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Journal articles on the topic 'Transferrin'

Author: Grafiati

Published: 4 June 2021

Last updated: 28 July 2024

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1

FAST, Beate, Katrin KREMP, Michael BOSHART, and Dietmar STEVERDING. "Iron-dependent regulation of transferrin receptor expression in Trypanosoma brucei." Biochemical Journal 342, no. 3 (September 5, 1999): 691–96. http://dx.doi.org/10.1042/bj3420691.

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Transferrin is an essential growth factor for African trypanosomes. Here we show that expression of the trypanosomal transferrin receptor, which bears no structural similarity with mammalian transferrin receptors, is regulated by iron availability. Iron depletion of bloodstream forms of Trypanosoma brucei with the iron chelator deferoxamine resulted in a 3-fold up-regulation of the transferrin receptor and a 3-fold increase of the transferrin uptake rate. The abundance of expression site associated gene product 6 (ESAG6) mRNA, which encodes one of the two subunits of the trypanosome transferrin receptor, is regulated 5-fold by a post-transcriptional mechanism. In mammalian cells the stability of transferrin receptor mRNA is controlled by iron regulatory proteins (IRPs) binding to iron-responsive elements (IREs) in the 3′-untranslated region (UTR). Therefore, the role of a T. brucei cytoplasmic aconitase (TbACO) that is highly related to mammalian IRP-1 was investigated. Iron regulation of the transferrin receptor was found to be unaffected in δaco::NEO/δaco::HYG null mutants generated by targeted disruption of the TbACO gene. Thus, the mechanism of post-transcriptional transferrin receptor regulation in trypanosomes appears to be distinct from the IRE/IRP paradigm. The transferrin uptake rate was also increased when trypanosomes were transferred from medium supplemented with foetal bovine serum to medium supplemented with sera from other vertebrates. Due to varying binding affinities of the trypanosomal transferrin receptor for transferrins of different species, serum change can result in iron starvation. Thus, regulation of transferrin receptor expression may be a fast compensatory mechanism upon transmission of the parasite to a new host species.

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2

Kawabata, Hiroshi. "Transferrin and transferrin receptors update." Free Radical Biology and Medicine 133 (March 2019): 46–54. http://dx.doi.org/10.1016/j.freeradbiomed.2018.06.037.

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3

Carlevaro, Mariella F., Adriana Albini, Domenico Ribatti, Chiara Gentili, Roberto Benelli, Silvia Cermelli, Ranieri Cancedda, and Fiorella Descalzi Cancedda. "Transferrin Promotes Endothelial Cell Migration and Invasion: Implication in Cartilage Neovascularization." Journal of Cell Biology 136, no. 6 (March 24, 1997): 1375–84. http://dx.doi.org/10.1083/jcb.136.6.1375.

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During endochondral bone formation, avascular cartilage differentiates to hypertrophic cartilage that then undergoes erosion and vascularization leading to bone deposition. Resting cartilage produces inhibitors of angiogenesis, shifting to production of angiogenic stimulators in hypertrophic cartilage. A major protein synthesized by hypertrophic cartilage both in vivo and in vitro is transferrin. Here we show that transferrin is a major angiogenic molecule released by hypertrophic cartilage. Endothelial cell migration and invasion is stimulated by transferrins from a number of different sources, including hypertrophic cartilage. Checkerboard analysis demonstrates that transferrin is a chemotactic and chemokinetic molecule. Chondrocyte-conditioned media show similar properties. Polyclonal anti-transferrin antibodies completely block endothelial cell migration and invasion induced by purified transferrin and inhibit the activity produced by hypertrophic chondrocytes by 50–70% as compared with controls. Function-blocking mAbs directed against the transferrin receptor similarly reduce the endothelial migratory response. Chondrocytes differentiating in the presence of serum produce transferrin, whereas those that differentiate in the absence of serum do not. Conditioned media from differentiated chondrocytes not producing transferrin have only 30% of the endothelial cell migratory activity of parallel cultures that synthesize transferrin. The angiogenic activity of transferrins was confirmed by in vivo assays on chicken egg chorioallantoic membrane, showing promotion of neovascularization by transferrins purified from different sources including conditioned culture medium. Based on the above results, we suggest that transferrin is a major angiogenic molecule produced by hypertrophic chondrocytes during endochondral bone formation.

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4

Sarich, V. M. "Transferrin." Transactions of the Zoological Society of London 33, no. 2 (July 8, 2010): 165–71. http://dx.doi.org/10.1111/j.1096-3642.1976.tb00050.x.

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5

Li, Hongyan, and Zhong Ming Qian. "Transferrin/transferrin receptor-mediated drug delivery." Medicinal Research Reviews 22, no. 3 (March 26, 2002): 225–50. http://dx.doi.org/10.1002/med.10008.

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6

Farhud, D. D., P. Daneshmand, M. Saffari, R. Hackler, and K. Altland. "Transferrin subtypes in Iran." Anthropologischer Anzeiger 48, no. 4 (December 19, 1990): 347–50. http://dx.doi.org/10.1127/anthranz/48/1990/347.

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7

Xin, Vechtova, Shaliutina-Kolesova, Fussy, Loginov, Dzyuba, Linhart, et al. "Transferrin Identification in Sterlet (Acipenser ruthenus) Reproductive System." Animals 9, no. 10 (September 30, 2019): 753. http://dx.doi.org/10.3390/ani9100753.

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Transferrins are a superfamily of iron-binding proteins and are recognized as multifunctional proteins. In the present study, transcriptomic and proteomic methods were used to identify transferrins in the reproductive organs and sperm of out-of-spawning and spermiating sterlet (Acipenser ruthenus) males. The results showed that seven transferrin transcripts were identified in the transcriptome of sterlet, and these transcripts were qualified as two different transferrin genes, serotransferrin and melanotransferrin, with several isoforms present for serotransferrin. The relative abundance of serotransferrin isoforms was higher in the kidneys and Wolffian ducts in the spermiating males compared to out-of-spawning males. In addition, transferrin was immunodetected in sterlet seminal plasma, but not in sterlet spermatozoa extract. Mass spectrometry identification of transferrin in seminal plasma but not in spermatozoa corroborates immunodetection. The identification of transferrin in the reproductive organs and seminal plasma of sterlet in this study provides the potential function of transferrin during sturgeon male reproduction.

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8

Bou Abdallah, Fadi, and Jean-Michel El Hage Chahine. "Transferrins. Hen ovo-transferrin, interaction with bicarbonate and iron uptake." European Journal of Biochemistry 258, no. 3 (December 15, 1998): 1022–31. http://dx.doi.org/10.1046/j.1432-1327.1998.2581022.x.

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9

Huebers, H. A., and C. A. Finch. "The physiology of transferrin and transferrin receptors." Physiological Reviews 67, no. 2 (April 1987): 520–82. http://dx.doi.org/10.1152/physrev.1987.67.2.520.

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10

Yu, Ronghua, and Anthony B. Schryvers. "Transferrin receptors on ruminant pathogens vary in their interaction with the C-lobe and N-lobe of ruminant transferrins." Canadian Journal of Microbiology 40, no. 7 (July 1, 1994): 532–40. http://dx.doi.org/10.1139/m94-086.

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The interaction between ruminant transferrins and receptor proteins on the surface of the ruminant pathogens Pasteuerella haemolytica, Haemophilus somnus, Pasteurella multocida, Haemophilus agnii, and Moraxella bovis was evaluated by a combination of binding assays and affinity isolation procedures. Membranes isolated from P. haemolytica, P. multocida, and H. agnii were capable of binding sheep, goat, and cattle transferrins whereas binding by membranes from H. somnus and M. bovis was specific for bovine transferrin. Proteolytically derived bovine transferrin C-lobe was capable of inhibiting the interaction between bovine transferrin and both Tbpl and Tbp2 from P. haemolytica and M. bovis but only Tbpl from H. somnus and P. multocida. Proteolytically derived N-lobe inhibited the binding of P. multocida and H. somnus Tbp2 to bovine transferrin and the binding of bovine transferrin to the single receptor protein identified in H. agnii. The implications of these results regarding the nature of the ligand–receptor interaction and similarities of this interaction with ligand–receptor interactions in different species are discussed.Key words: iron acquisition, transferrin receptor, binding specificity, Pasteurella, ruminants.

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11

Hadden, Jonathan M., Michael Bloemendal, Parvez I. Haris, Surjit K. S. Srai, and Dennis Chapman. "Fourier transform infrared spectroscopy and differential scanning calorimetry of transferrins: human serum transferrin, rabbit serum transferrin and human lactoferrin." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1205, no. 1 (March 1994): 59–67. http://dx.doi.org/10.1016/0167-4838(94)90092-2.

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12

Graham, Ross M., Gail M. Reutens, Carly E. Herbison, Roheeth D. Delima, Anita C. G. Chua, John K. Olynyk, and Debbie Trinder. "Transferrin receptor 2 mediates uptake of transferrin-bound and non-transferrin-bound iron." Journal of Hepatology 48, no. 2 (February 2008): 327–34. http://dx.doi.org/10.1016/j.jhep.2007.10.009.

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13

Strobos, Jur, Paul Seligman, and Allen Nissenson. "Transferrin oversaturation." American Journal of Kidney Diseases 34, no. 2 (August 1999): 401–2. http://dx.doi.org/10.1016/s0272-6386(99)70376-8.

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14

Wiwanitkit, Viroj. "Molecular Structure of Human Transferrin – Transferrin Receptor Complex." International Journal of Molecular Sciences 7, no. 7 (July 27, 2006): 197–203. http://dx.doi.org/10.3390/i7070197.

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15

Baynes, R. D. "Transferrin Reduces the Production of Soluble Transferrin Receptor." Experimental Biology and Medicine 209, no. 3 (July 1, 1995): 286–94. http://dx.doi.org/10.3181/00379727-209-43904.

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16

Johnson, Martha B., and Caroline A. Enns. "Diferric transferrin regulates transferrin receptor 2 protein stability." Blood 104, no. 13 (December 15, 2004): 4287–93. http://dx.doi.org/10.1182/blood-2004-06-2477.

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Abstract Transferrin receptor 2 (TfR2) is a type 2 transmembrane protein expressed in hepatocytes that binds iron-bound transferrin (Tf). Mutations in TfR2 cause one form of hereditary hemochromatosis, a disease in which excessive absorption of dietary iron can lead to liver cirrhosis, diabetes, arthritis, and heart failure. The function of TfR2 in iron homeostasis is unknown. We have studied the regulation of TfR2 in HepG2 cells. Western blot analysis shows that TfR2 increases in a time- and dose-dependent manner after diferric Tf is added to the culture medium. In cells exposed to diferric Tf, the amount of TfR2 returns to control levels within 8 hours after the removal of diferric Tf from the medium. However, TfR2 does not increase when non–Tf-bound iron (FeNTA) or apo Tf is added to the medium. The response to diferric Tf appears to be hepatocyte specific. Real-time quantitative reverse transcription–polymerase chain reaction (qRT-PCR) analysis shows that TfR2 mRNA levels do not change in cells exposed to diferric Tf. Rather, the increase in TfR2 is attributed to an increase in the half-life of TfR2 protein in cells exposed to diferric Tf. Our results support a role for TfR2 in monitoring iron levels by sensing changes in the concentration of diferric Tf.

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17

Maenhout, Thomas M., Marc Uytterhoeven, Elke Lecocq, Marc L. De Buyzere, and Joris R. Delanghe. "Immunonephelometric Carbohydrate-Deficient Transferrin Results and Transferrin Variants." Clinical Chemistry 59, no. 6 (June 1, 2013): 997–98. http://dx.doi.org/10.1373/clinchem.2012.195891.

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18

Cheng, Yifan, Olga Zak, Philip Aisen, Stephen C. Harrison, and Thomas Walz. "Structure of the Human Transferrin Receptor-Transferrin Complex." Cell 116, no. 4 (February 2004): 565–76. http://dx.doi.org/10.1016/s0092-8674(04)00130-8.

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19

Li, Hongyan, and Zhong Ming Qian. "ChemInform Abstract: Transferrin/Transferrin Receptor-Mediated Drug Delivery." ChemInform 33, no. 26 (May 21, 2010): no. http://dx.doi.org/10.1002/chin.200226275.

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20

Ha-Duong, Nguyêt-Thanh, Miryana Hémadi, Zohra Chikh, and Jean-Michel El Hage Chahine. "Kinetics and thermodynamics of metal-loaded transferrins: transferrin receptor 1 interactions." Biochemical Society Transactions 36, no. 6 (November 19, 2008): 1422–26. http://dx.doi.org/10.1042/bst0361422.

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Transferrin receptor 1 (R) and human serum transferrin (T) are the two main actors in iron acquisition by the cell. R binds TFe2 (iron-loaded transferrin), which allows its internalization in the cytoplasm by endocytosis. T also forms complexes with metals other than iron. In order to follow the iron-acquisition pathway, these metals should obey at least two essential rules: (i) formation of a strong complex with T; and (ii) interaction of this complex with R. In the present paper, we propose a general mechanism for the interaction of five metal-loaded Ts [Fe(III), Al(III), Bi(III), Ga(III) and Co(III)] with R and we discuss their potential incorporation by the iron-acquisition pathway. With iron- and cobalt-loaded Ts, the interaction of R takes place in two steps: the first is detected by the T-jump technique and occurs in the 100 μs range, whereas the second is slow and occurs in the hour range. Bi(III)- and Ga(III)-loaded Ts interact with R in a single fast kinetic step, which occurs in the 100–500 μs range. No interaction is detected between R and aluminium-saturated T. The fast steps are ascribed to the interaction of the C-lobe of metal-loaded T with the helical domain of R: dissociation constant, K′1, of 0.50±0.07, 0.82±0.25, 4±0.4 and 1.10±0.12 μM for Fe(III), Co(III), Bi(III) and Ga(III) respectively. The second slow steps are ascribed to changes in the conformation of the protein–protein adducts which increase the stability to achieve, at thermodynamic equilibrium, an overall dissociation constant, K1, of 2.3 and 25 nM for Fe(III) and Co(III) respectively. This last step occurs over several hours, whereas endocytosis takes place in several minutes. This implies that metal-loaded Ts are internalized with only the C-lobe interacting with R. This suggests that, despite a lower affinity for R when compared with TFe2, some metal-loaded Ts can compete kinetically with TFe2 for the interaction with R and thus follow the iron-acquisition pathway.

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21

Modun, Belinda, Robert W. Evans, Christopher L. Joannou, and Paul Williams. "Receptor-Mediated Recognition and Uptake of Iron from Human Transferrin by Staphylococcus aureus andStaphylococcus epidermidis." Infection and Immunity 66, no. 8 (August 1, 1998): 3591–96. http://dx.doi.org/10.1128/iai.66.8.3591-3596.1998.

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ABSTRACT Staphylococcus aureus and Staphylococcus epidermidis both recognize and bind the human iron-transporting glycoprotein, transferrin, via a 42-kDa cell surface protein receptor. In an iron-deficient medium, staphylococcal growth can be promoted by the addition of human diferric transferrin but not human apotransferrin. To determine whether the staphylococcal transferrin receptor is involved in the removal of iron from transferrin, we employed 6 M urea–polyacrylamide gel electrophoresis, which separates human transferrin into four forms (diferric, monoferric N-lobe, and monoferric C-lobe transferrin and apotransferrin). S. aureus and S. epidermidis but notStaphylococcus saprophyticus (which lacks the transferrin receptor) converted diferric human transferrin into its apotransferrin form within 30 min. During conversion, iron was removed sequentially from the N lobe and then from the C lobe. Metabolic poisons such as sodium azide and nigericin inhibited the release of iron from human transferrin, indicating that it is an energy-requiring process. To demonstrate that this process is receptor rather than siderophore mediated, we incubated (i) washed staphylococcal cells and (ii) the staphylococcal siderophore, staphyloferrin A, with porcine transferrin, a transferrin species which does not bind to the staphylococcal receptor. While staphyloferrin A removed iron from both human and porcine transferrins, neither S. aureus nor S. epidermidis cells could promote the release of iron from porcine transferrin. In competition binding assays, both native and recombinant N-lobe fragments of human transferrin as well as a naturally occurring human transferrin variant with a mutation in the C-lobe blocked binding of 125I-labelled transferrin. Furthermore, the staphylococci removed iron efficiently from the iron-loaded N-lobe fragment of human transferrin. These data demonstrate that the staphylococci efficiently remove iron from transferrin via a receptor-mediated process and provide evidence to suggest that there is a primary receptor recognition site on the N-lobe of human transferrin.

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22

Gosselaar, P. H., A. J. G. Van-Dijk, G. C. De-Gast, L. Polito, A. Bolognesi, W. C. Vooijs, A. F. M. Verheul, H. G. J. Krouwer, and J. J. M. Marx. "Transferrin toxin but not transferrin receptor immunotoxin is influenced by free transferrin and iron saturation." European Journal of Clinical Investigation 32 (March 2002): 61–69. http://dx.doi.org/10.1046/j.1365-2362.2002.0320s1061.x.

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23

Vogt, Todd M., Aaron D. Blackwell, Anthony M. Giannetti, Pamela J. Bjorkman, and Caroline A. Enns. "Heterotypic interactions between transferrin receptor and transferrin receptor 2." Blood 101, no. 5 (March 1, 2003): 2008–14. http://dx.doi.org/10.1182/blood-2002-09-2742.

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Cellular iron uptake in most tissues occurs via endocytosis of diferric transferrin (Tf) bound to the transferrin receptor (TfR). Recently, a second transferrin receptor, transferrin receptor 2 (TfR2), has been identified and shown to play a critical role in iron metabolism. TfR2 is capable of Tf-mediated iron uptake and mutations in this gene result in a rare form of hereditary hemochromatosis unrelated to the hereditary hemochromatosis protein, HFE. Unlike TfR, TfR2 expression is not controlled by cellular iron concentrations and little information is currently available regarding the role of TfR2 in cellular iron homeostasis. To investigate the relationship between TfR and TfR2, we performed a series of in vivo and in vitro experiments using antibodies generated to each receptor. Western blots demonstrate that TfR2 protein is expressed strongest in erythroid/myeloid cell lines. Metabolic labeling studies indicate that TfR2 protein levels are approximately 20-fold lower than TfR in these cells. TfR and TfR2 have similar cellular localizations in K562 cells and coimmunoprecipitate to only a very limited extent. Western analysis of the receptors under nonreducing conditions reveals that they can form heterodimers.

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24

Robb, Aeisha, and Marianne Wessling-Resnick. "Regulation of transferrin receptor 2 protein levels by transferrin." Blood 104, no. 13 (December 15, 2004): 4294–99. http://dx.doi.org/10.1182/blood-2004-06-2481.

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Abstract Transferrin receptor 2 (TfR2) plays a critical role in iron homeostasis because patients carrying disabling mutations in the TFR2 gene suffer from hemochromatosis. In this study, iron-responsive regulation of TfR2 at the protein level was examined in vitro and in vivo. HepG2 cell TfR2 protein levels were up-regulated after exposure to holotransferrin (holoTf) in a time- and dose-responsive manner. ApoTf or high-iron treatment with non–Tf-bound iron failed to elicit similar effects, suggesting that TfR2 regulation reflects interactions of the iron-bound ligand. Hepatic TfR2 protein levels also reflected an adaptive response to changing iron status in vivo. Liver TfR2 protein levels were down- and up-regulated in rats fed an iron-deficient and a high-iron diet, respectively. TfR2 was also up-regulated in Hfe-/- mice, an animal model that displays liver iron loading. In contrast, TfR2 levels were reduced in hypotransferrinemic mice despite liver iron overload, supporting the idea that regulation of the receptor is dependent on Tf. This idea is confirmed by up-regulation of TfR2 in β-thalassemic mice, which, like hypotransferrinemic mice, are anemic and incur iron loading, but have functional Tf. Based on these combined results, we hypothesize that TfR2 acts as a sensor of iron status such that receptor levels reflect Tf saturation.

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25

Chen, Juxing, Jinzhi Wang, Kathrin R. Meyers, and Caroline A. Enns. "Transferrin-Directed Internalization and Cycling of Transferrin Receptor 2." Traffic 10, no. 10 (October 2009): 1488–501. http://dx.doi.org/10.1111/j.1600-0854.2009.00961.x.

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26

Garrick, M. D., K. Gniecko, Y. Liu, D. S. Cohan, and L. M. Garrick. "Transferrin and the transferrin cycle in Belgrade rat reticulocytes." Journal of Biological Chemistry 268, no. 20 (July 1993): 14867–74. http://dx.doi.org/10.1016/s0021-9258(18)82413-9.

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27

Richardson, D. R. "Mysteries of the Transferrin-Transferrin Receptor 1 Interaction Uncovered." Cell 116, no. 4 (February 2004): 483–85. http://dx.doi.org/10.1016/s0092-8674(04)00165-5.

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28

Steinle, Alexander. "Transferrin‘ activation: Bonding with transferrin receptors tunes KLRG1 function." European Journal of Immunology 44, no. 6 (May 7, 2014): 1600–1603. http://dx.doi.org/10.1002/eji.201444670.

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29

Perera, Yasser, Darién García, Osmany Guirola, Vivian Huerta, Yanet García, and Yasmiana Muñoz. "Epitope mapping of anti-human transferrin monoclonal antibodies: potential uses for transferrin–transferrin receptor interaction studies." Journal of Molecular Recognition 21, no. 2 (2008): 103–13. http://dx.doi.org/10.1002/jmr.878.

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30

Wright, Gerard D., and John F. Honek. "Effects of iron binding agents on Saccharomyces cerevisiae growth and cytochrome P450 content." Canadian Journal of Microbiology 35, no. 10 (October 1, 1989): 945–50. http://dx.doi.org/10.1139/m89-156.

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The yeast Saccharomyces cerevisiae Y222 was studied in the presence of the following iron-binding agents: Desferal, dipyridyl, and human and bovine transferrins. We report that cell growth and lanosterol 14 α-demethylase cytochrome P450 are not affected by Desferal but that dipyridyl and serum transferrins decrease the cytochrome P450 content of the yeast. Paradoxically, while both human and bovine transferrins reduce cytochrome P450 content, only bovine transferrin appears to affect cell growth in this strain. No evidence for siderophore production by this strain was found under low iron conditions.Key words: Saccharomyces cerevisiae, iron, cytochrome P450, transferrin.

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31

Solomons, Hilary. "Carbohydrate Deficient Transferrin (cdt ) and Alcoholism." Clinical Medical Reviews and Reports 2, no. 01 (February 14, 2020): 01–02. http://dx.doi.org/10.31579/2690-8794/006.

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Alcohol abuse is an important public health problem. This condition is usually identified on the basis of clinical judgement, alcoholism related questionnaires and laboratory tests i.e. Gamma-glutamyltransferase (ggt), aspartate aminotransferase (ast ) or mean cell volume (mcv).

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32

Asmamaw, Berhan. "Transferrin in fishes: A review article." Journal of Coastal Life Medicine 4, no. 3 (March 2016): 176–80. http://dx.doi.org/10.12980/jclm.4.2016j5-255.

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33

Hackler, Rolf, Torsten Arndt, Angelika Helwig-Rolig, Juergen Kropf, Armin Steinmetz, and Juergen R. Schaefer. "Investigation by Isoelectric Focusing of the Initial Carbohydrate-deficient Transferrin (CDT) and non-CDT Transferrin Isoform Fractionation Step Involved in Determination of CDT by the ChronAlcoI.D. Assay." Clinical Chemistry 46, no. 4 (April 1, 2000): 483–92. http://dx.doi.org/10.1093/clinchem/46.4.483.

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Abstract Background: The introduction of a new set of reagents for the determination of carbohydrate-deficient transferrin (CDT) as a marker of chronic alcohol abuse requires an independent evaluation of the analytic specificity of the test. This information is needed for correct interpretation and classification of test results. Methods: Isoelectric focusing on the PhastSystemTM followed by immunofixation, silver staining, and densitometry was used to validate the initial transferrin isoform fractionation step on anion-exchange microcolumns involved in the ChronAlcoI.D.TM assay. Results: The in vitro transferrin iron load was complete and stable. The CDT and non-CDT transferrin fractionation on anion-exchange microcolumns was reliable and reproducible (CV ≤10%). Except for quantitatively unimportant traces of trisialo-Fe2-transferrin (<5% of total CDT), only asialo-, mono-, and disialo-Fe2-transferrin were detected in the microcolumn eluates (n = 170). There was a loss of proportionally similar amounts of asialo-Fe2-transferrin (during column rinsing) and disialo-Fe2-transferrin (on the anion exchanger). Thus, the peak height ratios for disialo- and asialo-Fe2-transferrin did not change from >1 (serum) to <1 (eluates) as described for the CDTect assays. The transferrin patterns in the ChronAlcoI.D. eluates were representative of those in serum. Transferrin D variants with isoelectric points close to that of trisialo-Fe2-transferrin C1 did not cause overdetermination of CDT by the ChronAlcoI.D. test. Conclusions: The initial CDT and non-CDT fractionation step involved in determination of CDT by the ChronAlcoI.D. assay is efficient for eliminating non-CDT transferrins from serum before quantification of CDT in the final turbidimetric immunoassay. We recommend IEF for validation of other (commercial) CDT analysis methods and of odd CDT results.

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34

Levenson, Mark J., Rosemary B. Desloge, and Simon C. Parisier. "Beta-2 Transferrin." Laryngoscope 106, no. 2 (February 1996): 159–61. http://dx.doi.org/10.1097/00005537-199602000-00010.

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35

Kamboh, M. I., and R. E. Ferrell. "Human Transferrin Polymorphism." Human Heredity 37, no. 2 (1987): 65–81. http://dx.doi.org/10.1159/000153680.

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36

Cook, J. D., B. S. Skikne, and R. D. Baynes. "Serum Transferrin Receptor." Annual Review of Medicine 44, no. 1 (February 1993): 63–74. http://dx.doi.org/10.1146/annurev.me.44.020193.000431.

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37

Haas, Michael J. "Transferrin, not transfusions." Science-Business eXchange 3, no. 7 (February 2010): 205. http://dx.doi.org/10.1038/scibx.2010.205.

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38

M??rtensson, Ola, Annika H??rlin, Ragnhild Brandt, Kaija Sepp??, and Pekka Sillanaukee. "Transferrin Isoform Distribution." Alcoholism: Clinical & Experimental Research 21, no. 9 (December 1997): 1710. http://dx.doi.org/10.1097/00000374-199712000-00024.

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Heinemann, A., M. Sterneck, R. Kuhlencordt, X. Rogiers, K. H. Schulz, B. Queen, F. Wischhusen, and K. P??schel. "Carbohydrate-Deficient Transferrin." Alcoholism: Clinical & Experimental Research 22, no. 8 (November 1998): 1806. http://dx.doi.org/10.1097/00000374-199811000-00028.

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Åkesson, Agneta, Per Bjellerup, Marika Berglund, Katarina Bremme, and Marie Vahter. "Soluble Transferrin Receptor." Obstetrics & Gynecology 99, no. 2 (February 2002): 260–66. http://dx.doi.org/10.1097/00006250-200202000-00017.

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Booyjz̈sen, Claire, Charlotte A. Scarff, Ben Moreton, Ian Portman, James H. Scrivens, Giovanni Costantini, and Peter J. Sadler. "Fibrillation of transferrin." Biochimica et Biophysica Acta (BBA) - General Subjects 1820, no. 3 (March 2012): 427–36. http://dx.doi.org/10.1016/j.bbagen.2011.11.004.

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Melanie, Brazil. "Transferrin' the load." Nature Reviews Drug Discovery 4, no. 7 (July 2005): 537. http://dx.doi.org/10.1038/nrd1786.

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Yoshiga, Toyoshi, Teodora Georgieva, Boris C. Dunkov, Nedjalka Harizanova, Kiril Ralchev, and John H. Law. "Drosophila melanogaster transferrin." European Journal of Biochemistry 260, no. 2 (December 25, 2001): 414–20. http://dx.doi.org/10.1046/j.1432-1327.1999.00173.x.

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Marsee, Derek K., Geraldine S. Pinkus, and Hongbo Yu. "CD71 (Transferrin Receptor)." American Journal of Clinical Pathology 134, no. 3 (September 2010): 429–35. http://dx.doi.org/10.1309/ajcpcrk3moaoj6at.

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Haas, Michael J. "Transferrin PET project." Science-Business eXchange 5, no. 39 (October 2012): 1022. http://dx.doi.org/10.1038/scibx.2012.1022.

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Skikne, Barry S. "Serum transferrin receptor." American Journal of Hematology 83, no. 11 (November 2008): 872–75. http://dx.doi.org/10.1002/ajh.21279.

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Aisen, Philip. "Transferrin receptor 1." International Journal of Biochemistry & Cell Biology 36, no. 11 (November 2004): 2137–43. http://dx.doi.org/10.1016/j.biocel.2004.02.007.

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Kleven, Mark D., Shall Jue, and Caroline A. Enns. "Transferrin Receptors TfR1 and TfR2 Bind Transferrin through Differing Mechanisms." Biochemistry 57, no. 9 (February 2018): 1552–59. http://dx.doi.org/10.1021/acs.biochem.8b00006.

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Meyer, Wilfried. "Immunohistochemical Demonstration of Transferrin and Transferrin Receptor in Mammalian Integument." Biotechnic & Histochemistry 72, no. 4 (January 1997): 223–28. http://dx.doi.org/10.3109/10520299709082242.

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Ruthner, Monika, Alajos Berczi, and Hans Goldenberg. "Interaction of a doxorubicin-transferrin conjugate with isolated transferrin receptors." Life Sciences 54, no. 1 (January 1994): 35–40. http://dx.doi.org/10.1016/0024-3205(94)00575-3.

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