• Journal of Life Science
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• v.17 no.8 s.88
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• pp.1046-1052
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• 2007

Transferrin is a molecule carrying iron to store and maintain for iron homeostasis of living organisms. In this study, we have purified transferrin, as an iron-binding protein, from the last larval haemolymph of Papilio xuthus by KBr density gradient ultracentrifugation and gel filtration (superose 6 HR) using fast protein liquid chromatography (FPLC) and transferrin containing iron was identified by Ferene S staining. The purified haemolymph transferrin was shown to have molecular mass of 78 and 80 kDa and amino acid composition of transferrin was rich in aspartic acid, valine, leucine and glutamic acid. With immuno-diffusion assay, we confirmed the existence of the transferrin in the haemo-lymph and fat body by detection of visible and clear positive reaction. From the quantitative comparison by rocket immuno-electrophoresis process, the amount of transferrin were increased in the haemolymph of 3 days after pupation and the whole 5 days after pupation. Here, with biochemical and immunohistochemical analysis, we speculate the relationship of transferrin between the physical characteristics and distribution during metamorphosis of P. xuthus.

• YAKHAK HOEJI
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• v.33 no.5
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• pp.300-307
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• 1989

Expression of transferrin gene in various organs of rat was studied using rat transferrin cDNA. The hybridization method of $[^{35}S]-labeled$ transferrin cDNA with transferrin mRNA in cytoplasmic preparations was used to measure the level of transferrin mRNA. The rat from 15-day old fetus to 21-day old postnatal were employed as an animal model. In the liver, the level of transferrin mRNA increased with increasing age. However, the level of transferrin mRNA in brain was significantly lower than that in liver and the level did not increase with age.

• Nuclear Medicine and Molecular Imaging
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• v.40 no.3
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• pp.177-185
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• 2006

Purpose: Purpose of this study is to synthesize $^{99m}Tc$-labeled transferrin for injection imaging and to compare it with $^{67}Ga$-titrate for the detection of infectious foci. Materials and methods: Succinimidyl 6-hydrazino-nicotinate hydrochloride-chitosan-transferrin (Transferrin) was synthesized and radiolabeled with $^{99m}Tc$. Labeling efficiencies of $^{99m}Tc$-Transferrin were determined at 10 min, 30 min, 1 hr, 2 hr, 4 hr and 8 hr. Biodistribution and imaging studies with $^{99m}Tc$-Transferrin and $^{67}Ga$-citrate were performed in a rat abscess model induced with approximately $2{\times}10^8$ colony forming unit of Staphylococcus aureus ATCC 25923. Results: Successful synthesis of Transferrin was confirmed by mass spectrometry. Labeling efficiency of $^{99m}Tc$-Transferrin was $96.2{\pm}0.7%,\;96.4{\pm}0.5%,\;96.6{\pm}1.0%,\;96.9{\pm}0.5%,\;97.0{\pm}0.7%\;and\;95.5{\pm}0.7%$ at 10 min, 30 min, 1 hr, 2 hr, 4 hr and 8 hr, respectively. The injected dose per tissue gram of $^{99m}Tc$-Transferrin was $0.18{\pm}0.01\;and\;0.18{\pm}0.01$ in the lesion and $0.05{\pm}0.01\;and\;0.04{\pm}0.01$ in the normal muscle, and lesion-to-normal muscle uptake ratio was $3.7{\pm}0.6\;and\;4.7{\pm}0.4$ at 30 min and 3 hr, respectively. On image, lesion-to-background ratio of $^{99m}Tc$-Transferrin was $2.18{\pm}0.03,\;2.56{\pm}0.11,\;3.08{\pm}0.18,\;3.77{\pm}0.17,\;4.70{\pm}0.45\;and\;5.59{\pm}0.40$ at 10 min, 30 min, 1 hr, 2 hr, 4 hr and 10 hr and those of $^{67}Ga$-citrate was $3.06{\pm}0.84,\;4.12{\pm}0.54\;and\;4.55{\pm}0.74 $ at 2 hr, 24 hr and 48 hr, respectively. Conclusion: Transferrin is successfully labeled with $^{99m}Tc$, and its labeling efficiency was higher than 95% and stable for 8 hours. $^{99m}Tc$-Transferrin scintigraphy showed higher image quality in shorter time compared to $^{67}Ga$-citrate image. $^{99m}Tc$-transferrin is supposed to be useful in the detection of the infectious foci.

• Journal of Veterinary Clinics
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• v.34 no.2
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• pp.87-89
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• 2017

Apo-transferrin is an iron-binding protein that has been reported to have an antimicrobial effect. It is considered a major component of the host defense mechanism as it limits microbial access to iron. This study was performed to investigate whether bovine apo-transferrin would have an inhibitory effect on the growth of S. pseudintermedius, which is one of the most isolated bacteria from dogs, and to compare the antimicrobial efficacy with bovine holo-transferrin. S. pseudintermedius were grown at $37^{\circ}C$ in 96-well culture plates using Muller Hinton broth containing bovine apo-transferrin or bovine holo-transferrin at concentrations ranging from 0.5 or 2.5 to 5.0 mg/ml. The optical densities of the wells were then measured at 570 nm. In this study, the apo-transferrin showed dose-dependent antimicrobial effect against S. pseudintermedius while holo-transferrin did not inhibit the growth of S. pseudintermedius effectively. The results suggest that iron deprivation is an important pathway for inhibiting bacterial growth and bovine apo-transferrin has great antimicrobial effects against S. pseudintermedius.

• Journal of Pharmaceutical Investigation
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• v.29 no.4
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• pp.287-293
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• 1999

Transport study of horseradish peroxidase and transferrin-horseradish peroxidase conjugate was performed using an in vitro Caco-2 cell cultured monolayer grown on a polycarbonate membrane of $Transwell^{\circledR}$, Horseradish peroxidase was not transported across Caco-2 cell monolayer. Transferrin-horseradish peroxidase conjugate was transported through Caco-2 cell monolayer. The apparent membrane permeability coefficient $(P_{app})$ of transferrin horseradish peroxidase conjugate was $6.54{\times}10^{-7}\;cm/sec$. The $P_{app}$ value of transferrin-horseradish peroxidase conjugate across Caco-2 cell monolayer was increased to $11.9{\times}10^{-7}\;cm/sec$ in the presence of $50\;{mu}g/ml$ brefeldin-A. These results suggest the transferrin receptor mediated transcytosis of transferrin-horseradish peroxidase conjugate across Caco-2 cell monolayer.

• Journal of Microbiology
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• v.43 no.2
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• pp.183-190
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• 2005

Staphylococcus aureus is known to be capable of utilizing transferrin-bound iron, via both siderophore­and transferrin-binding protein (named IsdA)-mediated iron-acquisition systems. This study was designed in order to determine which iron-acquisition system plays the essential or dominant role with respect to the acquisition of iron from human transfenin, in the growth of S. aureus. Holotransferrin (HT) and partially iron-saturated transferrin (PT), but not apotransferrin (AT), were found to stimulate the growth of S. aureus. S. aureus consumed most of the transferrin-bound iron during the exponential growth phase. Extracellular proteases were not, however, involved in the liberation of iron from transferrin. Transferrin-binding to the washed whole cells via IsdA was not observed during the culture. The expression of IsdA was observed only in the deferrated media with AT, but not in the media supplemented with PT or HT. In contrast, siderophores were definitely produced in the deferrated media with PT and HT, as well as in the media supplemented with AT. The siderophores proved to have the ability to remove iron directly from transferrin, but the washed whole cells expressing IsdA did not. In the bioassay, the growth of S. aureus on transferrin-bound iron was stimulated by the siderophores alone. These results demonstrate that the siderophore-mediated iron-acquisition system plays a dominant and essential role in the uptake of iron from transferrin, whereas the IsdA-mediated iron-acquisition system may play only an ancillary role in the uptake of iron from transferrin.

• Preventive Nutrition and Food Science
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• v.3 no.3
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• pp.248-250
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• 1998

In this study, transferrin which is an iron-carrying glycoprotein in plasma was evaluted for its iron binding capacities(TIBC), iron solubilizing abilities, and enhancing effect of biological availbability of iron. Results of TIBC showed that 1 mg of transferrin could blind 1.28$\mu\textrm{g}$ of iron indicating that one molecule of transferrin can bind about 2 molecules of iron. Also, solubility of iorn (7.5$\mu\textrm{g}$ Fe/ml) was significantly incresed to 96.0% with addition of transferrin (5mg/ml) .When FeCl3(80$\mu\textrm{g}$ Fe/ml) was injected to iron-deficient rats by intestinal segment in situ technique, 18.4% of injected iron was absorbed wherease 48.49 and 48.76% of injected iron was absorbed with addition of 10 and 20 mg transferrin/ml , respectively.

• Journal of Aquaculture
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• v.2 no.1
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• pp.9-20
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• 1989

This study was taken to isolate transferrin fractions from the sera of tilapia(Oreochromis niloticus) by physico-chemical analyses such as the rivanol precipitation, iron-staining method, SDS-polyacrylamide gel electrophoresis and $^{59}FeCl_3$ autoradiography, and to calculate gene frequencies by using Hardy-Weinberg Law. The results obtained in this experiment were summarized as follow : 1. The transferrin fraction is composed of several components possessing relative lower electrophoretic mobilities and higher molecular sizes than the albumin components. 2. When different staining method was compared with transferrin in band, it was not found difference. 3. It was concluded that the optimun ratio of rivanol to serum was 2 : 1 and this ratio was used in all further fractionation. 4. The molecular weight of transferrin component was about 70,000 $\pm$ 2,000. 5. Tilapia transferrin fractionations were found to be polymorphic. 6. There transferrin variants(A, B and C) have been found in tilapia(Oreochromis niloticus) and Tf types were assumed to be controlled by three codominant alleles Tf A, Tf B and Tf C. Six different phenotypes can be theoretically expected Tf AA, Tf AB, Tf AC, Tf BB, Tf BC, and Tf CC. Only five types of these were observed and Tf CC types(homozygotes) was not found. 7. The frequencies of the three allele Tf A, Tf B and Tf C were 0.795, 0.15 and 0.055 respectively.

• Journal of Dairy Science and Biotechnology
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• v.35 no.3
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• pp.196-201
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• 2017

Recent studies have reported that certain lactic acid bacteria and their metabolites, such as exopolysaccharides (EPSs), have immunological effects and can modulate the immune system following oral administration. Lactococcus lactis subsp. cremoris FC is a lactic acid bacteria isolated from fermented milk from Caucasians and has been shown to produce EPSs. In this study, the effects of lactoferrins (apo-lactoferrin, holo-lactoferrin, and native-lactoferrin) and transferrins (apo-transferrin and holo-lactoferrin) on the growth of L. lactis subsp. cremoris FC were examined. The addition of lactoferrins and transferrins to L. lactis subsp. cremoris FC cultures was found to be effective at concentrations of 0.5 or 1 mg/mL.

• Animal cells and systems
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• v.13 no.3
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• pp.297-304
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• 2009

A complete mRNA sequence of transferrin from the wax moth, Galleria mellonella, was obtained, and compared with those of other species. We previously reported that the sequence was most similar to those of Manduca sexta and Bombyx mori. As in other moths, G. mellonella transferrin had only one iron-binding site at its N-terminal region. Semi-qRT PCR was conducted to investigate tissue-specific distribution and transcriptional regulation of the wax moth transferrin mRNA. Larval muscle and fat body contained larger quantity of mRNA than other tested tissues. In this study, it was observed that iron and cadmium regulated transferrin transcription, and this regulation pattern was tissue specific. Iron up-regulated transferrin mRNA level in fat body, while suppressed it in the Malpighian tubules and silk glands. Cadmium decreased the mRNA level in fat body, muscle, and Malpighian tubules, but significantly increased the mRNA level in silk glands. In addition, the mRNA expression was induced by all tested pathogen-associated molecular patterns (PAMPs) including LPS, lipoteichoic acid (LTA), glucan, and even chitin.