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PubMed1997

Transferrin gene expression and secretion in rat sertoli cells.

Transferrin secretion and expression were studied in cultured Sertoli cells recovered from fats at days 10 and 17 postpartum. Transferrin biosynthesis as measured by radioimmunoassay showed a dramatic, 3.9-fold increase between days 10 and 17. The majority of the transferrin was secreted, and a kinetic study revealed that the production was four times higher at day 17 than at day 10. This difference was not the result of altered transferrin degradation as the protein was shown to be very stable at both ages. To determine if this regulation was at the transcriptional or translation level, Northern blot analysis, nuclear run-on assays, mRNA stability (half-life) measurements, and mRNA intracytoplasmic distribution analyses were carried out. The Northern blots analysis, the nuclear run-on assays, and the half-life measurements revealed that transferrin mRNA levels, gene transcription rates, and mRNA stability were indistinguishable at both ages. Interestingly, the intracytoplasmic mRNA distribution analyses showed that most of the transferrin mRNA (80%) was associated with the 40 S and 60 S protein particles at both ages and was, therefore, theoretically untranslatable. However, approximately twice as much transferrin in RNA was found to be associated with polysomes at day 17 as compared to day 10. We have shown that the increase in transferrin biosynthesis by rat Sertoli cells during testicular development is not due to an increase in the amount of transferrin mRNA or an increase in its half-life, but appears to be due to an increase in translation rate of the transferrin mRNA.

Animals↗
PubMed1995

Transferrin receptor expression in nonsmall cell lung cancer. Histopathologic and clinical correlates.

BACKGROUND: In the search for tumor-related antigens with survival-predictive value, previous studies have yielded varied conclusions regarding the expression of one such antigen, the transferrin receptor in lung cancer. The goal of this study was to define the frequency of expression of transferrin receptor in lung cancer specimens and gather preliminary data regarding the prognostic value of this tumor-related antigen. METHODS: Tissue immunoreactivity was studied with a murine monoclonal antibody to transferrin receptor in patients with nonsmall cell lung cancer who underwent surgical resection at the Medical Center Hospital of Vermont during the period from January, 1988, to May, 1991. RESULTS: The study group consisted of 32 patients (21 males and 11 females) with an average follow-up length of 27 months (standard deviation of 16 months). There were 17 patients with adenocarcinoma, 14 with squamous cell carcinoma, and 1 with large cell carcinoma. At the end of data accumulation, a total of 16 deaths had been recorded (8 with squamous cell, 8 with adenocarcinoma). Normal lung tissue did not stain for transferrin receptor; however, 13 of 17 (76%) adenocarcinomas, 13 of 14 (93%) squamous cell carcinomas, and the 1 large cell carcinoma stained positively for transferrin receptor. Staining for transferrin receptor was graded according to pattern and intensity and categorized as absent-weak or strong. Survival analysis was performed to evaluate patient outcome based on a variety of clinical and experimentally determined characteristics. Groups based on N-status (N0 vs. N1 + N2, P = 0.08), stage (Stage 1 vs. Stage 2 + 3 P = 0.13), age (younger than 60 vs. 60 years or older, P = 0.09), and transferrin receptor staining (absent-weak vs. strong, P = 0.14) achieved nearly significant differences in survival. Further analysis of the differences in survival for groupings based on transferrin receptor staining found that these differences in survival reached significance for patients with larger tumors (T2 or T3, P = 0.02). CONCLUSIONS: Transferrin receptor is expressed in the majority of lung cancers and the presence of transferrin receptor in nonsmall cell lung cancers may be an indicator of poorer prognosis in certain groups of patients.

Adenocarcinoma↗
PubMed1989

Hemolysates reduce iron released from transferrin.

Transferrin donates iron to reticulocytes as follows: it binds to a receptor on the reticulocyte surface; the complex is endocytosed; both irons are released and the transferrin is recycled to the cell exterior. It has been proposed that the trigger for iron release after transferrin endocytosis is acidification of the endocytic vesicle. But this could account for removal of only one of transferrin's two irons, since only one of the irons is labile at acid pH. Moreover, iron continues to be removed from transferrin when acidification of the vesicle is blocked by a chloride-transport inhibitor. Thus a detailed explanation of iron removal from transferrin remains elusive. In earlier work we showed that iron can be removed from transferrin by whole hemolysates and also by the combined action of hemoglobin and ATP at pH 7. We now show that the iron released from transferrin by hemolysates, and by hemoglobin and ATP, is in the Fe(II) oxidation state. We also show that ADP and DPG can substitute for ATP and that NADH and NADPH can substitute for the hemoglobin, although with these substitutions Fe(II) is generated less efficiently. The reductive release of iron from transferrin is rapid enough to account for all the iron processed by a young reticulocyte. We speculate that transferrin iron may be reduced to Fe(II) before reaching the mitochondria.

Animals↗
PubMed1991

Expression of transferrin receptors on monocytes in hemochromatosis.

To assess whether an abnormality in transferrin receptor expression or regulation could represent an underlying metabolic defect in the reticuloendothelial (RE) system in hemochromatosis, monocytes were analyzed for the expression of the transferrin receptor using a monoclonal antibody (Act II) to the transferrin receptor (CD71) and flow cytometric analysis. Hemochromatosis patients (n = 14), and normal volunteers with no clinical evidence of iron overload (n = 14) were studied. A significant inverse relationship was observed for the relationship between the expression of transferrin receptor on monocytes and log(hepatic iron concentration) in hemochromatosis patients (r = -0.59, P less than .02) and also for the relationship between the expression of transferrin receptor and log(serum ferritin) in normal volunteers (r = -0.90, P less than .001). There was no significant difference in the mean expression of monocyte transferrin receptor between hemochromatosis patients and normal volunteers. However, the expression of the transferrin receptor in hemochromatosis patients was disproportionately higher than would be predicted from the relationship between serum ferritin and transferrin receptor expression in normal volunteers. The inverse relationship of the monocyte transferrin receptor relative to body iron stores in hemochromatosis is consistent with observations in other tissues, and suggests that non-transferrin iron metabolism, including ferritin, requires further investigation in the RE cell in hemochromatosis.

Antibodies↗
PubMed1987

Specific binding sites for transferrin on ameloblasts of the enamel maturation zone in the rat incisor.

During enamel maturation in rodents, an iron-containing pigment is deposited into the surface layer of the enamel. Maturation zone ameloblasts presumably are responsible for this deposition. The presence of large amounts of ferritin in the cytoplasm of these cells suggests that they receive iron, presumably from circulating transferrin. An in vivo radioautographic binding assay using iodinated transferrin was used to determine if indeed maturation ameloblasts possess transferrin receptors at their cell surfaces. Experimental rats received systemic injections of labeled transferrin while control rats received injections of labeled transferrin plus a large excess of unlabeled transferrin in order to compete with the labeled transferrin for available specific receptors. Light microscope radioautography showed that ruffle-ended ameloblasts (RAs) of the enamel maturation zone had a high density of specific receptors for transferrin relative to smooth-ended ameloblasts (SAs). Electron microscopy and energy-dispersive X-ray spectroscopy confirmed the presence of ferritin and iron, respectively, within these cells. It is postulated that the iron responsible for enamel pigmentation is transported by transferrin to maturation ameloblasts and is bound to specific transferrin receptors found mostly on RAs and that the modulation of these cells into SAs results in a loss of most of these receptors.

Ameloblasts↗
PubMed1977

Role of plasma membrane phospholipids in the uptake and release of transferrin and its iron by reticulocytes.

The involvement of membrane phospholipids in the utilization of transferrin-bound iron by reticulocytes was investigated using [59Fe]- and [125I]-labelled transferrin and rabbit reticulocytes which had been incubated with phospholipase A. Transferrin and iron uptake and release were all inhibited by phospholipase A which produced a marked decrease in the relative abundance of phosphatidylcholine and phosphatidylethanolamine and equivalent increases in their lyso-compounds in the reticulocyte plasma membrane. There was a close correlation between the iron uptake rate and the rate and amount of transferrin uptake and the amount of the lysophospholipids in the membrane. Incubation of the cells with exogenous lysophosphatidylethanolamine or lysophosphatidylcholine also produced inhibition of iron and transferrin uptake. The reduced uptake produced by phospholipase A could be reversed if the lyso-compounds were removed by fatty acid-free bovine serum albumin or by reincubation in medium 199. Treatment with phospholipase A was shown to increase the amount of transferrin bound by specific receptors on the reticulocyte membrane but to inhibit the entry of transferrin into the cells. The present investigation provides evidence that the phospholipid composition of the cell membrane influences the interaction of transferrin with its receptors, the processes of endocytosis and exocytosis whereby transferrin enters and leaves the cells, and the mechanism by which iron is mobilized between its binding to transferrin and incorporation into heme. In addition, the results indicate that phosphatidylethanolamine is present in the outer half of the lipid bilayer of reticulocyte membrane.

Animals↗
PubMed2002

Transferrin receptor in tissue and serum: updated clinical significance of soluble receptor.

The transferrin receptor is an essential component of cellular uptake of iron, and it binds to serum transferrin. Recently, 2 different types of transferrin receptors have been recognized: transferrin receptor (TfR or transferrin receptor 1) and transferrin receptor 2. Most cells possess a ubiquitous system controlling the biosynthesis of TfR at the posttranscriptional level to avoid excess iron influx into the cells through TfR. During the process of recycling of transferrin receptors, some are shed and appear as soluble or serum transferrin receptors. Measurement of serum transferrin receptor is a new marker of iron metabolism that reflects body iron stores and total erythropoiesis. It has been shown that serum transferrin receptor to ferritin ratios have significant predictive value for differentiating iron deficiency anemia from non-iron deficiency anemia, such as anemia of chronic disorders, whereas serum ferritin is the only significant independent predictor of iron deficiency anemia.

Anemia, Iron-Deficiency↗
PubMed1987

The interaction of anions with native and phenylglyoxal-modified human serum transferrin.

The interaction of various anions with human serum transferrin was investigated due to the concomitant binding of iron and a synergistic anion to form the transferrin-anion-iron complex. Two tetrahedral oxyanion oxidizing agents, periodate and permanganate, were found to partially inactivate transferrin when used at equimolar ratios of oxidizing agent to protein active sites. Hypochlorite, a strong oxidizing agent with little structural similarity to periodate and permanganate, had little effect on iron-binding activity when used at similar low molar ratios of reagent to transferrin active sites. Transferrin treated with a 3:1 molar ratio of periodate or permanganate to active sites lost 74 or 67% of its iron-binding capacity, respectively. The composition of the buffer affected the extent of transferrin inactivation by periodate and permanganate; for example, the extent of inactivation by periodate was threefold greater in a borate buffer than in a phosphate buffer. Comparative oxidations in buffer systems suggest the following order of affinity of three buffer anions for the apotransferrin metal-binding center: phosphate greater than bicarbonate greater than borate. The interaction of phosphate ions with the iron-transferrin complex was also examined due to the increased susceptibility to periodate inactivation of iron-saturated transferrin in phosphate buffer (M. H. Penner, R. B. Yamasaki, D. T. Osuga, D. R. Babin, C. F. Meares, and R. E. Feeney (1983) Arch. Biochem. Biophys. 225, 740-747). The apparent destabilization of the iron-transferrin complex in phosphate buffer was found to be due to the competitive removal of iron by phosphate from the iron-protein complex. We found that phenylglyoxal-modified Fe-transferrin, with no loss of bound iron, was much more resistant to iron removal by phosphate and other competitive chelators.

Aldehydes↗
PubMed1988

The preparation of poly (dT)-5'-transferrin conjugates and hybridisation studies with poly (dA)-tailed linearised pBR322 plasmid DNA.

The formation of transferrin-DNA complexes intended for ligand-directed transfection studies has been achieved through a hybridisation technique involving complementary homodeoxypolynucleotide chains attached to the participating protein and DNA species. Oligothymidylate residues (pT)n obtained by dicyclohexylcarbodiimide (CDI) polymerisation of thymidine-5'-monophosphate (5'-TMP) were activated to the 5'-imidazolides which on incubation with transferrin yielded the 5'linked phosphoramidates (pT)n-5'-transferrin. Homopolymeric chain extension of (pT)5-5'-transferrin by terminal transferase and dTTP at 30 degrees for 30 min yielded (pT) 300-5'-transferrin. Cleavage of the phosphoramide link in the polymer modified transferrin at 37 degrees was pronounced after 30 min although at 25 degrees hydrolysis was less than 5% after 4 hr. Poly(dT)-5'-transferrin readily hybridised with [3H]poly(dA)-tailed Pst 1 linearised pBR322 DNA. Resultant complexes were demonstrated by nitrocellulose filter binding and immunoprecipitation with anti-transferrin antibody. In contrast with poly(dT)-5'-transferrin, poly(dT)-5'-transferrin-poly(dA)-tailed pBR322 DNA complexes were stable at 37 degrees suggesting that annealing is followed by further stabilising interactions between the DNA and protein components.

Nucleic Acid Hybridization↗
PubMed1987

The regulation by low-density lipoproteins of the activation of oxidative enzyme-primed lymphocytes is governed by transferrin.

The activation of T lymphocytes was regulated in vitro by low-density lipoproteins (LDL). Not all prereplicative events induced by the oxidative enzymatic mitogens neuraminidase and galactose oxidase (NAGO) were susceptible to inhibition by LDL. The accessory cell-independent early blastogenic response was not suppressed. LDL suppressed accessory cell-dependent responses, and the extent of LDL suppression, depended on the concentration of transferrin. A gradient of transferrin determined the point in the cell cycle at which NAGO-primed lymphocytes were suppressed by LDL. When transferrin was low (0-10 micrograms/ml) and in serum-free medium (SFM), LDL suppressed the expression of cell surface receptors for interleukin-2 (IL-2R) and transferrin (TfR), the late blastogenic response prior to DNA replication (72 hr), and DNA replication. At higher levels of transferrin, about 100 micrograms/ml, the LDL-suppressed cells were IL-2R+, TfR+ and responsive to IL-2, but did not enter S phase. LDL suppression could be ablated by IL-2 and by high levels of transferrin (250-1000 micrograms/ml). In RPMI medium containing serum (FBS), the pattern of LDL suppression was different from that in SFM: fully activated IL-2R+, TfR+ lymphocytes were unresponsive to exogenous IL-2, suggesting that they were blocked at the G1/S boundary. This block was also relieved by transferrin (greater than 100 micrograms/ml). The data suggest that the interplay between transferrin and LDL is a critical factor in the NAGO-induced stimulation of T lymphocytes. LDL and transferrin exert negative and positive control of lymphocyte activation, respectively. In SFM, LDL appear to alter transferrin utilization by accessory cells; in RPMI-FBS, by fully activated T lymphocytes.

Antigen-Presenting Cells↗
PubMed1991

The release of iron and transferrin from the human melanoma cell.

The role of the transferrin homologue, melanotransferrin (p97), in iron metabolism has been studied using the human melanoma cell line, SK-MEL-28, which expresses this antigen in high concentrations. The release of iron and transferrin were studied after prelabelling cells with human transferrin doubly labelled with iron-59 and iodine-125. Approx. 45% of internalised iron was in ferritin with little redistribution during reincubation. Iron release was linear with time, while transferrin release was biphasic, suggesting that iron was leaving the cell independently of transferrin. Unlabelled diferric transferrin increased transferrin release, implying a degree of coupling between cell surface binding, internalisation and release of transferrin. Increasing the preincubation time increased the amount of transferrin which remained internalised within the cell. A membrane-bound, iron-binding component with properties consistent with melanotransferrin was observed. Desferrioxamine or pyridoxal isonicotinoyl hydrazone could not remove iron from this compartment, suggesting a high affinity for iron. The number of membrane iron-binding molecules per cell was estimated to be 387,000 +/- 7000 . The non-transferrin-bound membrane Fe did not decrease during reincubation periods up to 5 h, suggesting that the cell was not utilising it. Hence, melanotransferrin may not have a role in internalising iron in melanoma cells.

Antigens, Neoplasm↗
PubMed1994

Glomerular clearance and tubular reabsorption of transferrin in microtransferrinuric patients with non-insulin-dependent diabetes.

Our objective was to determine the role of increased glomerular clearance (GC) or reduced tubular reabsorption (TR) of transferrin in producing microtransferrinuria. An infusion of L-arginine was used to inhibit TR of transferrin, permitting the determination of both GC and TR of transferrin in 64 patients with non-insulin-dependent diabetes mellitus (NIDDM), with or without microtransferrinuria. Thirty-one healthy volunteers served as control subjects. The GC of transferrin in NIDDM patients with microtransferrinuria did not differ significantly from that in healthy controls or in NIDDM patients with normal transferrin excretion rates (TfER). No correlation was found between TfER and GC of transferrin in any group of the subjects. However, the TR of transferrin was inversely correlated with TfER in healthy controls and in the NIDDM patients, with or without microtransferrinuria. When transferrin absorption was plotted against the filtered load of transferrin, the regression lines for the three subject groups were parallel. The regression line for NIDDM patients with microtransferrinuria was shifted to the right of those for healthy controls and NIDDM patients with a normal TfER. These findings suggest that microtransferrinuria in patients with NIDDM is caused by the impaired tubular reabsorption of transferrin.

Adult↗
PubMed1992

Differential regulation and polyadenylation of transferrin mRNA in Xenopus liver and oviduct.

Estrogen destabilizes transferrin mRNA in male Xenopus liver in the same manner as observed for albumin and gamma-fibrinogen. The present study examined estrogen regulation of transferrin gene expression in female Xenopus liver and oviduct. In female Xenopus liver estrogen causes the same enhanced degradation of transferrin mRNA from the cytoplasm as seen in males. In contrast, transferrin is induced 3- to 4-fold in both oviduct nuclear and cytoplasmic RNA. The similar increase in transferrin RNA in both preparations suggests a transcriptional mechanism is responsible for this stimulation. Therefore, transferrin expression is differentially regulated in these tissues by the same hormone. Previous experiments showed that Xenopus serum albumin mRNA has a very short (17 residue) poly(A) tail that may play a role in its hormone-regulated instability. Transferrin mRNA has a similarly short poly(A) tail in liver of both male and female Xenopus. Estrogen has no effect on transferrin polyadenylation in liver. Similarly short poly(A) is found on transferrin mRNA from estrogen-deprived oviducts in explant culture. However, addition of estradiol to the medium results in the appearance of a 50-200 nucleotide poly(A) concurrent with induction. Therefore, transferrin mRNA is differentially polyadenylated in Xenopus liver and oviduct. In the latter tissue polyadenylation is under hormonal control.

Animals↗
PubMed2006

A novel method to quantify in vivo transferrin glycation: applications in diabetes mellitus.

BACKGROUND: In vitro glycation of transferrin leads to increased oxidative stress by impairing iron-binding antioxidant capacity. The aim of this study is to develop a method to evaluate in vivo transferrin glycation in diabetes. METHODS: We adapted the nitroblue tetrazolium assay to measure in micro-well plates the fructosamine content of transferrin isolated from serum by immunocomplexation. RESULTS: Introduction of the immunocomplexation step did not affect the analytical performance of the fructosamine measurement and analytical variability was lower than 7%. The diabetic group (n=107) had significantly higher transferrin glycation (1.39+/-1.12 versus 0.79+/-1.09 micromol fructosamine/g transferrin in the non-diabetic group, n=91, p<0.0005) and this was most pronounced in type 1 diabetes (1.95+/-1.02 versus 1.06+/-1.04 micromol fructosamine/g transferrin in type 2, p<0.0005). Transferrin glycation was associated with parameters of glycaemic control but did not correlate with serum iron or total iron-binding capacity. Total iron-binding capacity was lower in type 1 diabetes (63+/-9 versus 69+/-12 micromol/l in type 2, p<0.05) and was mainly determined by transferrin concentration. CONCLUSIONS: These results indicate that the adapted nitroblue tetrazolium assay combined with immunocomplexation of serum transferrin is suitable to detect differences in in vivo transferrin glycation between non-diabetic, type 1 and type 2 diabetic subjects.

Diabetes Mellitus↗
PubMed1999

Differential response of non-transferrin bound iron uptake in rat liver cells on long-term and short-term treatment with iron.

BACKGROUND: Uptake of non-transferrin-bound iron by the liver is important as a clearance mechanism in iron overload. In contrast to physiological uptake via receptor-mediated endocytosis of transferrin, no regulatory mechanisms for this process are known. This study compares the influence of long-term and short-term depletion and loading of hepatocytes with iron on the uptake of non-transferrin bound iron, its affinity, specificity and the interaction with the transferrin-mediated pathways. METHODS: Rats were fed iron-deficient, normal and 3,5,5-trimethylhexanoyl-ferrocene-containing diets to obtain livers with the corresponding desired status and the hepatocytes from these livers were used for transport studies. Hepatocytes from normal rats were depleted or loaded with iron by short-term treatment with desferrioxamine or ferric ammonium citrate, respectively. Uptake of non-transferrin bound iron was assayed from ferric citrate and from ferric diethylene triammine pentaacetate. RESULTS: Uptake of non-transferrin-bound iron in hepatocytes could be seen as consisting of a high-affinity (Km=600 nM) and a low-affinity component. Whereas in normal and in iron-starved rats the high-affinity component was more prominent, it disappeared altogether in hepatocytes from rats with iron overload resulting from prolonged feeding with TMH-ferrocene-enriched diet. Overloading also led to loss of inhibition by diferric transferrin, which occured in starved as well as normal cells. In contrast, short-term iron-depletion of isolated hepatocytes with desferrioxamine had only a weak stimulatory effect, whereas treatment with ferric ammonium citrate strongly increased the uptake rates. However, the inhibition by diferric transferrin also disappeared. In both cases, uptake of non-transferrin bound iron was inhibited by apotransferrin. CONCLUSIONS: Non-transferrin bound iron uptake in liver cells is apparently regulated by the iron status of the liver. The mode of response to iron loading depends on the method of loading in terms of time course and the form of iron used. It cannot be explained by the behavior of the iron regulatory protein, and it is complex, seeming to involve more than one transport system.

Animal Feed↗
PubMed1999

Time-course and localization of transferrin receptor expression in the substantia nigra of 6-hydroxydopamine-induced parkinsonian rats.

Parkinson's disease is a neurodegenerative disease characterized by dopaminergic cell death in the substantia nigra. The cause of the cell death is, however, obscure. Recently, accumulation of iron in the parkinsonian substantia nigra and iron-catalysed free radical generation have been proposed as possible causes of nigral cell death. The transferrin receptor has been implicated as a possible mediator of this iron accumulation in the parkinsonian substantia nigra. The present study investigated the distribution of transferrin receptor-immunoreactive proteins and its co-localization with tyrosine hydroxylase in the normal rat substantia nigra and their expressions in the parkinsonian substantia nigra from three days to three months after 6-hydroxydopamine lesioning. Computer image analysis of the grey mean of transferrin receptor staining in the microvessels was also employed. The results showed that the transferrin receptor immunolabelling was localized in some neurons and glial cells in the normal substantia nigra pars compacta and pars reticulata, and that about 54% of tyrosine hydroxylase-positive cells were also stained with transferrin receptor. There was a decrease of tyrosine hydroxylase- and transferrin receptor-positive cells in the 6-hydroxydopamine-lesioned substantia nigra. The grey mean of transferrin receptor staining in microvessels in the lesioned substantia nigra was, however, not different from that in the control. It was concluded that transferrin receptors in neurons, glial cells and microvessels might not be responsible for iron accumulation in the parkinsonian substantia nigra. The loss of transferrin receptor-immunopositive cells might, however, partly be accounted for by the death of transferrin receptor-positive dopaminergic cells induced by 6-hydroxydopamine lesioning.

Animals↗
PubMedDate not supplied

Transferrin-containing, cyclodextrin polymer-based particles for tumor-targeted gene delivery.

Transferrin is a well-studied ligand for tumor targeting due to upregulation of transferrin receptors in numerous cancer cell types. Here, we report the development of a transferrin-modified, cyclodextrin polymer-based gene delivery system. The delivery system is comprised of a nanoparticle (formed by condensation of a cyclodextrin polycation with nucleic acid) that is surface-modified to display poly(ethylene glycol) (PEG) for increasing stability in biological fluids and transferrin for targeting of cancer cells that express transferrin receptor. A transferrin-PEG-adamantane conjugate is synthesized for nanoparticle modification. The transferrin conjugate retains high receptor binding and self-assembles with the nanoparticles by adamantane (host) and particle surface cyclodextrin (guest) inclusion complex formation. At low transferrin modification, the particles remain stable in physiologic salt concentrations and transfect K562 leukemia cells with increased efficiency over untargeted particles. The increase in transfection is eliminated when transfections are conducted in the presence of excess free transferrin. The transferrin-modified nanoparticles are appropriate for use in the systemic delivery of nucleic acid therapeutics for metastatic cancer applications.

Adamantane↗
PubMed1977

Preferential utilization in vitro of iron bound to diferric transferrin by rabbit reticulocytes.

59Fe uptake by rabbit reticulocytes from human transferrin-bound iron was studied by using transferrin solutions (35, 50, 65, 80 and 100% saturated with iron) whose only common characteristic was their content of diferric transferrin. During the early incubation period, 59Fe uptake from each preparation by reticulocytes was identical despite wide variations in amounts of total transferrin, total iron, monoferric transferrin and apotransferrin in solution. During the later phase of incubation, rate of uptake declined and was proportional to each solution's monoferric transferrin content. Uptake was also studied in a comparative experiment which used two identical, partially saturated transferrin preparations, one uniformly 59Fe-labelled and the other tracer-labelled with [59Fe]diferric transferrin. In both experiments, iron uptake by reticulocytes corresponded to utilization of a ferric ion from diferric transferrin before utilization of iron from monoferric transferrin.

Animals↗