Editing Transferrin

{{Short description|Mammalian protein found in Homo sapiens}}
{{cs1 config|name-list-style=vanc}}
{{Infobox_gene}}
{{Infobox protein family
| Symbol = Transferrin
| Name = Transferrin
| image =
| width =
| caption =
| Pfam= PF00405
| InterPro= IPR001156
| SMART=
| Prosite = PDOC00182
| SCOP = 1lcf
| TCDB =
| OPM family=
| OPM protein= 
| PDB=
}}

'''Transferrins''' are [[glycoprotein]]s found in [[vertebrate]]s which bind and consequently mediate the transport of [[iron]] (Fe) through [[blood plasma]].<ref name="PUB00001349">{{Cite journal |vauthors=Crichton RR, Charloteaux-Wauters M |date=May 1987 |title=Iron transport and storage |journal=European Journal of Biochemistry |volume=164 |issue=3 |pages=485–506 |doi=10.1111/j.1432-1033.1987.tb11155.x |pmid=3032619|doi-access=free }}</ref> They are produced in the [[liver]] and contain binding sites for two [[Iron(III)|Fe<sup>3+</sup>]] ions.<ref>{{cite journal | vauthors = Hall DR, Hadden JM, Leonard GA, Bailey S, Neu M, Winn M, Lindley PF | title = The crystal and molecular structures of diferric porcine and rabbit serum transferrins at resolutions of 2.15 and 2.60 A, respectively | journal = Acta Crystallographica. Section D, Biological Crystallography | volume = 58 | issue = Pt 1 | pages = 70–80 | date = January 2002 | pmid = 11752780 | doi = 10.1107/s0907444901017309 | bibcode = 2002AcCrD..58...70H }}</ref> Human transferrin is encoded by the ''TF'' [[gene]] and produced as a 76 [[Dalton (unit)|kDa]] glycoprotein.<ref name="pmid6585826">{{cite journal | vauthors = Yang F, Lum JB, McGill JR, Moore CM, Naylor SL, van Bragt PH, Baldwin WD, Bowman BH | display-authors = 6 | title = Human transferrin: cDNA characterization and chromosomal localization | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 81 | issue = 9 | pages = 2752–6 | date = May 1984 | pmid = 6585826 | pmc = 345148 | doi = 10.1073/pnas.81.9.2752 | bibcode = 1984PNAS...81.2752Y | doi-access = free }}</ref><ref name="Kawabata_2019">{{cite journal | vauthors = Kawabata H | title = Transferrin and transferrin receptors update | journal = Free Radical Biology & Medicine | volume = 133 | pages = 46–54 | date = March 2019 | pmid = 29969719 | doi = 10.1016/j.freeradbiomed.2018.06.037 | s2cid = 49674402 }}</ref>

Transferrin [[glycoprotein]]s bind iron tightly, but reversibly. Although iron bound to transferrin is less than 0.1% (4&nbsp;mg) of total body iron, it forms the most vital iron pool with the highest rate of turnover (25&nbsp;mg/24 h). Transferrin has a molecular weight of around 80 [[atomic mass unit|kDa]] and contains two specific high-affinity [[Fe(III)]] binding sites. The affinity of transferrin for Fe(III) is extremely high ([[association constant]] is 10<sup>20</sup> M<sup>−1</sup> at pH 7.4)<ref name="pmid204636">{{cite journal | vauthors = Aisen P, Leibman A, Zweier J | title = Stoichiometric and site characteristics of the binding of iron to human transferrin | journal = The Journal of Biological Chemistry | volume = 253 | issue = 6 | pages = 1930–7 | date = March 1978 | doi = 10.1016/S0021-9258(19)62337-9 | pmid = 204636 | doi-access = free }}</ref> but decreases progressively with decreasing [[pH]] below neutrality. Transferrins are not limited to only binding to iron but also to different metal ions.<ref>{{cite journal | vauthors = Nicotra S, Sorio D, Filippi G, De Gioia L, Paterlini V, De Palo EF, Grandori R, Tagliaro F, Santambrogio C | display-authors = 6 | title = Terbium chelation, a specific fluorescent tagging of human transferrin. Optimization of conditions in view of its application to the HPLC analysis of carbohydrate-deficient transferrin (CDT) | journal = Analytical and Bioanalytical Chemistry | volume = 409 | issue = 28 | pages = 6605–6612 | date = November 2017 | pmid = 28971232 | doi = 10.1007/s00216-017-0616-z | s2cid = 13929228 }}</ref> These glycoproteins are located in various bodily fluids of vertebrates.<ref name="MacGillivray_1998">{{cite journal | vauthors = MacGillivray RT, Moore SA, Chen J, Anderson BF, Baker H, Luo Y, Bewley M, Smith CA, Murphy ME, Wang Y, Mason AB, Woodworth RC, Brayer GD, Baker EN | display-authors = 6 | title = Two high-resolution crystal structures of the recombinant N-lobe of human transferrin reveal a structural change implicated in iron release | journal = Biochemistry | volume = 37 | issue = 22 | pages = 7919–28 | date = June 1998 | pmid = 9609685 | doi = 10.1021/bi980355j }}</ref><ref name="Dewan_1993">{{cite journal | vauthors = Dewan JC, Mikami B, Hirose M, Sacchettini JC | title = Structural evidence for a pH-sensitive dilysine trigger in the hen ovotransferrin N-lobe: implications for transferrin iron release | journal = Biochemistry | volume = 32 | issue = 45 | pages = 11963–8 | date = November 1993 | pmid = 8218271 | doi = 10.1021/bi00096a004 }}</ref> Some invertebrates have proteins that act like transferrin found in the [[hemolymph]].<ref name="MacGillivray_1998" /><ref name="Baker_1992">{{cite journal | vauthors = Baker EN, Lindley PF | title = New perspectives on the structure and function of transferrins | journal = Journal of Inorganic Biochemistry | volume = 47 | issue = 3–4 | pages = 147–60 | date = August 1992 | pmid = 1431877 | doi = 10.1016/0162-0134(92)84061-q }}</ref>

When not bound to iron, transferrin is known as "apotransferrin" (see also [[Apoenzyme#Cofactors|apoprotein]]).

== Occurrence and function ==

Transferrins are glycoproteins that are often found in biological fluids of vertebrates. When a transferrin protein loaded with iron encounters a [[transferrin receptor]] on the surface of a [[cell (biology)|cell]], e.g., erythroid precursors in the bone marrow, it binds to it and is transported into the cell in a [[vesicle (biology)|vesicle]] by [[receptor-mediated endocytosis]].<ref name="Halbrooks_2003">{{cite journal | vauthors = Halbrooks PJ, He QY, Briggs SK, Everse SJ, Smith VC, MacGillivray RT, Mason AB | title = Investigation of the mechanism of iron release from the C-lobe of human serum transferrin: mutational analysis of the role of a pH sensitive triad | journal = Biochemistry | volume = 42 | issue = 13 | pages = 3701–7 | date = April 2003 | pmid = 12667060 | doi = 10.1021/bi027071q }}</ref> The pH of the vesicle is reduced by hydrogen ion pumps ([[V-ATPase|{{chem|H|+}} ATPases]]) to about 5.5, causing transferrin to release its iron ions.<ref name="MacGillivray_1998" /> Iron release rate is dependent on several factors including pH levels, interactions between lobes, temperature, salt, and chelator.<ref name="Halbrooks_2003" /> The receptor with its [[ligand]] bound transferrin is then transported through the [[endocytic cycle]] back to the cell surface, ready for another round of iron uptake.
Each transferrin molecule has the ability to carry two iron ions in the [[ferric]] form ({{chem|Fe|3+}}).<ref name="Baker_1992" />

=== Humans and other mammals ===
The [[liver]] is the main site of transferrin synthesis but other tissues and organs, including the brain, also produce transferrin. A major source of transferrin secretion in the brain is the [[choroid plexus]] in the [[ventricular system]].<ref name="Moos">{{cite journal | vauthors = Moos T | title = Brain iron homeostasis | journal = Danish Medical Bulletin | volume = 49 | issue = 4 | pages = 279–301 | date = November 2002 | pmid = 12553165 }}</ref> The main role of transferrin is to deliver iron from absorption centers in the [[duodenum]] and white blood cell [[macrophages]] to all tissues. Transferrin plays a key role in areas where erythropoiesis and active cell division occur.<ref name="pmid18473900" /> The receptor helps maintain iron [[homeostasis]] in the cells by controlling iron concentrations.<ref name="pmid18473900" />

The [[gene]] coding for transferrin in humans is located in [[chromosome]] band 3q21.<ref name="pmid6585826" />

Medical professionals may check serum transferrin level in [[Iron deficiency (medicine)|iron deficiency]] and in [[iron overload disorder]]s such as [[hemochromatosis]].

=== Other species ===
''[[Drosophila melanogaster]]'' has three transferrin genes and is highly divergent from all other model clades, ''[[Ciona intestinalis]]'' one, ''[[Danio rerio]]'' has three highly divergent from each other, as do ''[[Takifugu rubripes]]'' and ''[[Xenopus tropicalis]]'' and ''[[Gallus gallus]]'', while ''[[Monodelphis domestica]]'' has two divergent [[ortholog]]s, and ''[[Mus musculus]]'' has two relatively close and one more distant ortholog. Relatedness and orthology/[[paralog]]y data are also available for ''[[Dictyostelium discoideum]]'', ''[[Arabidopsis thaliana]]'', and ''[[Pseudomonas aeruginosa]]''.<ref name="Gabaldon-Koonin-2013">{{cite journal | vauthors = Gabaldón T, Koonin EV | title = Functional and evolutionary implications of gene orthology | journal = Nature Reviews. Genetics | volume = 14 | issue = 5 | pages = 360–6 | date = May 2013 | pmid = 23552219 | doi = 10.1038/nrg3456 | publisher = [[Nature Portfolio]] | author2-link = Eugene Koonin | pmc = 5877793 }}</ref>

== Structure ==

In humans, transferrin consists of a polypeptide chain containing 679 [[amino acids]] and two carbohydrate chains. The protein is composed of [[alpha helix|alpha helices]] and [[beta sheet]]s that form two [[protein domain|domains]].<ref name="stedwards">{{cite web | url = http://www.cs.stedwards.edu/chem/Chemistry/CHEM43/CHEM43/Projects04/Transferrin/structure.htm | title = Transferrin Structure | date = 2005-07-18 | publisher = St. Edward's University | access-date = 2009-04-24 | url-status = dead | archive-url = https://archive.today/20121211180614/http://www.cs.stedwards.edu/chem/Chemistry/CHEM43/CHEM43/Projects04/Transferrin/structure.htm | archive-date = 2012-12-11 }}</ref> The N- and C- terminal sequences are represented by globular lobes and between the two lobes is an iron-binding site.<ref name="Dewan_1993" />

The [[amino acids]] which bind the iron ion to the transferrin are identical for both lobes; two [[tyrosines]], one [[histidine]], and one [[aspartic acid]]. For the iron ion to bind, an [[anion]] is required, preferably [[carbonate]] ({{chem|CO|3|2−}}).<ref name="stedwards"/><ref name="Baker_1992" />

Transferrin also has a transferrin iron-bound [[receptor (biochemistry)|receptor]]; it is a disulfide-linked [[homodimer]].<ref name="pmid18473900">{{cite journal | vauthors = Macedo MF, de Sousa M | title = Transferrin and the transferrin receptor: of magic bullets and other concerns | journal = Inflammation & Allergy - Drug Targets | volume = 7 | issue = 1 | pages = 41–52 | date = March 2008 | pmid = 18473900 | doi = 10.2174/187152808784165162 }}</ref> In humans, each monomer consists of 760 amino acids. It enables [[ligand]] bonding to the transferrin, as each [[monomer]] can bind to one or two atoms of iron. Each monomer consists of three domains: the protease, the helical, and the apical domains. The shape of a transferrin receptor resembles a butterfly based on the intersection of three clearly shaped domains.<ref name="stedwards"/> Two main transferrin receptors found in humans denoted as transferrin receptor 1 (TfR1) and transferrin receptor 2 (TfR2). Although both are similar in structure, TfR1 can only bind specifically to human TF where TfR2 also has the capability to interact with [[Bovinae|bovine]] TF.<ref name="Kawabata_2019" />

<gallery>
File:PDB 1suv EBI.jpg|Transferrin bound to its receptor.<ref name="pmid14980223">{{PDB|1suv}}; {{cite journal | vauthors = Cheng Y, Zak O, Aisen P, Harrison SC, Walz T | title = Structure of the human transferrin receptor-transferrin complex | journal = Cell | volume = 116 | issue = 4 | pages = 565–76 | date = Feb 2004 | pmid = 14980223 | doi = 10.1016/S0092-8674(04)00130-8 | s2cid = 2981917 }}</ref>
File:PDB 2nsu EBI.jpg|Transferrin receptor complex.<ref name="pmid17420467">{{PDB|2nsu}}; {{cite journal | vauthors = Hafenstein S, Palermo LM, Kostyuchenko VA, Xiao C, Morais MC, Nelson CD, Bowman VD, Battisti AJ, Chipman PR, Parrish CR, Rossmann MG | title = Asymmetric binding of transferrin receptor to parvovirus capsids | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 104 | issue = 16 | pages = 6585–9 | date = Apr 2007 | pmid = 17420467 | pmc = 1871829 | doi = 10.1073/pnas.0701574104 | bibcode = 2007PNAS..104.6585H | doi-access = free }}</ref>
</gallery>

== Immune system ==

Transferrin is also associated with the [[innate immune system]]. It is found in the [[mucosa]] and binds iron, thus creating an environment low in free iron that impedes bacterial survival in a process called iron withholding. The level of transferrin decreases in inflammation.<ref name=Ritchie>{{cite journal | vauthors = Ritchie RF, Palomaki GE, Neveux LM, Navolotskaia O, Ledue TB, Craig WY | title = Reference distributions for the negative acute-phase serum proteins, albumin, transferrin and transthyretin: a practical, simple and clinically relevant approach in a large cohort | journal = Journal of Clinical Laboratory Analysis | volume = 13 | issue = 6 | pages = 273–9 | year = 1999 | pmid = 10633294 | pmc = 6808097 | doi = 10.1002/(SICI)1098-2825(1999)13:6<273::AID-JCLA4>3.0.CO;2-X }}</ref>

==Role in disease==

An increased plasma transferrin level is often seen in patients with iron deficiency [[anemia]], during pregnancy, and with the use of oral contraceptives, reflecting an increase in transferrin protein expression. When plasma transferrin levels rise, there is a reciprocal decrease in percent transferrin iron saturation, and a corresponding increase in [[Total iron-binding capacity|total iron binding capacity]] in iron deficient states<ref>{{cite journal | vauthors = Miller JL | title = Iron deficiency anemia: a common and curable disease | journal = Cold Spring Harbor Perspectives in Medicine | volume = 3 | issue = 7 | pages = a011866 | date = July 2013 | pmid = 23613366 | pmc = 3685880 | doi = 10.1101/cshperspect.a011866 }}</ref>

A decreased plasma transferrin level can occur in iron overload diseases and protein malnutrition. An absence of transferrin results from a rare genetic disorder known as [[atransferrinemia]], a condition characterized by anemia and [[hemosiderosis]] in the heart and liver that leads to heart failure and many other complications as well as to [[H63D Syndrome|H63D syndrome]].

Studies reveal that a transferrin saturation (serum iron concentration ÷ total iron binding capacity) over 60 percent in men and over 50 percent in women identified the presence of an abnormality in iron metabolism (Hereditary hemochromatosis, heterozygotes and homozygotes) with approximately 95 percent accuracy. This finding helps in the early diagnosis of Hereditary hemochromatosis, especially while serum [[ferritin]] still remains low. The retained iron in Hereditary hemochromatosis is primarily deposited in parenchymal cells, with reticuloendothelial cell accumulation occurring very late in the disease. This is in contrast to transfusional iron overload in which iron deposition occurs first in the reticuloendothelial cells and then in parenchymal cells. This explains why ferritin levels remain relative low in Hereditary hemochromatosis, while transferrin saturation is high.<ref name="pmid21452290">{{cite journal | vauthors = Bacon BR, Adams PC, Kowdley KV, Powell LW, Tavill AS | title = Diagnosis and management of hemochromatosis: 2011 practice guideline by the American Association for the Study of Liver Diseases | journal = Hepatology | location = Baltimore, Md. | volume = 54 | issue = 1 | pages = 328–43 | date = July 2011 | pmid = 21452290 | pmc = 3149125 | doi = 10.1002/hep.24330 }}</ref><ref>{{cite web | title = Hemochromatosis | url = http://eguideline.guidelinecentral.com/i/98549-aasld-hemochromatosis/2 | work = guidelinecentral.com }}</ref>

Transferrin and its receptor have been shown to diminish [[tumour cells]] when the receptor is used to attract [[antibodies]].<ref name="pmid18473900"/>

== Transferrin and nanomedicine ==
Many drugs are hindered when providing treatment when crossing the blood-brain barrier yielding poor uptake into areas of the brain. Transferrin glycoproteins are able to bypass the [[Blood–brain barrier|blood-brain barrier]] via receptor-mediated transport for specific transferrin receptors found in the brain capillary endothelial cells.<ref>{{cite journal | vauthors = Ghadiri M, Vasheghani-Farahani E, Atyabi F, Kobarfard F, Mohamadyar-Toupkanlou F, Hosseinkhani H | title = Transferrin-conjugated magnetic dextran-spermine nanoparticles for targeted drug transport across blood-brain barrier | journal = Journal of Biomedical Materials Research Part A | volume = 105 | issue = 10 | pages = 2851–2864 | date = October 2017 | pmid = 28639394 | doi = 10.1002/jbm.a.36145 }}</ref> Due to this functionality, it is theorized that [[Nanoparticles for drug delivery to the brain|nanoparticles]] acting as drug carriers bound to transferrin glycoproteins can penetrate the blood-brain barrier allowing these substances to reach the diseased cells in the brain.<ref>{{cite journal | vauthors = Gaspar R | title = Nanoparticles: Pushed off target with proteins | journal = Nature Nanotechnology | volume = 8 | issue = 2 | pages = 79–80 | date = February 2013 | pmid = 23380930 | doi = 10.1038/nnano.2013.11 | bibcode = 2013NatNa...8...79G }}</ref> Advances with transferrin conjugated nanoparticles can lead to non-invasive drug distribution in the brain with potential therapeutic consequences of [[central nervous system]] (CNS) targeted diseases (e.g. [[Alzheimer's disease|Alzheimer's]] or [[Parkinson's disease|Parkinson's]] disease).<ref>{{cite journal | vauthors = Li S, Peng Z, Dallman J, Baker J, Othman AM, Blackwelder PL, Leblanc RM | title = Crossing the blood-brain-barrier with transferrin conjugated carbon dots: A zebrafish model study | journal = Colloids and Surfaces B: Biointerfaces | volume = 145 | pages = 251–256 | date = September 2016 | pmid = 27187189 | doi = 10.1016/j.colsurfb.2016.05.007 | doi-access = free }}</ref>

== Other effects ==

[[Carbohydrate deficient transferrin]] increases in the blood with heavy [[ethanol]] consumption and can be monitored through laboratory testing.<ref name="pmid11732647">{{cite journal | vauthors = Sharpe PC | title = Biochemical detection and monitoring of alcohol abuse and abstinence | journal = Annals of Clinical Biochemistry | volume = 38 | issue = Pt 6 | pages = 652–64 | date = November 2001 | pmid = 11732647 | doi = 10.1258/0004563011901064 | s2cid = 12203099 | doi-access =  }}</ref>

Transferrin is an acute phase protein and is seen to decrease in inflammation, cancers, and certain diseases (in contrast to other acute phase proteins, e.g., C-reactive protein, which increase in case of acute inflammation).<ref name="pmid21430962">{{cite journal | vauthors = Jain S, Gautam V, Naseem S | title = Acute-phase proteins: As diagnostic tool | journal = Journal of Pharmacy & Bioallied Sciences | volume = 3 | issue = 1 | pages = 118–27 | date = January 2011 | pmid = 21430962 | pmc = 3053509 | doi = 10.4103/0975-7406.76489 | doi-access = free }}</ref>

== Pathology ==

[[Atransferrinemia]] is associated with a deficiency in transferrin.

In nephrotic syndrome, urinary loss of transferrin, along with other serum proteins such as thyroxine-binding globulin, gammaglobulin, and anti-thrombin III, can manifest as iron-resistant [[microcytic anemia]].

== Reference ranges ==
An example [[Reference ranges for blood tests#Other electrolytes and metabolites|reference range]] for transferrin is 204–360&nbsp;mg/dL.<ref name="southwest">{{cite web|url=http://pathcuric1.swmed.edu/PathDemo/nrrt.htm |title=Normal Reference Range Table |work=Interactive Case Study Companion to Pathological Basis of Disease |publisher=The University of Texas Southwestern Medical Center at Dallas |access-date=2008-10-25 |url-status=dead |archive-url=https://web.archive.org/web/20111225185659/http://pathcuric1.swmed.edu/PathDemo/nrrt.htm |archive-date=2011-12-25 }}<br/>{{cite book | author = Kumar V, Hagler HK | title = Interactive Case Study Companion to Robbins Pathologic Basis of Disease | edition = 6th Edition (CD-ROM for Windows & Macintosh, Individual) | publisher = W B Saunders Co | year = 1999 | isbn = 0-7216-8462-9 }}</ref> Laboratory test results should always be interpreted using the reference range provided by the laboratory that performed the test{{citation needed|date=November 2023}}.

[[File:Blood values sorted by mass and molar concentration.png|thumb|550px|left|[[Reference ranges for blood tests]], comparing blood content of transferrin and other iron-related compounds (shown in brown and orange) with other constituents]]

{{Clear}}

A high transferrin level may indicate an [[iron deficiency anemia]]. Levels of [[serum iron]] and [[total iron binding capacity]] (TIBC) are used in conjunction with transferrin to specify any abnormality. See [[TIBC#Interpretation|interpretation of TIBC]]. Low transferrin likely indicates [[malnutrition]].

== Interactions ==

Transferrin has been shown to [[Protein-protein interaction|interact]] with [[insulin-like growth factor 2]]<ref name="pmid11749962">{{cite journal | vauthors = Storch S, Kübler B, Höning S, Ackmann M, Zapf J, Blum W, Braulke T | title = Transferrin binds insulin-like growth factors and affects binding properties of insulin-like growth factor binding protein-3 | journal = FEBS Letters | volume = 509 | issue = 3 | pages = 395–8 | date = December 2001 | pmid = 11749962 | doi = 10.1016/S0014-5793(01)03204-5 | s2cid = 22895295 | doi-access = free }}</ref> and [[IGFBP3]].<ref name="pmid11297622">{{cite journal | vauthors = Weinzimer SA, Gibson TB, Collett-Solberg PF, Khare A, Liu B, Cohen P | title = Transferrin is an insulin-like growth factor-binding protein-3 binding protein | journal = The Journal of Clinical Endocrinology and Metabolism | volume = 86 | issue = 4 | pages = 1806–13 | date = April 2001 | pmid = 11297622 | doi = 10.1210/jcem.86.4.7380 | doi-access = free }}</ref> Transcriptional regulation of transferrin is upregulated by [[retinoic acid]].<ref name="pmid1315521">{{cite journal | vauthors = Hsu SL, Lin YF, Chou CK | title = Transcriptional regulation of transferrin and albumin genes by retinoic acid in human hepatoma cell line Hep3B | journal = The Biochemical Journal | volume = 283 ( Pt 2) | issue = 2 | pages = 611–5 | date = April 1992 | pmid = 1315521 | pmc = 1131079 | doi = 10.1042/bj2830611 }}</ref>

==Related proteins==
Members of the family include blood serotransferrin (or siderophilin, usually simply called transferrin); [[lactotransferrin]] (lactoferrin); milk transferrin; egg white [[ovotransferrin]] (conalbumin); and membrane-associated [[melanotransferrin]].<ref>{{cite journal | vauthors = Chung MC | title = Structure and function of transferrin | journal = Biochemical Education | volume = 12 | issue = 4 | pages = 146–154 |date=October 1984 | doi = 10.1016/0307-4412(84)90118-3 }}</ref>

== See also ==
* [[Beta-2 transferrin]]
* [[Transferrin receptor]]
* [[Total iron-binding capacity]]
* [[Transferrin saturation]]
* [[Ferritin]]
* [https://invitria.com/products/optiferrin-recombinant-human-transferrin/ Optiferrin recombinant human transferrin]
* [[Atransferrinemia]]
* [[Hypotransferrinemia]]
* [[HFE H63D gene mutation]]

== References ==
{{Reflist|33em}}

== Further reading ==
{{Refbegin}}
* {{cite journal | vauthors = Hershberger CL, Larson JL, Arnold B, Rosteck PR, Williams P, DeHoff B, Dunn P, O'Neal KL, Riemen MW, Tice PA | display-authors = 6 | title = A cloned gene for human transferrin | journal = Annals of the New York Academy of Sciences | volume = 646 | issue = 1 | pages = 140–54 | date = December 1991 | pmid = 1809186 | doi = 10.1111/j.1749-6632.1991.tb18573.x | bibcode = 1991NYASA.646..140H | s2cid = 19519911 }}
* {{cite book | vauthors = Bowman BH, Yang FM, Adrian GS | title = Transferrin: evolution and genetic regulation of expression | volume = 25 | pages = 1–38 | year = 1989 | pmid = 3057819 | doi = 10.1016/S0065-2660(08)60457-5 | isbn = 9780120176250 | series = Advances in Genetics }}
* {{cite journal | vauthors = Parkkinen J, von Bonsdorff L, Ebeling F, Sahlstedt L | title = Function and therapeutic development of apotransferrin | journal = Vox Sanguinis | volume = 83 | issue = Suppl 1 | pages = 321–6 | date = August 2002 | pmid = 12617162 | doi = 10.1111/j.1423-0410.2002.tb05327.x | s2cid = 5876134 }}
{{Refend}}

== External links ==
* {{MeshName|Transferrin}}
* {{PDBe-KB2|P02787|Serotransferrin}}

{{PDB Gallery|geneid=7018}}
{{Iron-binding proteins}}
{{Beta globulins}}
{{Acute phase proteins}}
{{Iron metabolism}}
{{Authority control}}

[[Category:Chemical pathology]]
[[Category:Iron metabolism]]
[[Category:Transferrins]]