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Journal articles on the topic 'Transferrin'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

Hemangini, Chaudhari, Dixit R., and Jadeja J.M. "Serum Level Of Iron And Transferrin In Normal And Anemic Pregnant Women." International Journal of Basic and Applied Physiology 2, no. 1 (2013): 123–26. https://doi.org/10.5281/zenodo.4483106.

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Iron deficiency anemia is a major health problem in our country especially in pregnancy. For accurate diagnosis of iron deficiency anemia we require accurate indicators based on which treatment can be given. Purpose of this study is to prevent unnecessary iron overload by accurate diagnosis in pregnancy as excessive iron can lead to oxidative damage. Method: Serum level of Iron and transferrin and total iron binding capacity and % saturation of transferrin were estimated in 70 women in their I, II and III trimester of pregnancy. Only healthy subjects (without infective, metabolic, and degenera

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2

FAST, Beate, Katrin KREMP, Michael BOSHART, and Dietmar STEVERDING. "Iron-dependent regulation of transferrin receptor expression in Trypanosoma brucei." Biochemical Journal 342, no. 3 (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 transferri

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3

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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4

Carlevaro, Mariella F., Adriana Albini, Domenico Ribatti, et al. "Transferrin Promotes Endothelial Cell Migration and Invasion: Implication in Cartilage Neovascularization." Journal of Cell Biology 136, no. 6 (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 source

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5

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

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6

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

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7

Xin, Vechtova, Shaliutina-Kolesova, et al. "Transferrin Identification in Sterlet (Acipenser ruthenus) Reproductive System." Animals 9, no. 10 (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 se

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8

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

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9

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 (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 t

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10

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 (1998): 1022–31. http://dx.doi.org/10.1046/j.1432-1327.1998.2581022.x.

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11

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

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12

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 (1994): 59–67. http://dx.doi.org/10.1016/0167-4838(94)90092-2.

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13

Graham, Ross M., Gail M. Reutens, Carly E. Herbison, et al. "Transferrin receptor 2 mediates uptake of transferrin-bound and non-transferrin-bound iron." Journal of Hepatology 48, no. 2 (2008): 327–34. http://dx.doi.org/10.1016/j.jhep.2007.10.009.

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14

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 (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

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15

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

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16

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

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17

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

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18

Johnson, Martha B., and Caroline A. Enns. "Diferric transferrin regulates transferrin receptor 2 protein stability." Blood 104, no. 13 (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 T

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19

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 (2013): 997–98. http://dx.doi.org/10.1373/clinchem.2012.195891.

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20

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

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21

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

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22

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 (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) an

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23

Gosselaar, P. H., A. J. G. Van-Dijk, G. C. De-Gast, et al. "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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24

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 (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 cond

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25

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 (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 o

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26

Robb, Aeisha, and Marianne Wessling-Resnick. "Regulation of transferrin receptor 2 protein levels by transferrin." Blood 104, no. 13 (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 lev

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27

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

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28

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 (1993): 14867–74. http://dx.doi.org/10.1016/s0021-9258(18)82413-9.

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29

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

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30

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

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31

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 (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

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32

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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33

Appiah, Samuel K., Simon B. Bani, Charles Nkansah, et al. "Serum Soluble Transferrin Receptor and Transferrin Levels among Regular Blood Donors." SciMedicine Journal 4, no. 3 (2022): 101–10. http://dx.doi.org/10.28991/scimedj-2022-04-03-01.

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Background: The study evaluated the effects of regular blood donation on serum transferrin and soluble transferrin receptor levels at Wenchi Methodist Hospital. Methods: This was a hospital-based cross-sectional study conducted at the Medical Laboratory Department of the Wenchi Methodist Hospital in the Bono Region of Ghana. A total of eighty-nine (89) venous blood samples from apparently healthy blood donors were analyzed. Complete blood count parameters were analyzed using an automated haematology analyzer and serum transferrin and transferrin receptor using ELISA. The data were analyzed usi

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34

Solomons, Hilary. "Carbohydrate Deficient Transferrin (cdt ) and Alcoholism." Clinical Medical Reviews and Reports 2, no. 01 (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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35

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

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36

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

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37

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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38

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

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39

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

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40

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

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41

Heinemann, A., M. Sterneck, R. Kuhlencordt, et al. "Carbohydrate-Deficient Transferrin." Alcoholism: Clinical & Experimental Research 22, no. 8 (1998): 1806. http://dx.doi.org/10.1097/00000374-199811000-00028.

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42

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

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43

Booyjz̈sen, Claire, Charlotte A. Scarff, Ben Moreton, et al. "Fibrillation of transferrin." Biochimica et Biophysica Acta (BBA) - General Subjects 1820, no. 3 (2012): 427–36. http://dx.doi.org/10.1016/j.bbagen.2011.11.004.

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44

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

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45

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 (2001): 414–20. http://dx.doi.org/10.1046/j.1432-1327.1999.00173.x.

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46

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

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47

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

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48

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

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49

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

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50

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

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