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Lactotransferrin
File:Lactopherrin.png
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 OMIM150210 MGI96837 HomoloGene1754 GeneCards: LTF Gene
Orthologs
Species Human Mouse
Entrez 4057 17002
Ensembl ENSG00000012223 ENSMUSG00000032496
UniProt P02788 Q3TP24
RefSeq (mRNA) NM_002343 NM_008522
RefSeq (protein) NP_002334 NP_032548
Location (UCSC) Chr 3:
46.48 - 46.53 Mb
Chr 9:
110.86 - 110.89 Mb
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 (150 mg/l).[1]

Contents

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]

Cystic fibrosis

The human lung as well as saliva contain a wide range of antimicrobial compound including lactoperoxidase system producing hypothiocyanite and lactoferrin while hypothiocyanite is missing in cystic fibrosis patients.[6] Lactoferrin, a component of innate immunity, prevents bacterial biofilm development.[7][8] The loss of microbicidal activity and increased formation of biofilm due to decreased lactoferrin activity in patients with cystic fibrosis.[9] These findings demonstrate the important role of lactoferrin in human host defence and especially in lung.[10]

Lactoferrin with hypothiocyanite has been been granted orphan drug status by the EMEA[11] and the FDA.[12]

See also

References

  1. ^ a b Sánchez L, Calvo M, Brock JH (May 1992). "Biological role of lactoferrin". Arch. Dis. Child. 67 (5): 657–61. PMID 1599309. 
  2. ^ Baker EN, Baker HM (January 2009). "A structural framework for understanding the multifunctional character of lactoferrin". Biochimie 91 (1): 3–10. doi:10.1016/j.biochi.2008.05.006. PMID 18541155. 
  3. ^ Levay PF, Viljoen M (1995). "Lactoferrin: a general review". Haematologica 80 (3): 252–67. PMID 7672721. 
  4. ^ 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. PMID 15709021. 
  5. ^ 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. 
  6. ^ Moskwa P, Lorentzen D, Excoffon KJ, Zabner J, McCray PB, Nauseef WM, Dupuy C, Bánfi B (January 2007). "A novel host defense system of airways is defective in cystic fibrosis". Am. J. Respir. Crit. Care Med. 175 (2): 174–83. doi:10.1164/rccm.200607-1029OC. PMID 17082494. 
  7. ^ Singh PK, Schaefer AL, Parsek MR, Moninger TO, Welsh MJ, Greenberg EP (October 2000). "Quorum-sensing signals indicate that cystic fibrosis lungs are infected with bacterial biofilms". Nature 407 (6805): 762–4. doi:10.1038/35037627. PMID 11048725. 
  8. ^ Singh PK, Parsek MR, Greenberg EP, Welsh MJ (May 2002). "A component of innate immunity prevents bacterial biofilm development". Nature 417 (6888): 552–5. doi:10.1038/417552a. PMID 12037568. 
  9. ^ Rogan MP, Taggart CC, Greene CM, Murphy PG, O'Neill SJ, McElvaney NG (October 2004). "Loss of microbicidal activity and increased formation of biofilm due to decreased lactoferrin activity in patients with cystic fibrosis". J. Infect. Dis. 190 (7): 1245–53. doi:10.1086/423821. PMID 15346334. 
  10. ^ Rogan MP, Geraghty P, Greene CM, O'Neill SJ, Taggart CC, McElvaney NG (2006). "Antimicrobial proteins and polypeptides in pulmonary innate defence". Respir. Res. 7: 29. doi:10.1186/1465-9921-7-29. PMID 16503962. 
  11. ^ "Public summary of positive opinion for orphan designation of hypothiocyanite / lactoferrin for the treatment of cystic fibrosis". Pre-authorisation Evaluation of Medicines for Human Use. European Medicines Agency. 2009-09-07. http://www.ema.europa.eu/pdfs/human/comp/opinion/39298409en.pdf. Retrieved 2010-01-23. 
  12. ^ "Meveol: orphan drug status granted by the FDA for the treatment of cystic fibrosis.". United States Food and Drug Administration. c2009-11-05. http://www.bioalaxia.eu/content/meveol-orphan-drug-status-granted-fda-treatment-cystic-fibrosis. Retrieved 2010-01-23. 

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