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Overview

Lactoferrin: the first line of defense for the body's immune system
Lactoferrin is a minor glycoprotein component of whey. It belongs to the iron transporter or transferrin family of glycoproteins. Lactoferrin is also found in exocrine secretions from mammals and is released from neutrophil granules during inflammation. The lactoferrin concentration in bovine (cows) milk is only 0.5% to 1.0% while human breast milk can contain as much as 15% lactoferrin.

Lactoferrin plays several important roles in human biology. First, Lactoferrin is believed to play a role in the uptake and absorption of iron through the intestinal mucosa. It may be the primary or sole source of iron for breast fed infants. Second, Lactoferrin appears to have antibacterial, antiviral, antifungal, anti-inflammatory, antioxidant and immunomodulatory activities. Receptors for lactoferrin are found in monocytes, lymphocytes, neutrophils, intestinal tissue and on certain bacteria. Lactoferrin's ability to bind iron may account for some of its anti-bacterial activity. Iron is essential to support the growth of pathogenic bacteria. Lactoferrin may also inhibit the attachment of bacteria to the intestinal wall.

The possible antiviral activity of supplemental lactoferrin may be due to its inhibition of virus-cell fusion and viral entry into cells. It is believed that Lactoferrin may promote the growth and differentiation of T- lymphocytes. Lactoferrin appears to bind uniquely to sites on the T4 (helper) and T8 (suppressor) lymphocytes. Lactoferrin also appears to play a role in the regulation of cytokines and lymphokines, such as tumor necrosis (TNF)-alpha and interleukin (IL)-6.
Lactoferrin's possible antioxidant activity may also contribute to its possible immunomodulatory activity. Antioxidants are getting increasing attention as possible therapeutic agents in infections and a variety of other diseases. Lactoferrin's ability to bind iron probably contributes to both its antioxidant properties and its antibacterial action. Free iron is a contributor in the generation of free radicals.

What is Lactoferrin ?
Lactoferrin is an iron-binding glycoprotein that belongs to the transferrin family. It is present in breast milk, in epithelial secretions, and in the secondary granules of neutrophils. In healthy subjects lactoferrin circulates at concentrations of 2-7 x 10−6 g/ml. Lactoferrin is a pleiotropic factor with potent antimicrobial and immunomodulatory activities. Recently, we have shown that lactoferrin can also promote bone growth. At physiological concentrations, lactoferrin potently stimulates the proliferation and differentiation of primary osteoblasts and also acts as a survival factor inhibiting apoptosis induced by serum withdrawal. Lactoferrin also affects osteoclast formation and, in murine bone marrow culture, lactoferrin potently inhibits osteoclastogenesis. In vivo, local injection of lactoferrin above the hemicalvaria of adult mice results in substantial increases in the dynamic histomorphometric indices of bone formation and bone area.
The mitogenic effect of lactoferrin in osteoblast-like cells is mediated mainly through LRP1, a member of the family of low-density lipoprotein receptor-related proteins that are primarily known as endocytic receptors. Using confocal laser scanning microscopy, we demonstrated that fluorescently labeled lactoferrin is endocytosed and can be visualized in the cytoplasm of primary osteoblastic cells. Lactoferrin also induces activation of p42/44 MAPK signaling in primary osteoblasts, but the two pathways seem to operate independently as activation of MAPK signaling, but not endocytosis, is necessary for the mitogenic effect of lactoferrin. We conclude that lactoferrin may have a physiological role in bone growth and healing, and a potential therapeutic role as an anabolic factor in osteoporosis.

How it is made
Most medicinal human lactoferrin is taken from specially engineered rice, but some are extracting high purity lactoferrin from milk.

Where it is found
It is found in both human and bovine milk. (Human breast milk and cow's milk) and in colostrum, the first milk produced for newborns.
Though a natural component of cows and human mother's milk, lactoferrin is found throughout the human body and occurs in all secretions that bathe mucous membranes such as saliva, tears, bronchial and nasal secretions, hepatic bile, pancreatic fluids, and is an essential factor in the immune response. Human colostrum has the highest concentration, followed by human milk, then cow milk.

Product related PDF file
Lactoferrin in health and disease.
Lactoferrin - Slide show

Benefits / uses
IBS (Irritable Bowel Syndrome) and Gut Health
Lactoferrin capsules help maintain optimum levels of beneficial bacteria such as "Bifidus", in the intestinal tract and so prevent gastrointestinal inflammations. Lactoferrin does not target specific types of bacteria. This is very important. This non-specific nature has proved to be a blessing in disguise. Many antibiotics are designed to counter specific bacteria. They can become less effective over time because bacteria are capable of developing strains that are resistant to the antibiotic. This is not the case with lactoferrin.

Lactoferrin has exhibited significant activity against Escherichia coli (E-Coli), Proteus mirabilis, Staphylococcus aureus, Candida albicans, HIV, herpes simplex type 1, hepatitis C, cytomegalovirus and other pathogens in vitro (in a lab dish) studies. Lactoferrin ability to carry iron without generating free radicals is one form of antioxidant activity. This antioxidant activity helps protect the body.

Lactoferrin and Cancer Prevention
Over a dozen studies from specialist Universities around the world have shown that Lactoferrin and related peptides suppress tumour growth and prevent tumour formation. It has been used in conjunction with chemotherapy to reduce the number of infections due to weakening of the immune system. One study notes that Lactoferrin "might become the substance of choice for the adjutant therapy against pancreatic cancer".

Lactoferrin and Skin Care
Lactoferrin is used as an ingredient in anti-aging formulas, and in Acne/problem skin products. From an anti-ageing perspective, Lactoferrin inhibits the forming of free radicals which damage the DNA makeup of your skin. Also, in preventing the degradation of Collagen in the skin, Lactoferrin delays the visual ageing process.

Lactoferrin is widely used in overseas countries and has been for quite some time. Its anti-bacterial, anti-viral and anti-fungal properties clearly benefit the internal health of user's in many ways. Lactoferrin is being continually researched and studied and it becomes more and more apparent that this natural substance is certainly beneficial to ones health.

Doses
Oral lactoferrin dosed at 40 mg daily has been used in a couple of clinical trials. Those who supplement with lactoferrin typically take 250 mg daily.

Possible Side effects / Precautions / Possible Interactions:
Some individuals may have a hypersensitivity or allergy to lactoferrin. It is contraindicated for those individuals. It is generally recommended that pregnant women and nursing mothers avoid using lactoferrin because it has not been tested in these conditions. Some in vitro studies suggest that lactoferrin acts synergistically with antifungal agents, making them more potent.

Research Studies / References

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arw M. Sorensen and S. P. L. Sorensen, Compf. rend. trav. lab. Carlsberg (1939) 23, 55, cited by Groves (1960)


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arw .N aidu AS (2000). Lactoferrin: natural, multifunctional, antimicrobial. Boca Raton: CRC Press. pp. 1-2. ISBN 0-8493-0909-3. http://books.google.com/?id=2oTsweiwImAC&pg=PA2.


arw Birgens HS (1985). "Lactoferrin in plasma measured by an ELISA technique: evidence that plasma lactoferrin is an indicator of neutrophil turnover and bone marrow activity in acute leukaemia". Scand J Haematol 34 (4): 326-31. doi:10.1111/j.1600-0609.1985.tb00757.x. PMID 3858982.


arw Baker HM, Anderson BF, Kidd RD, Shewry SC, Baker EN (2000). "Lactoferrin three-dimensional structure: a framework for interpreting function". In Shimazaki, Kei-ichi. Lactoferrin: structure, function, and applications: proceedings of the 4th International Conference on Lactoferrin: Structure, Function, and Applications, held in Sapporo, Japan, 18-22 May 1999. Amsterdam: Elsevier. ISBN 0-444-50317-X.


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arw Shongwe MS, Smith CA, Ainscough EW, Baker HM, Brodie AM, Baker EN (1992). "Anion binding by human lactoferrin: results from crystallographic and physicochemical studies". Biochemistry 31 (18): 4451-8. doi:10.1021/bi00133a010. PMID 1581301.


arw a b c Bennett RM, Davis J (1982). "Lactoferrin interacts with deoxyribonucleic acid: a preferential reactivity with double-stranded DNA and dissociation of DNA-anti-DNA complexes". J. Lab. Clin. Med. 99 (1): 127-38. PMID 6274982.


arw Bagby GC, Bennett RM (1982). "Feedback regulation of granulopoiesis: polymerization of lactoferrin abrogates its ability to inhibit CSA production". Blood 60 (1): 108-12. PMID 6979357.


arw Mantel C, Miyazawa K, Broxmeyer HE (1994). "Physical characteristics and polymerization during iron saturation of lactoferrin, a myelopoietic regulatory molecule with suppressor activity". Adv. Exp. Med. Biol. 357: 121-32. PMID 7762423.


arw Furmanski P, Li ZP, Fortuna MB, Swamy CV, Das MR (1989). "Multiple molecular forms of human lactoferrin. Identification of a class of lactoferrins that possess ribonuclease activity and lack iron-binding capacity". J. Exp. Med. 170 (2): 415-29. doi:10.1084/jem.170.2.415. PMC 2189405. PMID 2754391. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2189405.


arw "Lactoferrin: a review". Veterinarni Medicina 53: 457. 2008. http://www.vri.cz/docs/vetmed/53-9-457.pdf.


arw a b Farnaud S, Evans RW (2003). "Lactoferrin--a multifunctional protein with antimicrobial properties". Mol. Immunol. 40 (7): 395-405. doi:10.1016/S0161-5890(03)00152-4. PMID 14568385.


arw Xanthou M (1998). "Immune protection of human milk". Biol. Neonate 74 (2): 121-33. doi:10.1159/000014018. PMID 9691154.


arw Odell EW, Sarra R, Foxworthy M, Chapple DS, Evans RW (1996). "Antibacterial activity of peptides homologous to a loop region in human lactoferrin". FEBS Lett. 382 (1-2): 175-8. doi:10.1016/0014-5793(96)00168-8. PMID 8612745.


arw Kuwata H, Yip TT, Yip CL, Tomita M, Hutchens TW (1998). "Bactericidal domain of lactoferrin: detection, quantitation, and characterization of lactoferricin in serum by SELDI affinity mass spectrometry". Biochem. Biophys. Res. Commun. 245 (3): 764-73. doi:10.1006/bbrc.1998.8466. PMID 9588189.


arw a b c d Sojar HT, Hamada N, Genco RJ (1998). "Structures involved in the interaction of Porphyromonas gingivalis fimbriae and human lactoferrin". FEBS Lett. 422 (2): 205-8. doi:10.1016/S0014-5793(98)00002-7. PMID 9490007.


arw ^ a b van der Strate BW, Beljaars L, Molema G, Harmsen MC, Meijer DK (2001). "Antiviral activities of lactoferrin". Antiviral Res. 52 (3): 225-39. doi:10.1016/S0166-3542(01)00195-4. PMID 11675140.


arw Fujihara T, Hayashi K (1995). "Lactoferrin inhibits herpes simplex virus type-1 (HSV-1) infection to mouse cornea". Arch. Virol. 140 (8): 1469-72. doi:10.1007/BF01322673. PMID 7661698.


arw a b Giansanti F, Rossi P, Massucci MT, Botti D, Antonini G, Valenti P, Seganti L (2002). "Antiviral activity of ovotransferrin discloses an evolutionary strategy for the defensive activities of lactoferrin". Biochem. Cell Biol. 80 (1): 125-30. doi:10.1139/o01-208. PMID 11908636.


arw Harmsen MC, Swart PJ, de Béthune MP, Pauwels R, De Clercq E, The TH, Meijer DK (1995). "Antiviral effects of plasma and milk proteins: lactoferrin shows potent activity against both human immunodeficiency virus and human cytomegalovirus replication in vitro". J. Infect. Dis. 172 (2): 380-8. PMID 7622881.


arw a b Puddu P, Borghi P, Gessani S, Valenti P, Belardelli F, Seganti L (1998). "Antiviral effect of bovine lactoferrin saturated with metal ions on early steps of human immunodeficiency virus type 1 infection". Int. J. Biochem. Cell Biol. 30 (9): 1055-62. doi:10.1016/S1357-2725(98)00066-1. PMID 9785469.


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arw a b c Nozaki A, Ikeda M, Naganuma A, Nakamura T, Inudoh M, Tanaka K, Kato N (2003). "Identification of a lactoferrin-derived peptide possessing binding activity to hepatitis C virus E2 envelope protein". J. Biol. Chem. 278 (12): 10162-73. doi:10.1074/jbc.M207879200. PMID 12522210.


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