User:Frog21/Ltf using MGI Gene box
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. 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 has the highest concentration, followed by human milk, then cow milk.
Structure
[edit]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+2 ions. It contains 4 identical domains, with two surrounding each iron atom.
Function
[edit]Lactoferrin antimicrobial activity is due partly to its high affinity for Fe3+ (ferric state). LF proteolysis produces lactoferricin, kaliocin-1 small peptides with antimicrobial activity. The combination of iron and lactoferrin in mucosal secretions modulate the ability and aggregation of pathogenic bacteria, and inhibit both bacteria and viruses by binding to host cells/viral particles. This inhibits the ability of bacteria and viruses to attach to cell membranes. It is also an antifungal agent.
Lactoferrin receptors have been found on brush-border cells, PMN, monocytes, Mφ and activated lymphocytes.
Lactoferrin inhibits dendritic cell-mediated HIV-1 transmission by blocking gp120 to DC-SIGN , which is a critical protein that never changes regardless of strain.[1]
Genetics
[edit]In humans, the lactoferrin gene (LTF) is located on chromosome 3; location: 3q21-q23.
References
[edit]- ^ 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:10.1128/JVI.79.5.3009-3015.2005. PMC 548463. PMID 15709021.
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Further reading
[edit]- van der Strate BW, Beljaars L, Molema G; et al. (2002). "Antiviral activities of lactoferrin". Antiviral Res. 52 (3): 225–39. doi:10.1016/S0166-3542(01)00195-4. PMID 11675140.
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(help)CS1 maint: multiple names: authors list (link) - Weinberg ED (2002). "Human lactoferrin: a novel therapeutic with broad spectrum potential". J. Pharm. Pharmacol. 53 (10): 1303–10. doi:10.1211/0022357011777792. 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:10.1007/s00018-005-5372-0. 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:10.1007/s00018-005-5369-8. PMID 16261256.
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External links
[edit]- lactoferrinresearch.org
- InVitria - sells Lacromin, a holo-lactoferrin (iron saturated)
- Expasy Database, chemical structure
- LTF on the National Center for Biotechnology Information
- Thompson.net Supported information about lactoferrin.
- FDA Lactoferrin Considered Safe to Fight E. Coli.
- Ventria Bioscience - a source of non-animal breastmilk equivalent lactoferrin
- Agennix.com A biopharmaceutical company focused on developing protein-based drugs for cancer and diabetic ulcers.
- Pharming.com A biopharmaceutical company producing lactoferrin.