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Proline-rich Polypeptides and Lactoferrin References
General
Dutta RC. (2002) Peptide immunomodulators versus infection; an analysis. Immunology Letters 83(3):153-61. Immune stimulators have been found to be useful in helping to fight off infections, while immunosuppressors have been found useful in autoimmune conditions and transplants.
PubMed Reference
PMID:
12095705
Zimecki M, Artym J. (2005) [Therapeutic properties of proteins and peptides from colostrum and milk] Postepy Higieny i Medycyny Doświadczalnej 59:309-23. Colostrum and milk are rich in peptides and proteins which play an active role in innate immunity. Lactoferrin has antibacterial, antifungal, antiviral, antiparasitic, and antitumor activities. It helps protect the intestinal epithelium, promotes bone growth, and accelerates the recovery of immune system function in immunocompromised animals. PRP has a variety of immunotropic functions, including the promotion of T cell maturation and inhibition of autoimmune disorders.
PubMed Reference
PMID:15995598
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Proline-rich Polypeptides (PRP)
Includes transfer factor, colostrinin(e), dialyzable leukocyte extract (DLE)
Ablashi DV, Levine PH, De Vinci C, Whitman JE Jr, Pizza G, Viza D. Use of anti HHV-6 transfer factor for the treatment of two patients with chronic fatigue syndrome (CFS). Two case reports. Biotherapy 9(1-3):81-6 (1996). Transfer factor (PRP) specific to Human Herpes Virus-6 (HHV-6) significantly improved the clinical manifestations of one patient suffering from chronic fatigue syndrome, while another showed no improvement.
PubMed Reference
PMID:8993763
Alvarez-Thull L, Kirkpatrick CH. (1996) Profiles of cytokine production in recipients of transfer factors. Biotherapy 9(1-3):55-9. Cell cultures from mice responded to HSV infection by secreting large amounts of IL-2 and INF-γ, modest amounts of IL-10, and no IL-4. The same cells responded to concanavalin A and HSV in a similar manner, but instead of IL-2, they produced large amounts of TNF-α, showing that TF (i.e. PRP) treatment selectively affects cytokine production depending on antigenic stimulation.
PubMed Reference
PMID:8993758
An Examination of Immune Response Modulation in Humans by Ai/E¹º® Utilizing A Double Blind Study. Immune Consultants, Inc., Tucson, Arizona (2001). 20 subjects, 10 men and 10 women, ranging in age from 32-61 participated in a double blind study in which 10 received DLE and the other 10 received placebo. 7 of the 10 receiving the DLE had a significant increase in three major immune markers: NK cell activity, TNF-α levels, and phagocytic index (PI), an indicator of macrophage activity. Those receiving placebo had mixed results
Boldogh I, Liebenthal D, Hughes TK, Juelich TL, Georgiades JA, Kruzel ML, Stanton GJ. (2003) Modulation of 4HNE-mediated signaling by proline-rich peptides from ovine colostrum. Journal of Molecular Neuroscience 20(2):125-34. PRP, also known as colostrinin, induces mitogenic stimulation as well as a variety of cytokines in peripheral leukocytes. It also possess antioxidant activity in pheochromocytoma (P12) cells, a cancer cell line used for in vitro studies. PRP was shown to reduce the amount of 4HNE-protein adducts, reduce intracellular levels of reactive oxygen species, inhibit 4HNE-mediated glutathione depletion, and inhibit 4HNE-induced activation of the molecular signal cascade which results in the production of c-Jun N-terminal kinase (JNK) in P12 cells. This shows that PRP acts as both an antioxidant and a molecular signaling device.
PubMed Reference
PMID:12794306
Boldogh I, Aguilera-Aguirre L, Bacsi A, Choudhury BK, Saavedra-Molina A, Kruzel M. (2008) Colostrinin Decreases Hypersensitivity and Allergic Responses to Common Allergens. International Archives of Allergy and Immunology 146(4):298-306. Colostrinin (PRP) significantly reduced IgE and IgG1 production, airway eosinophilia, mucin production, and hypersensitivity induced by allergen extracts from ragweed pollen grains and house dust mites. Colostrinin itself is non-allergenic. This study supports the use of colostrinin for the prevention of allergic inflammation in humans.
PubMed Reference
PMID:18367843
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De Vinci C, Levine PH, Pizza G, Fudenberg HH, Orens P, Pearson G, Viza D. (1996) Lessons from a pilot study of transfer factor in chronic fatigue syndrome. Biotherapy 9(1-3):87-90. Transfer factor (PRP) was used in a placebo controlled study of 20 chronic fatigue patients. Efficacy of the treatment was measured by clinical monitoring and testing for antibodies to Epstein-Barr and human herpes virus-6 antibodies. Improvement was noted in 12 of the 20 patients.
PubMed Reference
PMID:8993764
Effects of Oral Dietary Supplementation with Ai/E¹º® Upon Natural Killer (NK) Cell Activity in a Healthy Human Population. Quantum Research, Inc., Scottsdale, Arizona (2001). Dialyzable Leukocyte Extract (DLE) was administered to 12 healthy male and female subjects aged 24-63. Natural Killer (NK) cell activity was prior to initiation of the study and after completion of the study. NK cell activity averaged 30 lytic units (LU) prior to the study and 101 LU following the study for an average increase of 207%.
Fernandez-Ortega, C, Dubed, M, Ruibal, O, Vilarrubia, OL, Menendez de San Pedro, JC, Navea, L, Ojeda, M, Arana, MJ. Inhibition of in vitro HIV infection by dialysable leucocyte extracts. Biotherapy 9(1-3):33-40 (1996). A PRP extract from leukocytes inhibits HIV infection in MT-4 cell cultures.
PubMed Reference
PMID:8993755
Ferrer-Argote VE, Romero-Cabello R, Hernandez-Mendoza L, Arista-Viveros A, Rojo-Medina J, Balseca-Olivera F, Fierro M, Gonzalez-Constandse R. (1994) Successful treatment of severe complicated measles with non-specific transfer factor. In Vivo 8(4):555-7. 10 patients with severe complicated measles, a life-threatening illness, were treated with non-specific transfer factor. 8 of 9 patients experiencing respiratory failure recovered, while the single case of encephalitis was clear of neurologic sequelae within two weeks following the last dose.
PubMed Reference
PMID:7893983
Hughes RA. (1983) Immunological treatment of multiple sclerosis. Journal of Neurology 230(2):73-80. Transfer factor (PRP) slowed the progession of the disease whereas interferon and levamisole did not.
PubMed Reference
PMID:6196462
Iseki M, Aoyama T, Koizumi Y, Ojima T, Murase Y, Osano M. [Effects of transfer factor on chronic hepatitis B in childhood] Kansenshogaku Zasshi 63(12):1329-1332 (1989). Nine children with chronic hepatitis B received transfer factor (PRPs) for 3-17 months. Of these, 4 became hepatitis-B negative. After 22-48 months, 6 of the 9 were negative. No side effects were observed.
PubMed Reference
PMID:2621386
Janusz M, Lisowski J. (1993) Proline-rich polypeptide (PRP)--an immunomodulatory peptide from ovine colostrum. Archivum immunologiae et therapiae experimentalis (Warszava) 41(5-6):275-9. PRP increases the permeability of blood vessels in the skin and causes the differentiation of thymocytes into mature T cells.
PubMed Reference
PMID:8010865
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Janusz M, Staroscik K, Zimecki M, Wieczorek Z, Lisowski J. (1986)
A proline-rich polypeptide (PRP) with immunoregulatory properties isolated from ovine colostrum. Murine thymocytes have on their surface a receptor specific for PRP. Archivum immunologiae et therapiae experimentalis (Warszava) 34(4):427-36. PRP has immunoregulatory properties. It induces the maturation of thymocytes into mature helper or suppressor T cells.
PubMed Reference
PMID:
3026278
Julius MH, Janusz M, Lisowski J. (1988) A colostral protein that induces the growth and differentiation of resting B lymphocytes. Journal of Immunology 140(5):1366-71. PRP induced resting B cells and supported their progression through the cell cycle to form mature B cells. It had the same action on splenocytes.
PubMed Reference
PMID:3257974
Keech A. (2006) Unpublished data. In trials conducted in Nigeria and Kenya, a PRP spray was effective in restoring T cell levels to normal or near normal levels in AIDS patients. Concommitantly, the AIDS symptoms also were alleviated in nearly all patients.
Khan A. Non-specificity of transfer factor. Annals of Allergy 38(5):320-322 (1977).
PubMed Reference
PMID:855952
Kirkpatrick CH. (1993) Structural nature and functions of transfer factors. Annals of the New York Academy of Sciences. 685:362-8. Transfer factors (PRP) are molecules that "educate" target cells to express cell-mediated immunity. They cause the target cells to express delayed-type hypersensitivity to a given antigen (foreign protein) and produce cytokines which control the immune response.
PubMed Reference
PMID:8363241
Kruzel ML, Janusz M, Lisowski J, Fischleigh RV, Georgiades JA. (2001) Towards an understanding of biological role of colostrinin peptides. Journal of Molecular Neuroscience 17(3):379-89. PRP (colostrinin) is a potent inducer of leukocyte proliferation and of certain cytokines.
PubMed Reference
PMID:11859934
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Kubis A, Marcinkowska E, Janusz M, Lisowski J. (2005) Studies on the mechanism of action of a proline-rich polypeptide complex (PRP): effect on the stage of cell differentiation. Peptides 26(11):2188-92. PRP affects the differentiation and maturation of cells of the monocyte/ macrophage lineage and may regulate in this way the inflammatory processes in which these cells participate.
PubMed Reference
PMID:15904991
Leszek J, Inglot AD, Janusz M, Lisowski J, Krukowska K, Georgiades JA. (1999) Colostrinin: a Proline-Rich Polypeptide (PRP) Complex Isolated from Ovine Colostrum for Treatment of Alzheimer's Disease. A Double - Blind Placebo-Controlled Study. Archivum Immunologiae et Therapiae Experimentalis. 47(6):377-85. PRP, derived from colostrum, has shown promise in the treatment of Alzheimer's disease and other dementias, plus it is a very safe drug.
PubMed Reference
PMID:10608295
McMeeking A, Borkowsky W, Klesius PH, Bonk S, Holzman RS, Lawrence HS. (1990) A controlled trial of bovine dialyzable leukocyte extract for cryptosporidiosis in patients with AIDS. Journal of Infectious Diseases 161(1):108-112. A trial using bovine dialyzable leukocyte extract (PRPs) in AIDS patients suffering from cryptosporidial diarrhea was promising with 6 of 7 patients showing improvement or complete elimination of symptoms and oocytes.
PubMed Reference
PMID:
Meduri R, Campos E, Scorolli L, De Vinci C, Pizza G, Viza D. (1996) Efficacy of transfer factor in treating patients with recurrent ocular herpes infections. Biotherapy 9(1-3):61-6. Herpes-specific transfer factor (PRP) significantly increased the cell-mediated immune response to viral antigens in patients with recurrent ocular herpes infections, and significantly reduced relapses.
PubMed Reference
PMID:8993759 Nitsch A, Nitsch FP. (1998) Clinical Use of Bovine Colostrum. Journal of Orthomolecular Medicine 13(2). Low molecular weight components of colostrum (PRPs) were used in a clinical study for the treatment of rheumatoid arthritis with promising results.
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Orzechowska B, Janusz M, Domaraczenko B, Blach-Olszewska Z. (1998) Antiviral effect of proline-rich polypeptide in murine resident peritoneal cells. Acta Virologica 42(2):75-8. It is known that resident peritoneal (RP) cells from BALB/c female mice express a constitutive non-specific antiviral immunity which is progressively reduced during several days of cultivation in vitro. In this report, we have studied the effect of a proline-rich polypeptide (PRP) isolated from ovine colostrum on the kinetics of vesicular stomatitis virus (VSV) replication in freshly isolated and one-day cultured RP cells. The polypeptide was added to the cells immediately after virus adsorption or one day before or after viral infection. Independently on time of PRP addition, an inhibition of VSV replication (virus titres reduced by up to 4 log units) was observed.
PubMed Reference
PMID:9770073
Pizza G, Meduri R, De Vinci C, Scorolli L, Viza D. (1994) Transfer factor prevents relapses in herpes keratitis patients: a pilot study. Biotherapy 8(1):63-8. Use of HSV-specific transfer factor (PRP) reduced relapses in herpes ocular infections from 20.1 to 0.51.
PubMed Reference
PMID:7547082
Pizza, G, Chiodo, F, Colangeli, V, Gritti, F, Raise, E, Fudenberg, HH, De Vinci, C, Viza, D. Preliminary observations using HIV-specific transfer factor in AIDS. Biotherapy 9(1-3):4-47 (1996). 25 HIV infected patients at various stages (CDC stages II-IV) were treated with HIV-specific transfer factor (PRP) for periods of 60-1870 days. All patients were receiving antiviral treatment as well. Clinical improvement or a stabilized clinical condition was observed in 20 of the 25, and 12 of 14 anergic patients showed restored delayed hypersensitivity reactions to recall antigens within 60 days. Treatment was well-tolerated and appears beneficial to AIDS patients.
PubMed Reference
PMID:8993756
Pizza G, Viza D, De Vinci C, Palareti A, Cuzzocrea D, Fornarola V, Baricordi R. (1996) Orally administered HSV-specific transfer factor (TF) prevents genital or labial herpes relapses. Biotherapy 9(1-3):67-72. Patients with genital or labial herpes received HSV-specific transfer factor (PRP) over a course of 6 months. Controls experienced a relapse index (RI) of 61.2 while those in the experimental group had an RI of 21.4.
PubMed Reference
PMID:8993760
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Pizza G, Amadori M, Ablashi D, De Vinci C, Viza D. (2006) Cell mediated immunity to meet the avian influenza A (H5N1) challenge. Medical Hypotheses 67(3):601-8. As no vaccine can be made ahead of time for a possible bird flu pandemic, cell mediated immunity via specific transfer factor (PRP) may be useful for both the prevention and treatment of infection.
PubMed Reference
PMID:16603322
Raise E, Guerra L, Viza D, Pizza G, De Vinci C, Schiattone ML, Rocaccio L, Cicognani M, Gritti F. (1996) Preliminary results in HIV-1-infected patients treated with transfer factor (TF) and zidovudine (ZDV). Biotherapy 9(1-3):49-54. HIV-1 specific transfer factor (an alternative name for PRP) plus zidovudine (ZDV) was tested for efficacy in patients with AIDS-related complex (ARC). Patients receiving both transfer factor and ZDV experienced an increase in white blood cells, CD8+ lymphocytes and IL-2 levels over those receiving ZDV alone.
PubMed Reference
PMID:8993757
Rona ZP. (1998) Bovine Colostrum Emerges as Immunity Modulator. American Journal of Natural Medicine March, 1998.
ABSTRACT: PRP from colostrum can work as a regulatory substance of the thymus gland. It has been demonstrated to improve or eliminate symptomology of both allergies and autoimmune diseases (MS, rheumatoid arthritis, lupus, and myasthenia gravis). PRP inhibits the overproduction of lymphocytes and T-cells and reduces the major symptoms of allergies and autoimmune disease: pain, swelling, and inflammation.
Staroscik K, Janusz M, Zimecki M, Wieczorek Z, Lisowski J. (1983) Immunologically active nonapeptide fragment of a proline-rich polypeptide from ovine colostrum: amino acid sequence and immuno-regulatory properties. Molecular Immunology 20(12):1277-82. Small peptide chains in colostrum called proline-rich polypeptides (PRP) have the same ability to regulate the activity of the immune system as the hormones of the thymus gland. PRP activates an underactive immune system, helping it move into action against disease-causing organisms. PRP also suppresses an overactive immune system such as is often seen in the autoimmune diseases. PRP is highly anti-inflammatory and also appears to act on T-cell precursors to produce helper T-cells and suppressor T-cells.
PubMed Reference
PMID:6656774
Wieczorek Z, Zimecki M, Janusz M, Staroscik K, Lisowski J. (1979) Proline-rich polypeptide from ovine colostrum: its effect on skin permeability and on the immune system. Immunology. 36(4):879-81. PRP has a regulatory activity stimulating the immune response.
PubMed Reference
PMID:437850
Wieczorek Z, Zimecki M, Spiegel K, Lisowski J, Janusz M. (1989) Differentiation of T cells into helper cells from immature precursors: identification of a target cell for a proline-rich polypeptide (PRP). Archivum immunologiae et therapiae experimentalis (Warszava) 37(3-4):313-322. The precursors of helper T cells belong to a minor thymocyte subset bearing the Thy-1 +/-, H-2+, L3T4-, lyt 2-, CD3- phenotype. PRP induced the production of antigens consistent with mature helper T cells.
PubMed Reference
PMID:2534785
Zablocka A, Janusz M, Rybka K, Wirkus-Romanowska I, Kupryszewski G, Lisowski J. (2001) Cytokine-inducing activity of a proline-rich polypeptide complex (PRP) from ovine colostrum and its active nonapeptide fragment analogs. European Cytokine Network 12(3):462-467. PRP induces the production of INF-γ, TNF-α, IL-6 and IL-10 in human whole blood cultures.
PubMed Reference
PMID:11566627
Zimecki M, Staroscik K, Janusz M, Lisowski J, Wieczorek Z. (1983) The inhibitory activity of a proline-rich polypeptide (PRP) on the immune response to polyvinylpyrrolidone (PVP). Archivum immunologiae et therapiae experimentalis (Warszava) 31(6):895-903. PRP administered to a test animal before immunization with PVP inhibits the immune response to this antigen. PRP did this by increasing the activity of suppressor T cells and by increasing the generation of new suppressor T cells.
PubMed Reference
PMID:6234865
Zimecki M, Lisowski J, Hraba T, Wieczorek Z, Janusz M, Staroscik K. (1984) The effect of a proline-rich polypeptide (PRP) on the humoral immune response. I. Distinct effect of PRP on the T cell properties of mouse glass-nonadherent (NAT) and glass-adherent (GAT) thymocytes in thymectomized mice. Archivum immunologiae et therapiae experimentalis (Warszava) 32(2):191-196. Glass-nonadherent thymocytes are a precursor of helper T cells, and glass-adherent thymocytes are a precursor of suppressor T cells. PRP causes each of these cell types to develop into their lymphocyte types.
PubMed Reference
PMID:6333228
Zimecki M, Lisowski J, Hraba T, Wieczorek Z, Janusz M, Staroscik K. (1984) The effect of a proline-rich polypeptide (PRP) on the humoral immune response. II. PRP induces differentiation of helper cells from glass-nonadherent thymocytes (NAT) and suppressor cells from glass-adherent thymocytes (GAT). Archivum immunologiae et therapiae experimentalis (Warszava) 32(2):197-201. PRP induces differentiation of both helper and suppressor T cells.
PubMed Reference
PMID:6237628
Zimecki M, Pierce CW, Janusz M, Wieczorek Z, Lisowski J. (1987) Proliferative response of T lymphocytes to a proline-rich polypeptide (PRP): PRP mimics mitogenic activity of Il-1. Archivum immunologiae et therapiae experimentalis (Warszava) 35(3):339-349. PRP had the same mitogenic effect on T cells as interleukin-1, inducing proliferation of non-antigen specific T cells.
PubMed Reference
PMID:3502239
Zimecki M, Hraba T, Janusz M, Lisowski J, Wieczorek Z. (1991) Effect of a proline-rich polypeptide (PRP) on the development of hemolytic anemia and survival of New Zealand black (NZB) mice. Archivum immunologiae et therapiae experimentalis (Warszava) 39(5-6):461-467. When PRP was given to New Zealand Black mice showing signs of hemolytic anemia, it significantly lowered the incidence of positive Coombs' reaction and prolonged the mean age of the mice. Hemolytic anemia is an autoimmune disease in these mice, indicating that PRP may have therapeutic value in the treatment of autoimmune disorders in humans.
PubMed Reference
PMID:1841543
Zimecki M. (2008) A proline-rich polypeptide from ovine colostrum: colostrinin with immunomodulatory activity. Advances in Experimental and Medical Biology 606:241-250. PRP are immunomodulatory peptides from colostrum that promote T cell maturation from early thymic precursors into mature helper cells or mature suppressor cells. They suppressed autoimmune hemolytic anemia in New Zealand black mice. PRP modulate cytokine production in blood. PRP has also been shown to be effective in the treatment of Alzheimer's disease by delaying the progress of the disease.
PubMed Reference
PMID:18183932
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Lactoferrin
Abe H, Saito H, Miyakawa H, Tamura Y, Shimamura S, Nagao E, Tomita M. (1991) Heat stability of bovine lactoferrin at acidic pH. Journal of Dairy Science. 74:65-71. Pasteurizing lactoferrin at pH 4.0 preserves its activity.
Andersen JH, Jenssen H, Gutteberg TJ. (2003) Lactoferrin and lactoferricin inhibit Herpes simplex 1 and 2 infection and exhibit synergy when combined with acyclovir. Antiviral Research 58(3):209-215. When used against HSV-1 and -2, the combination of lactoferrin or its peptide lactoferricin with acyclovir demonstrated good synergy. The effective dosage of both lactoferrin and acyclovir could be reduced 2-7 times.
PubMed Reference
PMID:12767468
Andersson Y, Lindquist S, Lagerqvist C, Hernell O. (2000) Lactoferrin is responsible for the fungistatic effect of human milk. Early Human Development 59:95-105. Lactoferrin, through its iron-binding ability, is very effective against fungal infections with Candida and other fungi.
PubMed Reference
PMID:10996747
Appelmelk BJ, An YQ, Geerts M, Thijs BG, de Boer HA, MacLaren DM, de Graaff J, Nuijens JH. (1994) Lactoferrin is a lipid A-binding protein. Infection and Immunity. 62:2628-32. Lactoferrin binds to lipopolysaccharides (LPS) secreted as endotoxin by pathogenic bacteria such as E. coli, Klebsiella pneumoniae, Pseudomonas aeruginosa, Neisseria meningitides,and Haemophilus influenzae, all dangerous pathogens. It also binds to lipid A, a component of LPS. This appears to be one of the ways in which lactoferrin expresses its antibacterial and anti-endotoxic effects.
PubMed Reference
PMID: 94245381
Arnold D, Di Biase AM, Marchetti M, Pietrantoni A, Valenti P, Seganti L, Superti F. (2002) Antiadenovirus activity of milk proteins: lactoferrin prevents viral infection. Antiviral Research 53(2):153-158. Lactoferrin prevented viral infection by adenovirus when added before or during the viral adsorption stage.
PubMed Reference
PMID:11750941
Artym J. (2006) [Antitumor and chemopreventive activity of lactoferrin] Postepy Higieny i Medycyny Doświadczalnej 60:352-369. Lactoferrin participates in iron homeostasis, has immunoregulatory, anti-inflammatory, anti-tumor, and analgesic actions, regulation of bone metabolism, participates in embryonic development, reproductive functions, and others. It provides anti-tumor protection through its immunomodulatory abilities, so it is of particular value in cancer patients with impaired immunity. Lactoferrin increases the number and the activity of T and B cells and NK cells, stimulates the release of a number of cytokines (IL-1, IL-6, IL-8, IL-18, IFN-γ, TNF-α), increases the phagocytic and cytotoxic activity of monocytes and macrophages, accelerates the maturation of T and B cells, and elevates the expression of several types of cellular receptors, including CD4, zeta chain of the CD3 complex, LFA-1, CD11, ICAM-1, and selectin P. In addition, it also exhibits chemopreventive properties, regulates the activity of Phase I and Phase II enzymes which participate in the activation and detoxification of carcinogens, and regulates the composition of the intestinal flora.
PubMed Reference
PMID:16885906
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Baker EN, Anderson BF, Baker HM, Day CL, Haridas M, Norris GE, Rumball SV, Smith CA, Thomas DH. (1994) Three-dimensional structure of lactoferrin in various functional states. Lactoferrin: Structure and Function. 1-12. The three dimensional structure of lactoferrin is important in its function.
PubMed Reference
PMID:7762421
Baveye S, Elass E, Mazurier J, Spik G, Legrand D. (1999) Lactoferrin: a multifunctional glycoprotein involved in the modulation of the inflammatory process. Clinical Chemistry and Laboratory Medicine 37(3):281-286. Lactoferrin modulates the inflammatory process mainly by preventing the release of cytokines from monocytes and by regulating the proliferation and differentiation of immune cells. It is also prophylactic against septicemia. Lactoferrin is one of the key molecules which modulate the inflammatory response.
PubMed Reference
PMID:10353473
Bellamy W, Takase M, Yamauchi K, Wakabayashi H, Kawase K, Tomita M. (1992) Identification of the bactericidal domain of lactoferrin. Biochemica et Biophysica Acta 1121(1-2):130-6. A domain near the N-terminus of lactoferrin appears to be responsible for the bactericidal activity of lactoferrin.
PubMed Reference
PMID:1599934
Beaumont SL, Maggs DJ, Clarke HE. (2003) Effects of bovine lactoferrin on in vitro replication of feline herpes virus. Veterinary Ophthalmology 6(3):245-50. Bovine lactoferrin has a notable inhibitory effect on the in vitro replication of feline herpes virus prior to and during viral adsorption, but not after. It appears that the lactoferrin blocks adsorption to the cell surface and/or penetration of the virus into the cell.
PubMed Reference
PMID:12950656
Britigan BE, Lewis TS, Waldschmidt M, McCormick ML, Krieg AM. (2001) Lactoferrin binds CpG-containing oligonucleotides and inhibits their immunostimulatory effects on human B cells. Journal of Immunology 167(5):2921-28. Unmethylated CpG dinucleotide motifs in bacterial DNA, as well as oligodeoxynucleotides (ODN) containing these motifs, are potent stimuli for many host immunological responses. These CpG motifs may enhance host responses to bacterial infection and are being examined as immune activators for therapeutic applications in cancer, allergy/asthma, and infectious diseases. Lactoferrin and lactoferricin B, but not transferrin, inhibited CpG ODN stimulation of CD86 expression in the human Ramos B cell line and decreased cellular uptake of ODN, a process required for CpG bioactivity. Lactoferrin binding of CpG-containing ODN may serve to modulate and terminate host response to these potent immunostimulatory molecules at mucosal surfaces and sites of bacterial infection.
PubMed Reference
PMID:11509640
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Buchta R. (1991) Ovine lactoferrin: Isolation from colostrum and characterization. Journal of Dairy Research 58(2):211-8. Lactoferrin was isolated from sheep colostrum and was found to have 80% homology with human lactoferrin.
PubMed Reference
PMID:1856354
Drobni P, Naslund J, Evander M. (2004) Lactoferrin inhibits human papilloma virus binding and uptake in vitro. Antiviral Research 64(1):63-68. Lactoferrin, particularly bovine lactoferrin, blocks entry of human papilloma virus (HPV) into target cells in vitro. HPV has been implicated in the development of cervical and other cancers.
PubMed Reference
PMID:15451180
Elrod, KC, Moore WR, Abraham WM, Tanaka RD. (1997) Lactoferrin, a potent tryptase inhibitor, abolishes late-phase airway responses in allergic sheep. American Journal of Respiratory Critical Care Medicine 156(2 Pt 1):375-381 (1997). Lactoferrin released from neutrophil granules inhibits tryptase, which is involved in late-phase bronchoconstriction and airway hyperactivity in asthma.
PubMed Reference
PMID:9279212
Gahr M, Speer CP, Damerau B, Sawatzki G. (1991) Influence of lactoferrin on the function of human polymorphonuclear leukocytes and monocytes. Journal of Leukocyte Biology 49(5):427-433 (1991). White blood cells (polymorphonuclear leucocytes) exposed to lactoferrin from bovine colostrum exhibit increased motility and produce more superoxide (a powerful antioxidant).
PubMed Reference
PMID:1849951
Gutteridge J, Paterson S, Segal A, Halliwell B. (1981) Inhibition of lipid peroxidation by the iron-binding protein lactoferrin. Biochem. Journal 199(1):259-61. Lactoferrin is an inhibitor of lipid peroxidation induced by iron and ascorbic acid. Therefore lactoferrin as an antioxidant may help to protect neutrophils, inflammatory foci and secretions from metal-ion-dependent oxidative damage.
PubMed Reference
PMID:7337708
Hara K, Ikeda M, Saito S, Matsumoto S, Numata K, Kato N, Tanaka K, Sekihara H. (2002) Lactoferrin inhibits hepatitis B virus infection in cultured human hepatocytes. Hepatology Research 24(3):228. Bovine lactoferrin prevents infection of cultured human liver cells with hepatitis B virus, while transferrin, casein and lactalbumin had no effect.
PubMed Reference
PMID:12393024
Haridas M, Anderson BF, Baker HM, Norris GE, Baker EN. (1994) X-ray structure analysis of bovine lactoferrin at 2.5 Ångstrom resolution. Lactoferrin: Structure and Function pp 235-38. High resolution X-ray crystallography revealed the two dimensional structure of lactoferrin.
PubMed Reference
PMID:7762437
Harmsen MC, Swart PJ, de Bethune 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. Journal of Infectious Diseases. 172(2):380-8. Lactoferrin from bovine or human milk and colostrum completely blocks Human Cytomegalus Virus (CMV) infection and inhibited HIV-1-induced cytopathic effect. It appears to exert its effect at the level of virus adsorption and penetration (or both).
PubMed Reference
PMID:7622881
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Hasegawa K, Motsuchi W, Tanaka S, Dosako S. (1994) Inhibition with lactoferrin of in vitro infection with human herpes virus. Japanese Journal of Medical Science and Biology 47(2):73-85. Both human and bovine lactoferrin inhibited human herpes simplex virus-1 in vitro.
PubMed Reference
PMID:7853749
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Hashizume S, Kuroda K, Murakami H. (1983) Identification of lactoferrin as an essential growth factor for human lymphocytic cell lines in serum-free medium. Biochimica et Biophysica Acta 763(4):377-382 (1983). Lactoferrin is an essential growth factor for lymphocytes. It has higher growth stimulatory activity than transferrin. Bovine lactoferrin was found to be as effective as human.
PubMed Reference
PMID:6652116
Hayashida K, Takeuchi T, Ozaki T, Shimizu H, Ando K, Miyamoto A, Harada E. (2004) Bovine lactoferrin has a nitric oxide-dependent hypotensive effect in rats. American Journal of Physiology – Regulatory, Integrative and Comparative Physiology 286(2):R359-65. Bovine lactoferrin has a hypotensive effect via an endothelium- dependent vasodilation that is strongly mediated by NO production.
PubMed Reference
PMID:14563657
Hayashida K, Kaneko T, Takeuchi T, Shimizu H, Ando K, Harada E. (2004) Oral administration of lactoferrin inhibits inflammation and nociception in rat adjuvant-induced arthritis. Journal of Veterinary Medical Science 66(2):149-54. Lactoferrin is an immunomodulator and has also been found to produce micro-opioid receptor-mediated analgesia. In an rat experimental arthritis model, bovine lactoferrin suppressed the development of the arthritis and lessened the pain (as determined by hyperalgesia of the infected paw). Lactoferrin also suppressed TNF-alpha (pro-inflammatory) production and increased IL-10 (anti-inflammatory) production. Thus lactoferrin has both preventive and therapeutic effects on both the inflammation and pain associated with arthritis.
PubMed Reference
PMID:15031542
Iigo M, Kuhara T, Ushida Y, Sekine K, Moore MA, Tsuda H. (1999) Inhibitory effects of bovine lactoferrin on colon carcinoma 26 lung metastasis in mice. Clinical and Experimental Metastasis. 17(1):35-40. Bovine lactoferrin exhibited significant inhibition of lung metastatic colony formation from implanted tumors in mice. AsialoGM+1 and CD8+ cell levels increased after treatment with the lactoferrin, suggesting they play a role in tumor inhibition.
PubMed Reference
PMID:10390145
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Ikeda M, Sugiyama K, Tanaka T, Tanaka K, Sekihara H, Shimotohno K, Kato N. (1998) Lactoferrin markedly inhibits hepatitis C virus infection in cultured human hepatocytes. Biochemical and biophysical research communications 245(2):549-53. Bovine lactoferrin effectively prevented infection with Hepatitis C virus in cultured human hepatocytes (liver cells), which are very susceptible to infection with the virus. Lactoferrin may prove to be very effective in the treatment of patients with chronic hepatitis, and it is very well tolerated.
PubMed Reference
PMID:9571193
Jenssen H, Andersen JH, Uhlin-Hansen L, Gutteberg TJ, Rekdal O. (2004) Anti-HSV activity of lactoferricin analogues is only partly related to their affinity for heparan sulfate. Antiviral Research 61(2):101-109. It has been shown that bovine lactoferricin (a biologically active peptide derived from lactoferrin) blocks herpes simplex virus (HSV) binding by competing for receptor (heparin sulfate) sites on target cells. However, this is apparently not the only mechanism that accounts for the anti-HSV activity of lactoferricin. Hydrophobicity, molecular size, spatial distribution of charged and lipophilic amino acids, and the ring structure of lactoferricin also seem to be important factors.
PubMed Reference
PMID:14670583
Jenssen H. (2005) Anti-herpes simplex virus activity of lactoferrin/lactoferricin – an example of antiviral activity of antimicrobial protein/peptide. Cellular and Molecular Life Sciences 62(24):3002-3013. Lactoferrin and a peptide derived from lactoferrin, lactoferricin, block entry of HSV into cells.
PubMed Reference
PMID:16261265
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Kawakami H. (1988) Effects of iron-saturated Lactoferrin on iron absorption. Agricultural and Biological Chemistry 52(4):903-8. Iron absorption was studied in iron-deficient anemic rats. Rats fed iron-saturated lactoferrin showed statistically significant increases in red blood cell density, hematocrit and hemoglobin values compared to rats receiving ferrous sulfate. This suggests that iron from iron-saturated lactoferrin is absorbed across the intestinal mucosa by a mechanism other than that used by soluble ferrous sulfate.
Kawasaki Y, Isoda H, Shinmoto H, Tanimoto M, Dosako S, Idota T, Nakajima I. (1993) Inhibition by kappa-casein glycomacropeptide and lactoferrin of influenza virus hemagglutination. Bioscience, Biotechnology, and Biochemistry 57(7):1214-1215. Lactoferrin inhibits the hemagglutination (clumping of blood cells) of the influenza virus. Hemagglutination inhibition is one of the tests which show the effectiveness of influenza vaccines.
PubMed Reference
PMID:7763995
Kruzel M, Bacsi A, Choudhury B, Sur S, Boldogh I. (2006) Lactoferrin decreases pollen antigen-induced allergic airway inflammation in a murine model of asthma. Immunology 119(2):159-66. Pollen grains contain reduced nicotinamide adenine dinucleotide phosphate (NADPH) oxidases and in contact with mucosal surfaces generate superoxide anion (O2*-). In the presence of iron, O2*- may be converted to more reactive oxygen radicals, such as to H2O2 and/or *OH, which may augment antigen-induced airway inflammation. LF lowered the increase in cellular reactive oxygen species (ROS) levels in bronchial epithelial cells. The results suggest the utility of LF in human allergic inflammatory disorders.
PubMed Reference
PMID:16800860
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Kuhara T, Yamauchi K, Tamura Y, Okamura H. (2006) Oral administration of lactoferrin increases NK cell activity in mice via increased production of IL-18 and type I IFN in the small intestine. Journal of Interferon and Cytokine Research 26(7):489-499 (2006). Orally administered bovine lactoferrin increases NK cell populations in blood and spleen and enhances interferon-gamma production. It also increases the production of IL-18 and increases the production of interferon-alpha and interferon-beta in the Peyer's Patches in the intestines and mesenteric lymph nodes.
PubMed Reference
PMID:16800788
Kussendrager KD. (2003) Effects of heat treatment on structure and iron-binding capacity of bovine lactoferrin. Indigenous Antimicrobial Agents of Milk - Recent Developments, International Dairy Foundation pp 133-46. As heat treatment of lactoferrin derived from milk and colostrum may impair its bioactive state and functionality, it is necessary to determine the optimum conditions of pH, salts and whey protein to achieve optimal conditions for pasteurization.
Kwiat G. (1998) Lactoferrin. NutriCology in Focus pp 1-13. Lactoferrin influences many disease processes from cancer to immune deficiency in addition to its normal bodily functions such as the transport of iron.
Levay PF, Viljoen M. (1980) Lactoferrin: A general review. Haematologica 3:252-267. Receptors for lactoferrin can be found on intestinal tissue, monocytes and macrophages, neutrophils, lymphocytes, platelets, and on certain bacteria.
PubMed Reference
PMID:7672721
Li YM, Tan A, Vlassara T, Vlassara H. (1995) Antibacterial activity of lysozyme and lactoferrin is inhibited by binding of advanced glycation-modified proteins to a conserved motif. Nature Medicine. 1(10):1057-61. Diabetes is associated with abnormally high sensitivity to infection. Lysozyme and lactoferrin, two major antibacterial antibodies found in colostrum and milk, specifically bind glucose-modified proteins with advanced glycation end-products (AGE). AGE is elevated in tissues and serum of diabetic patients which may inhibit antibacterial proteins by binding to them, thus increasing susceptibility to infection.
PubMed Reference
PMID:7489363
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Lonnerdal B, Iyer S. (1995) Lactoferrin: molecular structure and biological function. Annual Review of Nutrition 15:93-110. Lactoferrin functions are tied to both its iron-binding capability as well as other functions, such as a growth factor and bactericidal agent.
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PMID:8527233
Marchetti M, Pisani S, Antonini G, Valenti P, Seganti L, Orsi N. (1998) Metal complexes of bovine lactoferrin inhibit in vitro replication of herpes simplex virus type 1 and 2. Biometals 11(2):89-94. Bovine lactoferrin saturated with iron, manganese or zinc proved strongly inhibitory to viral replication of herpes simplex virus types 1 and 2 in cell cultures (Vero).
PubMed Reference
PMID:9542061
Marchetti M, Superti F, Ammendolia MG, Rossi P, Valenti P, Seganti L. (1999) Inhibition of poliovirus type 1 infection by iron-, manganese- and zinc-saturated lactoferrin. Medical Microbiology and Immunology 187(4):199-204. The actions of human and bovine lactoferrin on the infection of Vero cell cultures by poliovirus type 1 were compared to other milk proteins, including mucin, alpha-lactalbumin and beta-lactoglobulin. Only the lactoferrins were able to inhibit infection by blocking attachment to the cells. Only lactoferrin combined with zinc was able to inhibit infection after the stage of attachment.
PubMed Reference
PMID:10363676
McCann KB, Lee A, Wan J, Roginski H, Coventry MJ. (2003) The effect of bovine lactoferrin and lactoferricin B on the ability of feline calicivirus (a norovirus surrogate) and poliovirus to infect cell cultures. Journal of Applied Microbiology 95(5):1026-1033. Lactoferrin interfered with the infection of cells by both feline calicivirus and poliovirus.
PubMed Reference
PMID:14633031
Mikogami T, Marianne T, Spik G. (1995) Effect of intracellular iron depletion by picolinic acid on expression of the lactoferrin receptor in the human colon carcinoma cell subclone HT29-18-C1. Biochemistry Journal. 308:391-7. Picolinic acid, an iron chelator, was used to deplete intracellular iron in a cell culture. This was followed by an increase in the synthesis of lactoferrin receptors in the cells, resulting in a 30% increase in iron uptake by the cells.
PubMed Reference
PMID:7772018
Murphy ME, Kariwa H, Mizutani T, Tanabe H, Yoshimatsu K, Arikawa J, Takashima I. (2001) Characterization of in vitro and in vivo antiviral activity of lactoferrin and ribavirin upon hanta virus. Journal of Veterinary Medicine and Science 63(6):637-45. Lactoferrin alone or ribavirin alone significantly inhibited hantavirus focus formation in vitro. When combined, the two completely inhibited focus formation. Lactoferrin inhibits adsorption of the virus to cells, and ribavirin inhibits viral protein synthesis.
PubMed Reference
PMID:11459009
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Ng TB, Lam TL, Au TK, Ye XY, Wan CC. (2001) Inhibition of human immunodeficiency virus type 1 reverse transcriptase, protease and integrase by bovine milk proteins. Life Science 69(19):2217-23. Lactoferrin strongly inhibits HIV-1 reverse transcriptase and slightly inhibited HIV-1 protease and integrase, enzymes which are crucial to the HIV-1 life cycle.
PubMed Reference
PMID:11669464
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. Journal of Biological Chemistry 278(12):10162-73. Both human and bovine lactoferrin prevent hepatitis C infection in vitro. A peptide in the lactoferrin molecule has been shown to a viral envelope protein, by which it apparently blocks the viral particles from binding to target cells.
PubMed Reference
PMID:12522210
Ohashi A, Murata E, Yamamoto K, Majima E, Sano E, Le QT, Katunuma N. (2003) New functions of lactoferrin and beta-casein in mammalian milk as cysteine protease inhibitors. Biochemistry and Biophysics Research Communications 306(1):98-103. Lactoferrin inhibits cathepsin L (a cysteine protease inhibitor), an activity which is dependent on the tertiary structure of lactoferrin. A peptide of lactoferrin shows 90% homology with the sequences of a common active site of cystatins.
PubMed Reference
PMID:12788072
Petschow B, Talbott R, Batema R. (1999) Ability of lactoferrin to promote the growth of Bifidobacterium spp. in vitro is independent of receptor binding capacity and iron saturation level. Journal of Microbiology. 48:541-9. Lactoferrin promotes the growth of beneficial bacteria, such as bifidobacteria, while inhibiting the growth of pathogenic bacteria. This study showed that the promotion of growth of bifidobacteria by lactoferrin is not correlated to the iron saturation level of the lactoferrin, and binding of lactoferrin to bifidobacteria, while it may occur, is not sufficient for stimulation of bifidobacterial growth.
PubMed Reference
PMID:10359303
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Pietrantoni A, Di Biase AM, Tinari A, Marchetti M, Valenti P, Seganti L, Superti F. (2003) Bovine lactoferrin inhibits adenovirus infection by interacting with viral structural polypeptides. Antimicrobial Agents and Chemotherapy 47(8):2688-91. In addition to competeing for common receptors on target cells, lactoferrin also neutralizes infection by adenovirus by binding to adenovirus particles, specifically viral III and IIIa polypeptides.
PubMed Reference
PMID:12878543
Pietrantoni A, Ammendolia MG, Tinari A, Siciliano R, Valenti P, Superti F. (2006) Bovine lactoferrin peptidic fragments involved in inhibition of Echovirus 6 in vitro infection. Antiviral Research 69(2):98-106. Lactoferrin inhibits Echovirus 6 infection by blocking viral attachment to cell receptors, possibly due to the cluster of positive charges at its N-terminus.
PubMed Reference
PMID:16386316
Polla B. (1999) Therapy by taking away: The case of iron. Biochemical Pharmacology. 57:1345-9. Iron deprivation has been shown to have a beneficial effect on muscle necrosis in an animal model of genetic myopathy. It is proposed that taking away of iron, such as with lactoferrin, may also have a beneficial effect on other diseases with a free radical component, and may also have an antioxidant effect that could be important in anti-aging.
PubMed Reference
PMID:10353254
Qiu J, Hendrixson DR, Baker EN, Murphy TF, St Geme JW III, Plaut AG. (1998) Human milk lactoferrin inactivates two putative colonization factors expressed by Haemophilus influenzae. Proceedings of the National Academy of Sciences USA 95:12641-12646. Lactoferrin prevents colonization of Haemophilus influenzae, the primary cause of otitis media and other respiratory infections in children, by inactivating two colonization factors expressed by the bacteria.
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Saito H, Miyakawa H, Tamura Y, Shimamura S, Tomita M. (1991) Potent bactericidal activity of bovine lactoferrin hydrolysate produced by heat treatment at acidic pH. Journal of Dairy Science 74(11):3724-30. Heat treatment at acidic pH produces a fragment of lactoferrin with antibacterial properties at only 10µg/ml. This indicates that antibacterial domains of lactoferrin have no relation to iron saturation.
PubMed Reference
PMID:1757616
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Seganti L, Di Biase AM, Marchetti M, Pietrantoni A, Tinari A, Superti F. (2004) Antiviral activity of lactoferrin towards naked viruses. Biometals 17(3):295-299. Lactoferrin is a well-known potent inhibitor of naked viruses, including rotavirus, enterovirus, and adenovirus. Lactoferrin is especially potent against viruses which replicate in the gastrointestinal system as it is resistant to tryptic digestion. Against rotavirus, it prevents viral attachment to the gastrointestinal wall by binding to viral particles, and it inhibits a post adsorption step. Lactoferrin interferes with an early infection step of the polio virus, and iron-saturated lactoferrin inhibits viral replication after the adsorption phase.
PubMed Reference
PMID:15222481
Shau H, Kim A, Golub SH. (1992) Modulation of natural killer and lymphokine-activated killer cell cytotoxicity by lactoferrin. Journal of Leukocyte Biology 51(4):343-349. Lactoferrin strongly augments the cytotoxic functions of natural killer (NK) cells and lymphokine-activated killer (LK) cells. Newborn infants have low NK and LK activity so lactoferrin may ‘turn on’ these cells in the infant.
PubMed Reference
PMID:1564398
Shimizu K, Matsuzawa H, Okada K, Tazume S, Dosako S, Kawasaki Y, Hashimoto K, Koga Y. (1996) Lactoferrin-mediated protection of the host from murine cytomegalovirus infection by a T-cell-dependent augmentation of natural killer cell activity. Archives of Virology 141(10):1875-1889. Lactoferrin protected mice from cytomegalovirus infection. The mechanism of action was apparently through the stimulation of NK cell activity, as athymic nude mice showed no increase in NK cell activity and no protection against cytomegalovirus infection.
PubMed Reference
PMID:8920822
Shin K, Yamauchi K, Teraguchi S, Hayasawa H, Tomita M, Otsuka Y, Yamazaki S. (1998) Antibacterial activity of bovine lactoferrin and its peptides against enterohaemorrhagic E. coli O157:H7. Letters in Applied Microbiology. 26(6):407-11. E. coli O157:H7, a form of E. coli that causes gastrointestinal bleeding, is susceptible to the antibacterial effects of lactoferrin and its peptides.
PubMed Reference
PMID:98383038
Shin K, Wakabayashi H, Yamauchi K, Teraguchi S, Tamura Y, Kurokawa M, Shiraki K. (2005) Effects of orally administered bovine lactoferrin and lactoperoxidase on influenza virus infection in mice. Journal of Medical Microbiology 54(Pt8):717-723. Mice infected with influenza virus were given either lactoferrin (LF) or lactoperoxidase (LPO) by mouth. While neither eliminated the virus, both caused a significantly lower lung consolidation score on day 6 (compared to control), significantly lower numbers of infiltrated leukocytes from bronchoalveolar lavage, and significantly lower levels of IL-6, a pro-inflammatory cytokine, indicating that both LF and LPO were effective in treating the pneumonia associated with the influenza.
PubMed Reference
PMID:16014423
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Superti F, Ammendolia MG, Valenti P, Seganti L. (1997) Antirotaviral activity of milk proteins: lactoferrin prevents rotavirus infection in the enterocyte-like cell line HT-29. Medical Microbiology and Immunology (Berlin) 186(2-3):83-91 . Beta-lactoglobulin, apo- and iron-saturated lactoferrin inhibit rotaviral infection in a dose-dependent manner. Apo-lactoferrin prevents both rotavirus hemagglutination and viral binding to susceptible cells. It also markedly inhibits rotavirus antigen synthesis when added during the virus adsorption step.
PubMed Reference
PMID:9403835
Tanaka T, Nakatani S, Xuan X, Kumura H, Igarashi I, Shimazaki K. (2003) Antiviral activity of lactoferrin against canine herpes virus. Antiviral Research 60(3):193-9. Bovine lactoferrin inhibits both the infection and replication of canine herpes virus in vitro.
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Thaler C, Labarrere C, Hunt J, Mcintyre J, Faulk P. (1999) Unique epitopes of lactoferrin expressed in human cytotrophoblasts involved in immunologic reactions. American Journal of Obstetrics and Gynecology 181(2):460-7. Cytotrophoblasts of the placenta expressed a unique form of lactoferrin in the presence of activated macrophages. This may be a response to inflammation and maternal allogenic recognition.
PubMed Reference
PMID:10454701
Tinari A, Pietrantoni A, Ammendolia MG, Valenti P, Superti F. (2005) Inhibitory activity of bovine lactoferrin against echovirus induced programmed cell death in vitro. International Journal of Antimicrobial Agents 25(5):433-8. Cells infected with echovirus 6 die as a result of apoptosis (programmed cell death). Lactoferrin inhibits this effect.
PubMed Reference
PMID:15848300
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Valenti P, Marchetti M, Superti F, Amendolia MG, Puddu P, Gessani S, Borghi P, Belardelli F, Antonini G, Seganti L. (1998) Antiviral activity of lactoferrin. Advances in Experimental and Medical Biology 443:199-203.
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van der Strate BW, Beljaars L, Molema G, Harmsen MC, Meijer DK. (2001) Antiviral activities of lactoferrin. Antiviral Research 52(3):225-39. Lactoferrin has antiviral activity against both DNA and RNA viruses, including respiratory syncytial virus, herpes virus, rotavirus and HIV. Its mechanism of action is mainly to block entry of the virus into target cells, either by blocking receptors on target cells or directly binding to virus particles.
PubMed Reference
PMID:11675140
van der Strate BW, De Boer FM, Bakker HI, Meijer DK, Molema G, Harmsen MC. (2003) Synergy of bovine lactoferrin with the anti-cytomegalovirus drug cidofovir in vitro. Antiviral Research 58(2):159-65. Combining lactoferrin with acyclovir or foscarnet resulted in antagonism, lactoferrin and ganciclovir showed neither antagonism or synergy, but lactoferrin with cidofovir showed marked synergy against cytomegalovirus.
PubMed Reference
PMID:12742576
Viani RM, Gutteberg TJ, Lathey JL, Spector SA. (1999) Lactoferrin inhibits HIV-1 replication in vitro and exhibits synergy when combined with zidovudine. AIDS 13(10):1273-4. Lactoferrin in combination with zidovudine is more effective than either alone in inhibiting HIV-1 replication.
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PMID:10416533
Vorland L, Ulvatne H, Andersen J, Haukland HH, Rekdal O, Svendsen JS, Gutteberg TJ. (1999) Antibacterial effects of lactoferricin B. Scandinavian Journal of Infected Disease 31:179-84. Lactoferricin is produced by cleaving the lactoferrin protein. Lactoferricin was found to maximum effect against bacteria when it did not have to act through a cell wall.
PubMed Reference
PMID: 99374995
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Waarts BL, Aneke OJ, Smit JM, Kimata K, Bittman R, Meijer DK, Wilschut J.(2005) Antiviral activity of human lactoferrin: inhibition of alpha virus interaction with heparan sulfate. Virology 333(2):284-292. Lactoferrin inhibits viral infection by alphaviruses (Sindbis and Semliki Forest) by interfering with virus-receptor interaction.
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PMID:15721362
Ward PP, Uribe-Luna S, Conneely OM. (2002) Lactoferrin and host defense. Biochemistry and Cell Biology 80(1):95-102. Lactoferrin is a prominent component of the first line of defense against infection and inflammation. It accomplishes its activity through a variety of methods, most notably iron sequestration and its effect on down-regulating TNF-α, which controls the inflammatory cascade.
PubMed Reference
PMID:11908649
Weng TY, Chen LC, Shyu HW, Chen SH, Wang JR, Yu CK, Lei HY, Yeh TM. (2005) Lactoferrin inhibits enterovirus 71 infection by binding to VP1 protein and host cells. Antiviral Research 67(1):31-37. Lactoferrin binds to host cells, preventing enterovirus 71 from attaching to them. It also interferes with the virus by binding to its VP1 protein.
PubMed Reference
PMID:15916817
Yamauchi K, Tomita M, Giehl TJ, Ellison RT. (1993) Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment. Infection and Immunity 61:719-28. Lactoferrin and lactoferricin damage the outer membranes of gram-negative bacteria. Lactoferricin also has direct bactericidal activity by the formation of "membrane blisters" on the bacteria.
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PMID:8423097
Zagulski T, Jarzabek Z, Zagulska A, Zimecki M. (1998) The main systemic, highly effective, and quickly acting antimicrobial mechanisms generated by lactoferrin in mammals in vivo. Activity in health and disease. Advances in Lactoferrin Research. 443:247-50. Review of the principal ways lactoferrin defends against pathogens.
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Zimecki M, Spiegel K, Wlaszczyk A, Kubler A, Kruzel ML. (1999) Lactoferrin increases the output of neutrophil precursors and attenuates the spontaneous production of TNF-alpha and IL-6 by peripheral blood cells. Archivum Immunologiae et Therapie Experimentalis 47(2):113-118. Lactoferrin supplementation profoundly decreased the product of TNF-alpha and IL-6 (pro-inflammatory cytokines) in blood cultures while causing a transient increase of immature neutrophils in the blood.
PubMed Reference
PMID:10202564
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