Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Transferrin”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 937 records · Page 52Linked to original sources
PubMed2001

Rapid transferrin efflux from brain to blood across the blood-brain barrier.

The brain efflux index method is used to examine the extent to which transferrin effluxes from brain to blood across the blood-brain barrier (BBB) following intracerebral injection. Whereas high-molecular-weight dextran is nearly 100% retained in brain for up to 90 min after intracerebral injection in the Par2 region of the parietal cortex of brain, there is rapid efflux of transferrin from brain to blood across the BBB. The efflux of apotransferrin is 3.5-fold faster than the efflux of holo-transferrin. The brain to blood efflux of apotransferrin is completely saturable by unlabeled transferrin, but is not inhibited by other plasma proteins. These studies provide evidence for reverse transcytosis of transferrin from brain to blood across the BBB. As circulating transferrin is known to undergo transcytosis across the BBB in the blood-to-brain direction, these studies support the model of bidirectional transcytosis of transferrin through the BBB in vivo.

Animals↗
PubMed1998

Total iron-binding capacity-estimated transferrin correlates with the nutritional subjective global assessment in hemodialysis patients.

We examined the value of transferrin concentrations in estimating nutritional status as determined by the subjective global assessment (SGA) score. Fifty-nine hemodialysis patients (37 men and 22 women, aged 59+/-16 years, dialyzed for 3.6+/-3.9 years) were selected by predetermined criteria. All received erythropoietin (EPO) and oral iron therapy. SGA evaluation was conducted twice by both a dietitian and a physician. Serum iron, total iron-binding capacity (TIBC; which is linearly correlated with transferrin), transferrin saturation ratio, ferritin, albumin, total protein, and cholesterol were measured. Twenty-seven (46%) patients were well nourished (group A), 20 (34%) were moderately nourished (group B), and 12 (20%) were poorly nourished (group C) according to the SGA. TIBC values were 276+/-47 mg/dL, 217+/-54 mg/dL, and 176+/-41 mg/dL, respectively (P < 0.00001), and thus directly correlated with the state of nutrition. The relationship between TIBC and nutritional status was independent of age and number of years on hemodialysis. Serum ferritin values were 104+/-93 ng/mL, 161+/-154 ng/mL, and 363+/-305 ng/mL, respectively (P < 0.0003), and thus inversely correlated with the state of nutrition. Transferrin saturation ratios were slightly higher in the severely malnourished patients. The number of years on dialysis were a determinant of nutritional status. These values were 2.4+/-2.4 years for group A, 3.9+/-4.0 years for group B, and 5.7+/-3.9 years for group C (P < 0.05). The average age of the poorly nourished patients was 10 years older than the well-nourished patients. Serum iron values were lower but transferrin saturation ratios were higher in the severely malnourished patients. The required EPO doses were higher in the poorly nourished patients. We suggest that transferrin values are superior to other laboratory tests in assessing nutrition and will supplement SGA criteria. Serum ferritin may be useful as a predictor of illness. Older patients who have been on dialysis longer warrant special concern. Malnutrition may be an indicator of EPO resistance in dialysis patients. Finally, since a decreased TIBC level in poorly nourished patients may erroneously increase the transferrin saturation ratio, our findings may have implications in making the diagnosis and treatment of anemia and iron deficiency in malnourished dialysis patients.

Adult↗
PubMed2001

Transferrin but not albumin mediates stimulation of complement C3 biosynthesis in human proximal tubular epithelial cells.

Complement is increasingly implicated in the pathogenesis of progressive renal disease resulting from persistent proteinuria. We have previously shown that apical serum proteins stimulate C3 in cultured human proximal tubular epithelial cells (PTECs), and that the stimulant is a nonalbumin compound of 30 to 100 kd. We postulated in this study that transferrin and apotransferrin, also important components of proteinuric urine in this molecular-weight range, might be the culprit. Human PTECs were obtained by differential sieving of renal cortical tissue from the normal pole of tumor nephrectomy specimens and characterized to be predominantly of proximal tubular origin. Complement C3 messenger RNA (mRNA) expression was analyzed in confluent growth-arrested PTEC monolayers in media containing different concentrations (2.5 to 20 mg/mL) of transferrin by reverse transcription and polymerase chain reaction. Pure human albumin was used as a control protein. C3 protein secretion was detected and quantified by a sandwich enzyme-linked immunosorbent assay on cell culture supernatants after distinct time points. Transferrin enhanced the rate of C3 secretion in a dose-dependent manner, reaching maximal stimulation at doses of 10 mg/mL. Selected experiments using the Transwell technique showed that C3 release was predominantly apical in the resting state. The addition of 10 mg/mL of transferrin apically but not basolaterally stimulated both apical and basolateral C3 secretion and increased the basolateral-apical ratio of C3 secretion from 0.45 +/- 0.16 to 0.93 +/- 0.24 (P: < 0.02). Constitutive C3 mRNA expression was upregulated by transferrin in a time- and dose-dependent fashion, reaching a peak after 24 hours. A similar degree of C3 upregulation was reproduced when iron-poor transferrin, apotransferrin, was used instead. These results indicate that C3 synthesis in PTECs is upregulated by transferrin, for which protein rather than iron moiety may account for the observed effects. These findings provide evidence linking proteinuria with overexpression of tubular complement.

Apoproteins↗
PubMed1998

Insulin antagonism: a novel role for human serum transferrin.

We have purified alpha2-glycoprotein (alpha2-GP), an insulin antagonist from human plasma which is induced by growth hormone (GH), and shown that pure alpha2-GP is a potent antagonist of severe insulin-induced hypoglycemia, producing acute hyperglycemia in intact rats and ketonuria in diabetic rats. The N-terminal amino acid sequence of alpha2-GP and the reactivity of alpha2-GP with an antitransferrin monoclonal antibody show that alpha2-GP is identical to human serum transferrin. Furthermore, pure human serum transferrin and non-glycosylated recombinant human transferrin reproduce the insulin antagonist effects of alpha2-GP in rats, whereas ovotransferrin shows no such effect. The neutralization of the insulin antagonism of human serum transferrin by an anti-transferrin monoclonal antibody shows that transferrin has a new function as a potent insulin antagonist. This novel role for human serum transferrin in the regulation of glucose metabolism provides a reasonable mechanism for the diabetogenic effect of GH, and has important implications for the etiology and progression of diabetes.

Amino Acid Sequence↗
PubMed2002

Iron uptake from plasma transferrin by the duodenum is impaired in the Hfe knockout mouse.

Hereditary hemochromatosis (HH) is a disorder of iron metabolism in which enhanced iron absorption of dietary iron causes increased iron accumulation in the liver, heart, and pancreas. Most individuals with HH are homozygous for a C282Y mutation in the HFE gene. The function of HFE protein is unknown, but it is hypothesized that it acts in association with beta(2)-microglobulin and transferrin receptor 1 to regulate iron uptake from plasma transferrin by the duodenum, the proposed mechanism by which body iron levels are sensed. The aim of this study was to test this hypothesis by comparing clearance of transferrin-bound iron in Hfe knockout (KO) mice with that observed in C57BL/6 control mice. The mice were fed either an iron-deficient, control, or iron-loaded diet for 6 weeks to alter body iron status. The mice then were injected i.v. with (59)Fe-transferrin, and blood samples were taken over 2 h to determine the plasma (59)Fe turnover. After 2 h, the mice were killed and the amount of radioactivity in the duodenum, liver, and kidney was measured. In both Hfe KO and C57BL/6 mice, plasma iron turnover and iron uptake from plasma transferrin by the duodenum, liver, and kidney correlated positively with plasma iron concentration. However, duodenal iron uptake from plasma transferrin was decreased in the Hfe KO mice compared with the control mice. Despite this difference in duodenal uptake, the Hfe KO mice showed no decrease in iron uptake by the liver and kidney or alteration in the plasma iron turnover when compared with C57BL/6 mice. These data support the hypothesis that HFE regulates duodenal uptake of transferrin-bound iron from plasma, and that this mechanism of sensing body iron status, as reflected in plasma iron levels, is impaired in HH.

Animals↗
PubMed1979

Identification of transferrin receptors on the surface of human cultured cells.

We have examined the binding of human transferrin to cultured human choriocarcinoma cell lines and to detergent extracts of such cells. The results indicate the presence of a high-affinity saturable binding site (Ka = 4.25 x 10(8) M-1) that is specific for transferrin. This receptor has also been detected on three other human cell lines of different phenotypic origin, including Wil-2 (splenic lymphocytes of B-cell origin), RPMI-2650 (a quasi-diploid nasopharyngeal carcinoma), and WI-38 (embryonic lung fibroblasts). By using anti-human transferrin antiserum to immunoprecipitate the receptor-transferrin complex from detergent extracts of cells containing saturating levels of transferrin followed by sodium dodecyl sulfate/polyacrylamide gel electrophoresis, a single polypeptide of 90,000 daltons has been identified as a subunit of the putative transferrin receptor. The protein shows immunochemical identity and coelectrophoreses in sodium dodecyl sulfate gels with a cell surface glycoprotein subunit, previously identified in placental brush border membrane preparations, on all human cultured cell lines examined. These results suggest that the recent demonstration of transferrin dependence of maximal cell growth in culture [e.g., Hutchings, S.E. & Sato, G.H. (1978) Proc. Natl. Acad. Sci. USA 75, 901-904] is mediated through expression of this glycoprotein receptor.

Cell Line↗
PubMed1983

pH and the recycling of transferrin during receptor-mediated endocytosis.

At pH 5.4 apotransferrin (iron-free transferrin) binds to cell-surface transferrin receptors to the same extent and with the same affinity as does diferric transferrin at pH 7.0. Apotransferrin is quickly dissociated from its receptor when the pH is raised to 7.0. These and other results strongly support a simple model that explains the cycling of transferrin during a single cycle of receptor-mediated endocytosis. Diferric transferrin binds to cell-surface receptors, and the transferrin-receptor complex is endocytosed. The pH of the endocytic vesicle is lowered to 5.5 or below; this causes dissociation of iron from the transferrin-receptor complex, but apotransferrin remains bound to its receptor. The iron remains within the cell, and the apotransferrin-receptor complex is recycled to the cell surface. Upon encountering the neutral pH of the medium, apotransferrin is dissociated from the cell.

Animals↗
PubMed1997

Mosquito transferrin, an acute-phase protein that is up-regulated upon infection.

When treated with heat-killed bacterial cells, mosquito cells in culture respond by up-regulating several proteins. Among these is a 66-kDa protein (p66) that is secreted from cells derived from both Aedes aegypti and Aedes albopictus. p66 was degraded by proteolysis and gave a virtually identical pattern of peptide products for each mosquito species. The sequence of one peptide (31 amino acids) was determined and found to have similarity to insect transferrins. By using conserved regions of insect transferrin sequences, degenerate oligonucleotide PCR primers were designed and used to isolate a cDNA clone encoding an A. aegypti transferrin. The encoded protein contained a signal sequence that, when cleaved, would yield a mature protein of 68 kDa. It contained the 31-amino acid peptide, and the 3' end exactly matched a cDNA encoding a polypeptide that is up-regulated when A. aegypti encapsulates filarial worms [Beerntsen, B. T., Severson, D. W. & Christensen, B. M. (1994) Exp. Parasitol. 79, 312-321]. This transferrin, like those of two other insect species, has conserved iron-binding residues in the N-terminal lobe but not in the C-terminal lobe, which also has large deletions in the polypeptide chain, compared with transferrins with functional C-terminal lobes. The hypothesis is developed that this transferrin plays a role similar to vertebrate lactoferrin in sequestering iron from invading organisms and that degradation of the structure of the C-terminal lobe might be a mechanism for evading pathogens that elaborate transferrin receptors to tap sequestered iron.

Aedes↗
PubMed2007

A multicopper ferroxidase involved in iron binding to transferrins in Dunaliella salina plasma membranes.

The halotolerant alga Dunaliella salina is unique among plants in that it utilizes a transferrin (TTf) to mediate iron acquisition (Fisher, M., Zamir, A., and Pick, U. (1998) J. Biol. Chem. 273, 17553-17558). Two new proteins that are induced by iron deprivation were identified in plasma membranes of D. salina as follows: a multicopper ferroxidase termed D-Fox and an internally duplicated glycoprotein (p130B). D-Fox and p130B are accessible to glycolytic, proteolytic, and biotin surface tagging treatments, suggesting that they are surface-exposed glycoproteins. Induction of D-Fox was also manifested by ferroxidase activity in plasma membrane preparations. These results are puzzling because ferroxidases in yeast and in Chlamydomonas reinhardtii function in redox-mediated iron uptake, a mechanism that is not known to operate in D. salina. Two lines of evidence suggest that D-Fox and p130B interact with D. salina triplicated transferrin (TTf). First, chemical cross-linking combined with mass spectroscopy analysis showed that D-Fox and p130B associate with TTf and with another plasma membrane transferrin. Second, detergent-solubilized D-Fox and p130B comigrated on blue native gels with plasma membrane transferrins. 59Fe autoradiography indicated that this complex binds Fe3+ ions. Also, the induction of D-Fox and p130B is kinetically correlated with enhanced iron binding and uptake activities. These results suggest that D-Fox and p130B associate with plasma membrane transferrins forming a complex that enhances iron binding and iron uptake. We propose that the function of D-Fox in D. salina has been modified during evolution from redox-mediated to transferrin-mediated iron uptake, following a gene transfer event of transferrins from an ancestral animal cell.

Algal Proteins↗
PubMed2005

Structural allostery and binding of the transferrin*receptor complex.

The structural allostery and binding interface for the human serum transferrin (Tf)*transferrin receptor (TfR) complex were identified using radiolytic footprinting and mass spectrometry. We have determined previously that the transferrin C-lobe binds to the receptor helical domain. In this study we examined the binding interactions of full-length transferrin with receptor and compared these data with a model of the complex derived from cryoelectron microscopy (cryo-EM) reconstructions (Cheng, Y., Zak, O., Aisen, P., Harrison, S. C. & Walz, T. (2004) Structure of the human transferrin receptor.transferrin complex. Cell 116, 565-576). The footprinting results provide the following novel conclusions. First, we report characteristic oxidations of acidic residues in the C-lobe of native Tf and basic residues in the helical domain of TfR that were suppressed as a function of complex formation; this confirms ionic interactions between these protein segments as predicted by cryo-EM data and demonstrates a novel method for detecting ion pair interactions in the formation of macromolecular complexes. Second, the specific side-chain interactions between the C-lobe and N-lobe of transferrin and the corresponding interactions sites on the transferrin receptor predicted from cryo-EM were confirmed in solution. Last, the footprinting data revealed allosteric movements of the iron binding C- and N-lobes of Tf that sequester iron as a function of complex formation; these structural changes promote tighter binding of the metal ion and facilitate efficient ion transport during endocytosis.

Allosteric Regulation↗
PubMed1976

Serum albumin and transferrin protein-energy malnutrition. Their use in the assessment of marginal undernutrition and the prognosis of severe undernutrition.

1. Deficits in weight- and length-for-age, and serum albumin and transferrin concentrations were determined for children who were either marginally undernourished (twenty-five children) or suffering from either marasmus (thirty-two children) or kwashiorkor (twenty-six children) defined according to the Wellcome Classification (Waterlow, 1972). The measurements were also made in eight children with kwashiorkor after the loss of oedema, and in sixteen children who were recovering from either marasmus or kwashiorkor. 2. The mean concentration of serum albumin was similar for children from the 'under-nourished' group and from the group with marasmus, but was significantly reduced in those with kwashiorkor. 3. The concentration of serum transferrin was significantly reduced in both the group of children with marasmus and those with kwashiorkor. The serum transferrin concentration was significantly lower in children with kwashiorkor when compared with the level in those with marasmus. 4. Seventeen children (seven with kwashiorkor and ten with marasmus) died. These children were neither lighter nor shorter than the severely malnourished children who survived. The concentration of serum albumin was not lower in the children who died than in those who survived. 5. In contrast to the results for serum albumin concentrations, the children who died had significantly lower levels of serum transferrin than those who survived. 6. There was a significant linear relationship between serum transferrin concentrations and the deficits in length-for-age (P less than 0-05) and weight-for-length (P less than 0-001) in the marginally undernourished children. The deficit in weight-for-length was also linearly related to the serum transferrin concentrations (P less than 0-001) in children recovering from severe malnutrition. 7. It is suggested that the measurement of serum transferrin concentrations provides an index of severity in severely malnourished children, and should prove useful in field assessments of nutritional status.

Body Weight↗
PubMed1983

Identification of transferrin as the principal plutonium-binding protein in the blood serum and liver cytosol of rats: immunological and chromatographic studies.

An analysis of 239Pu-labelled protein complexes in serum and liver cytosol fractions prepared from rats injected intravenously with 239Pu-citrate indicated that among the possible metal-binding proteins, ferritin, transferrin and metallothionein, 239Pu was bound almost exclusively to transferrin. The method employed for the quantitative determination of 239Pu-transferrin was chromatography on immobilized rabbit anti-rat apo-transferrin. There was no evidence that transferrins from serum and liver cytosol are serologically different. The residual blood content of perfused and non-perfused liver was measured using 51Cr-labelled red blood cells and the amounts of blood-derived 239Pu and 239Pu-transferrin in the liver cytosol were calculated. The results are discussed with respect to the possible role of transferrin in the uptake of Pu into cells.

Animals↗
PubMed2003

Transferrin modifications and lipid peroxidation: implications in diabetes mellitus.

Free iron is capable of stimulating the production of free radicals which cause oxidative damage such as lipid peroxidation. One of the most important mechanisms of antioxidant defense is thus the sequestration of iron in a redox-inactive form by transferrin. In diabetes mellitus, increased oxidative stress and lipid peroxidation contribute to chronic complications but it is not known if this is related to abnormalities in transferrin function. In this study we investigated the role of transferrin concentration and glycation. The antioxidant capacity of apotransferrin to inhibit lipid peroxidation by iron-binding decreased in a concentration-dependent manner from 89% at > or = 2 mg/ml to 42% at 0.5 mg/ml. Pre-incubation of apotransferrin with glucose for 14 days resulted in a concentration-dependent increase of glycation: 1, 5 and 13 micromol fructosamine/g transferrin at 0, 5.6 and 33.3 mmol/l glucose respectively, p < 0.001. This was accompanied by a decrease in the iron-binding antioxidant capacity of apotransferrin. In contrast, transferrin glycation by up to 33.3 mmol/l glucose did not affect chemiluminescence-quenching antioxidant capacity, which is iron-independent. Colorimetric evaluation of total iron binding capacity in the presence of an excess of iron (iron/transferrin molar ratio = 2.4) also decreased from 0.726 to 0.696 and 0.585mg/g transferrin after 0, 5.6 and 33.3 mmol/l glucose, respectively, p < 0.01. In conclusion, these results suggest that lower transferrin concentration and its glycation can, by enhancing the pro-oxidant effects of iron, contribute to the increased lipid peroxidation observed in diabetes.

Animals↗
PubMed2005

Bovine and canine transferrin inhibit the growth of Malassezia pachydermatis in vitro.

Transferrin, an iron-binding beta-globulin protein that transports iron to mammalian cells, may contribute to innate immunity to fungal pathogens, primarily by limiting microbial access to iron. We investigated whether unsaturated (apo) canine and bovine transferrin had an inhibitory effect in vitro on Malassezia pachydermatis, an important opportunistic cutaneous yeast pathogen of dogs. M. pachydermatis strains were grown at 32 degrees C in 96-well culture plates using Sabouraud's liquid medium containing canine or bovine apo-transferrin at concentrations ranging from 10.6 to 0.7 mg/ml. Optical densities (OD492) in the treated and control wells were measured and then compared between treatments. Bovine and canine transferrin inhibited (P < 0.01) yeast growth at all concentrations tested after five and six days of incubation; inhibition by 5.3 mg/ml exceeded (P < 0.05) that of 0.7 mg/ml on day six. Unsaturated and saturated bovine transferrin had comparable inhibitory effects on the growth of four strains, indicating that the inhibitory effects of transferrin on M. pachydermatis are not dependent upon iron depletion. These studies suggest that transferrin may contribute to innate immunity to M. pachydermatis in dogs and cattle.

Animals↗
PubMed2002

Transferrin-facilitated lipofection gene delivery strategy: characterization of the transfection complexes and intracellular trafficking.

We previously showed that mixing transferrin with a cationic liposome prior to the addition of DNA, greatly enhanced the lipofection efficiency. Here, we report characterization of the transfection complexes in formulations prepared with transferrin, lipofectin, and DNA (pCMVlacZ) in various formulations. DNA in all the formulations that contain lipofectin was resistant to DNase I treatment. Transfection experiments performed in Panc 1 cells showed that the standard formulation, which was prepared by adding DNA to a mixture of transferrin and lipofectin, yielded highest transfection efficiency. There was no apparent difference in zeta potential among these formulations, but the most efficient formulation contained complexes with a mean diameter of three to four times that of liposome and the complexes in other gene delivery formulations. Transmission electron microscopic examination of the standard transfection complexes formulated using gold-labeled transferrin showed extended circular DNA decorated with transferrin as compared to extensively condensed DNA found in lipofectin-DNA complexes and heterogeneous structures in other formulations. By confocal microscopy, DNA and transferrin were found to colocalize at the perinuclear space and in the nucleus, suggesting cotransportation intracellularly, including nuclear transport. We propose that transferrin enhances the transfection efficiency of the standard lipofection formulation by preventing DNA condensation, and facilitating endocytosis and nuclear targeting.

Active Transport, Cell Nucleus↗
PubMed1997

Promotion of transferrin folding by cyclic interactions with calnexin and calreticulin.

Calnexin, an abundant membrane protein, and its lumenal homolog calreticulin interact with nascent proteins in the endoplasmic reticulum. Because they have an affinity for monoglucosylated N-linked oligosaccharides which can be regenerated from the aglucosylated sugar, it has been speculated that this repeated oligosaccharide binding may play a role in nascent chain folding. To investigate the process, we have developed a novel assay system using microsomes freshly prepared from pulse labeled HepG2 cells. Unlike the previously described oxidative folding systems which required rabbit reticulocyte lysates, the oxidative folding of transferrin in isolated microsomes could be carried out in a defined solution. In this system, addition of a glucose donor, UDP-glucose, to the microsomes triggered glucosylation of transferrin and resulted in its cyclic interaction with calnexin and calreticulin. When the folding of transferrin in microsomes was analyzed, UDP-glucose enhanced the amount of folded transferrin and reduced the disulfide-linked aggregates. Analysis of transferrin folding in briefly heat-treated microsomes revealed that UDP-glucose was also effective in elimination of heat-induced misfolding. Incubation of the microsomes with an alpha-glucosidase inhibitor, castanospermine, prolonged the association of transferrin with the chaperones and prevented completion of folding and, importantly, aggregate formation, particularly in the calnexin complex. Accordingly, we demonstrate that repeated binding of the chaperones to the glucose of the transferrin sugar moiety prevents and corrects misfolding of the protein.

Calcium-Binding Proteins↗
PubMed1996

YY1 and Sp1 transcription factors bind the human transferrin gene in an age-related manner.

The iron-binding protein transferrin has major roles in transporting, delivering, and sequestering ferric ions acquired by body tissues. Yet, during aging, serum transferrin levels decrease in humans. Likewise, in transgenic mice carrying chimeric human transferrin transgenes, liver expression of transferrin transgenes decreases with age. The aging regulation is due to decreased gene transcription. Electrophoretic mobility shift assays and antibody-recognition have revealed the binding of 5' regulatory elements of the human transferrin gene by three YY1 proteins, called YY1, YY1-a, and YY1-b, and an Sp1-a transcription factor. An age-related increase in YY1-a and YY1-b binding activities and a decrease in Sp1-like binding activity were shown. Since Sp1 is a positive transcription factor and YY1 can be a negative transcription factor, the alterations in their binding with age could cause the decreased transcription of the human transferrin transgene, and also the age-related decreased serum transferrin levels in humans.

Aging↗
PubMed1994

Change in glycosylation of chicken transferrin glycans biosynthesized during embryogenesis and primary culture of embryo hepatocytes.

Transferrins were isolated by immunoaffinity chromatography from chicken serum, chicken embryo serum and from the culture medium of chicken embryo hepatocytes in primary culture. The glycovariants of these three transferrins were separated by ion-exchange chromatography using a fast protein liquid chromatography (FPLC) system. The structures of the oligosaccharide-alditols released by hydrazinolysis from the glycovariants were compared after analysis by a combination of methanolysis, methylation analysis and 1H-NMR spectroscopy. In the three transferrins analysed, the oligosaccharides were of the biantennary N-acetyllactosaminic type, having several prominent features. In particular, the embryo serum transferrin glycan differed from that of chicken serum transferrin by the presence of a bisecting N-acetylglucosamine, suggesting a developmental change in glycosylation. The glycan structure of the transferrin secreted by the embryo hepatocytes in primary culture was marked by the presence of fucose (alpha 1-6) linked to the core N-acetylglucosamine, suggesting that expression of the fucosyltransferase activity is dependent on cell culture conditions. Moreover, comparative analysis of chicken serum transferrin and ovotransferrin glycans reinforces the idea that the glycosylation of two identical polypeptide chains is organ specific.

Animals↗