An iron-binding protein found in neutrophils and bodily secretions (milk, tears, saliva, bile, etc.), having bactericidal activity, and acting as an inhibitor of colony formation by granulocytes and macrophages.
Lactoferrin
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| Lactotransferrin | ||||||||||||||
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| Richardson diagram of recombinant human lactoferrin. Based on PDB 1b0l. | ||||||||||||||
| Available structures | ||||||||||||||
| 1b0l, 1bka, 1cb6, 1dsn, 1eh3, 1fck, 1h43, 1h44, 1h45, 1hse, 1l5t, 1lcf, 1lct, 1lfg, 1lfh, 1lfi, 1lgb, 1n76, 1sqy, 1vfd, 1vfe, 1z6v, 1z6w, 2bjj | ||||||||||||||
| Identifiers | ||||||||||||||
| Symbols | LTF; GIG12; HLF2 | |||||||||||||
| External IDs | OMIM: 150210 MGI: 96837 HomoloGene: 1754 | |||||||||||||
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| Orthologs | ||||||||||||||
| Species | Human | Mouse | ||||||||||||
| Entrez | 4057 | 17002 | ||||||||||||
| Ensembl | ENSG00000012223 | ENSMUSG00000032496 | ||||||||||||
| UniProt | P02788 | Q3TP24 | ||||||||||||
| RefSeq | NM_002343 (mRNA) | NM_008522 (mRNA) | ||||||||||||
| NP_002334 (protein) | NP_032548 (protein) | |||||||||||||
| Location | Chr 3: 46.48 - 46.53 Mb |
Chr 9: 110.86 - 110.89 Mb |
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| PubMed search | [1] | [2] | ||||||||||||
Lactoferrin (LF), also known as lactotransferrin (LTF), is a globular multifunctional protein with antimicrobial activity (bacteriocide, fungicide) and is part of the innate defense, mainly at mucoses.[1] Lactoferrin is found in milk and many mucosal secretions such as tears and saliva. Lactoferrin is also present in secondary granules of PMN and also is secreted by some acinar cells. Lactoferrin can be purified from milk or produced recombinantly. Human colostrum ("first milk") has the highest concentration, followed by human milk, then cow milk.[1]
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Structure
Lactoferrin belongs to the transferrin family proteins (TF, melanotransferrin, ovotransferin, etc.). Its molecular mass is 80,000 u (80 kDa). It generally contains two bound Fe+3 ions. It contains 4 identical domains, with two surrounding each iron atom.[2]
Function
Lactoferrin's antimicrobial activity is due partly to its high affinity for Fe3+ (ferric state). LF proteolysis produces the small peptides lactoferricin and kaliocin-1 with antimicrobial activity. The combination of iron and lactoferrin in mucosal secretions modulates the ability and aggregation of pathogenic bacteria, and inhibits both bacteria and viruses from binding to host cells. It is also an antifungal agent[citation needed].
Lactoferrin receptors have been found on brush-border cells, PMN, monocytes, macrophages and activated lymphocytes.[3]
Lactoferrin inhibits dendritic cell-mediated HIV-1 transmission by blocking the binding of the HIV protein gp120 to the cellular receptor DC-SIGN, which is a critical binding interaction that never changes regardless of strain.[4]
Genetics
In humans, the lactoferrin gene (LTF) is located on chromosome 3; location: 3q21-q23.[5]
References
- ^ a b Sánchez L, Calvo M, Brock JH (May 1992). "Biological role of lactoferrin". Arch. Dis. Child. 67 (5): 657–61. PMID 1599309.
- ^ Baker EN, Baker HM (January 2009). "A structural framework for understanding the multifunctional character of lactoferrin". Biochimie 91 (1): 3–10. doi:. PMID 18541155.
- ^ Levay PF, Viljoen M (1995). "Lactoferrin: a general review". Haematologica 80 (3): 252–67. PMID 7672721.
- ^ Groot F, Geijtenbeek TB, Sanders RW, et al. (March 2005). "Lactoferrin prevents dendritic cell-mediated human immunodeficiency virus type 1 transmission by blocking the DC-SIGN--gp120 interaction". J. Virol. 79 (5): 3009–15. doi:. PMID 15709021.
- ^ McCombs JL, Teng CT, Pentecost BT, Magnuson VL, Moore CM, McGill JR (1988). "Chromosomal localization of human lactotransferrin gene (LTF) by in situ hybridization". Cytogenet. Cell Genet. 47 (1-2): 16–7. PMID 3356163.
Further reading
- van der Strate BW, Beljaars L, Molema G, et al. (2002). "Antiviral activities of lactoferrin". Antiviral Res. 52 (3): 225–39. doi:. PMID 11675140.
- Weinberg ED (2002). "Human lactoferrin: a novel therapeutic with broad spectrum potential". J. Pharm. Pharmacol. 53 (10): 1303–10. doi:. PMID 11697537.
- Valenti P, Antonini G (2006). "Lactoferrin: an important host defence against microbial and viral attack". Cell. Mol. Life Sci. 62 (22): 2576–87. doi:. PMID 16261253.
- Ward PP, Paz E, Conneely OM (2006). "Multifunctional roles of lactoferrin: a critical overview". Cell. Mol. Life Sci. 62 (22): 2540–8. doi:. PMID 16261256.
External links
- Expasy Database, chemical structure
- LTF on the National Center for Biotechnology Information
- FDA Lactoferrin Considered Safe to Fight E. Coli.
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 | Veterinary Dictionary. Saunders Comprehensive Veterinary Dictionary 3rd Edition. Copyright © 2007 by D.C. Blood, V.P. Studdert and C.C. Gay, Elsevier. All rights reserved. Read more |
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