the tau fraction of transferrin, which is believed to be specific for CSF, is also present in aqueous humor. Samples of aqueous humor and CSF from clinically normal individuals were analyzed by SDS-PAGE and isoelectric focusing (IEF), and probed with anti-transferrin antiserum and the lectin Limax flavus agglutinin. Specific bands which corresponded to transferrin and its tau fraction were detected in both fluids. After isolation of these bands by affinity chromatography with anti-transferrin antiserum, we detected a single, diffuse fraction at an apparent molecular weight of 80 kDa in both aqueous humor and CSF. Peptide mapping revealed no detectable difference in this fraction between the two fluids. The detection of the tau fraction in human aqueous humor indicates that this molecule cannot be considered a specific cerebrogenic marker as had been thought previously. In view of the known growth-promoting properties of transferrin, its isolation from both ocular and cranial fluids attains special significance.

Aged↗

PubMed1983

The identification of neurotrophic factor as a transferrin.

Partially purified neurotrophic factor (NTF) from chicken nerves comigrated with transferrin and a component in several preparations known to have neurotrophic effects on cultured skeletal muscle cells. One-dimensional gel electrophoretograms of proteolytic fragments of NTF and fragments obtained from transferrins purified from chicken eggs, serum and embryos were indistinguishable. These purified transferrins, like NTF, all stimulated the incorporation of [3H]thymidine and supported myotube formation to a similar degree as NTF. These studies suggest that NTF is a transferrin-like protein and that both transferrins and NTF act by initially promoting myoblast proliferation and subsequently supporting myogenesis in chick muscle cultures.

Animals↗

PubMed1994

Iron released from transferrin at acidic pH can catalyse the oxidation of low density lipoprotein.

Low density lipoprotein (LDL) oxidation within the arterial wall may contribute to the disease of atherosclerosis. We have investigated the conditions under which transferrin (the major iron-carrying protein in plasma) may release iron ions to catalyse the oxidation of LDL. Transferrin that had been incubated at pH 5.5 released approximately 10% of its bound iron in 24 h, as measured by ultrafiltration and atomic absorption spectroscopy. Furthermore, transferrin co-incubated with LDL and L-cysteine at pH 5.5 resulted in the oxidation of the LDL as measured by thiobarbituric acid-reactive substances and electrophoretic mobility. This effect was observed at transferrin concentrations as low as 40% of its average plasma concentration. The release of iron from transferrin in atherosclerotic lesions due to a localised acidic pH may help to explain why LDL oxidation occurs in these lesions.

Humans↗

PubMed1989

Ability of human colonic epithelium to express the 4F2 antigen, the common acute lymphoblastic leukemia antigen, and the transferrin receptor. Studies in inflammatory bowel disease and after in vitro exposure to different stimuli.

We investigated the ability of isolated human colonic epithelial cells to express the common acute lymphoblastic leukemia antigen (CALLA), the transferrin receptor, and the 4F2 antigen in response to different types of stimuli. The expression of these markers was assessed by immunofluorescence using monoclonal antibodies. Thirty-two percent of freshly isolated colonic epithelial cells from actively inflamed mucosa of patients with inflammatory bowel disease expressed the 4F2 antigen, 28% the transferrin receptor, and 13% the CALLA. Normal colonic epithelial cells were cultured and the kinetics of expression of the three antigens was studied. A significant increase in the expression of the three markers was observed throughout the culture period in response to the lectin phytohemagglutinin and the epidermal growth factor. The kinetics of expression of the 4F2 antigen and the CALLA after lectin stimulation appeared to differ from that observed after epidermal growth factor. At the end of the cultures one-third of the cells expressed the 4F2 antigen and the transferrin receptor, whereas one-fifth were positive for CALLA. Thus, after these cultures the expression of the three markers was quantitatively similar to that observed with freshly isolated cells from inflamed mucosa. gamma-Interferon markedly induced the 4F2 antigen but had no effect on the transferrin receptor and the CALLA. These data demonstrate that colonic epithelium is capable of expressing the 4F2 antigen and the CALLA in association with the transferrin receptor.

Antibodies, Monoclonal↗