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Last Updated on Tuesday, 08 September 2009 07:30 Saturday, 05 September 2009 14:46

Colostrum IC

Super Concentrated Immune Factors from Colostrum to Maintain Your Health

by John I. Buhmeyer, MS

Colostrum has long been known for its potent, broad spectrum immune benefits.  It has been used for thousands of years as a health maintenance supplement[i].  The antibodies used by Albert Sabin in preparing his first oral polio vaccine came from bovine colostrum[ii],[iii].  A recent study showed that oral supplementation with bovine colostrum is at least three times more effective than flu vaccine in preventing influenza in both healthy subjects and high-risk cardiopulmonary patients[iv].  Now there is a new product, Colostrum IC oral spray, that contains a super concentrate of all the immune factors found in whole colostrum for an even more powerful, and more cost-effective, way to maintain your health.

Designed by nature to be the first food a newborn eats in this life, colostrum contains all the immune and growth factors needed to complete the development of the gut and prime the infant’s immune system to be able to meet the challenges faced by life outside the protection of the mother’s womb.  This is even more important for calves as the placenta of the cow does not allow immune factors to cross over to the fetal blood, as happens in humans.  Thus bovine colostrum is loaded with Immunoglobulin G (IgG)[v], the type of immunoglobulin that provides systemic protection against pathogenic microorganisms and other threats.  Human colostrum, on the other hand, contains mostly Immunoglobulin A (IgA) which provides local immunity in the gut of the newborn.  This is because the immune system of human infant is already primed before birth because of the more permeable placenta of the mother.  This makes bovine colostrum even better for grown-up humans (including children) than human colostrum because IgG provides systemic immunity while IgA does not.

Immunoglobulins are produced by the immune system against a specific antigen (foreign protein) and provide specific immunity against this antigen, which may be a viral or bacterial protein or a toxin.  Bovine colostrum contains various forms of immunoglobulins, including IgG[vi], IgA, sIgA (a secretory form of IgA that is protected against digestion in the gut)[vii], IgD (work as antigen receptors on the surface of B lymphocytes)[viii], IgE (involved in allergic reactions)[ix], and IgM (a complex of IgG molecules produced as an initial response to an antigen)[x].  All of these forms of immunoglobulins work together to fight infections and form the basis of what is termed the adaptive immune system.

There is also a so-called innate immune system that fights infections non-specifically. Many of the immune components of colostrum are part of this system, particularly lactoferrin and PRP (Proline-Rich Polypeptides). 

Lactoferrin is a large protein that has many functions in the body, including iron homeostasis, bone metabolism regulation, embryonic development and reproductive functions, as well as analgesic, anti-inflammatory and anti-tumor activity [xi],[xii],[xiii],[xiv].  In its function as an integral component of host defense[xv], lactoferrin is a broad spectrum antimicrobial against viruses, bacteria, fungi, and protozoan invaders[xvi].  It also has an immunomodulatory role, stimulating the immune system when needed to fight off an infection and inhibiting the immune system to prevent damage to healthy tissues once the infection has been controlled[xvii].  Lactoferrin has an important role in adaptive immunity as well by increasing the number and activity levels of T and B lymphocytes and Natural Killer (NK) cells, accelerating the maturation of T and B lymphocytes, increasing the phagocytic activity and cytotoxicity of monocytes and macrophages, and stimulating the production of both pro- and anti-inflammatory cytokines, including Tumor Necrosis Factor-alpha (TNF-α), gamma interferon (INF-γ), and various interleukins, IL-1, IL-6, IL-8 and IL-1812.  It also increases the production of cell receptors involved in the immune response12.  Lactoferrin competes with viruses for binding sites, effectively blocking their entrance into target cells, including rotavirus (leading cause of diarrhea in young infants)[xviii], herpes simplex 1 and 2[xix], echovirus[xx], enterovirus[xxi], human papilloma virus (implicated in cervical and other human cancers)[xxii], polio virus[xxiii], hanta virus[xxiv], adenovirus[xxv], respiratory syncytial virus[xxvi], and alphaviruses[xxvii].  Lactoferrin also has the ability to bind directly with the structural proteins of certain viruses, inactivating them21,[xxviii],[xxix], and interfering with certain viral enzymes required for infection or viral replication[xxx],[xxxi],[xxxii].  Lactoferrin is equally effective at killing pathogenic bacteria, including Helicobacter pylori, a major cause of gastric ulcers[xxxiii], and fungal infections, such as Candida.

PRP, which are small peptides (short chains of amino acids), function as intercellular signaling molecules that act as immunomodulators, turning up an underactive immune system or toning down an overactive one by stimulating T lymphocytes to become either helper T-cells to stimulate antibody formation or suppressor T-cells that inhibit killer lymphocytes[xxxiv],[xxxv].  They work through specific receptors on the surface of target cells.  PRP also stimulate the growth and differentiation of B cells[xxxvi] (lymphocytes which produce antibodies) and increase NK activity by up to 10 times[xxxvii].  PRP, like lactoferrin, induce the production of both pro- and anti-inflammatory cytokines, such as TNF-α and INF-γ[xxxviii],[xxxix].  PRP also promotes the proliferation of white blood cells (leukocytes)[xl] and the differentiation and maturation of monocytes and macrophages[xli].  PRP increase the permeability of blood vessels in the skin as part of the inflammatory response[xlii].  As a potent immunomodulator, PRP may be effective in stopping the “cytokine storm” – the cytokine dysregulation that kills patients with bird flu by essentially drowning them in their own fluids[xliii].

In addition to these principal components, colostrum also contains a number of other immune factors.  Lysozyme is a potent antimicrobial which often works in tandem with lactoferrin to kill bacteria and other dangerous microorganisms[xliv],[xlv],[xlvi].  Lactoperoxidase catalyzes the reaction of thiocyanate in the presence of hydrogen peroxide (natural chemicals in the body)[xlvii],[xlviii].  This has a bacteriostatic and, for some bacteria such as E. coli, a bactericidal effect. It is particularly effective in airway defense[xlix],[l]. 

Cytokines are small proteins and peptides that regulate the immune response, acting as either pro- or anti-inflammatory factors.  Colostrum contains high levels of a number of cytokines, including lymphokines, which include the interleukins[li],[lii]:

 

  • IL-1β – enhances the proliferation of T lymphocytes and the growth and development of B lymphocytes, pro-inflammatory[liii]

  • IL-1ra – this is a receptor antagonist for IL-1 that prevents IL-1 from being inhibited

  • IL-2 – induces the proliferation of T lymphocytes, NK cells and activated B lymphocytes, pro-inflammatory

  • IL-4 – causes differentiation of B lymphocytes and Th2 cells (a type of helper T cell involved in IgE production), increases levels of IgG4 and IgE synthesis, anti-inflammatory

  • IL-5 – activates B lymphocytes to produce IgA and causes eosinophils (a type of white blood cell) to differentiate, pro-inflammatory

  • IL-6 – activates T cells, increases synthesis and secretion of immunoglobulins by B lymphocytes, pro-inflammatory[liv]

  • IL-8 – promotes angiogenesis (growth of blood vessels), protects cells from chemical injury, acts as a chemoattractant for neutrophils (white blood cells), pro-inflammatory[lv]

  • IL-10 – inhibits INF-γ and IL-2 secretion by T cells, increases B cell and mast cell proliferation, anti-inflammatory[lvi]

  • IL-12 – induces INF-γ and IL-2 secretion by T cells and NK cells, pro-inflammatory[lvii]

  • IL-13 – growth factor for B cells, modulates B cell responses, increases production of IgM, IgE and IgG4, anti-inflammatory

  • IL-16 – chemoattractant for CD4+ cells (various types of inflammatory immune cells, including helper T cells, monocytes, macrophages and dendritic cells), draws inflammatory cells to infection sites, pro-inflammatory

  • IL-18 – induces INF-γ production by T cells and NK cells, pro-inflammatory[lviii]

Another type of lymphokine in colostrum is interferon.  These interfere with the replication of RNA-viruses as well as activate NK cells and increase the resistance of host cells to viral infection.  Interferon also has significant anti-cancer activity.  Interferon-alpha (INF-α) increases the frequency of INF- γ producing CD4+ T cells and increases levels of IL-4, thus increasing the number of Th1 cells (a type of helper T cell involved in antimicrobial activity)[lix].   INF-γ[lx] is immunoregulatory and pro-inflammatory.

Another class of cytokine found in colostrum is called chemokines[lxi],[lxii].  Chemokines mainly guide the migration of cells out of the blood vessels and into the tissues.  These include:

Eotaxin – a chemoattractant for eosinophils

  • IP-10 – induces migration and activation of intestinal T lymphocytes to enhance mucosal immunity in the gut

  • MCP-1 (CCL2) – chemotactic for monocytes and T cells, induces monocytes to leave the bloodstream and become macrophages at the infection site

  • MIG – another chemotactic which induces lymphocytes to leave the blood stream and move into tumors, controlled by INF-γ

  • RANTES – also chemotactic for T cells, eosinophils and monocytes

TNF-α is a separate type of cytokine found in colostrum.  It is the main control cytokine for the entire pro-inflammatory cascade[lxiii].  It is also cytotoxic for many cancer cells.  TNF-α receptors are also found in colostrum[lxiv].  This a protein that binds to TNF-α, inactivating it. 

Another important component of the immune system found in colostrum is complement[lxv],[lxvi].  Complement is a system of small proteins which adhere to and attack pathogenic microorganisms and other threats in the blood, causing them to lyse (burst).  Nucleotides and nucleosides, the building blocks of DNA, are also important immune components of colostrum.  They modulate cell-mediated immunity and help prevent infection[lxvii].

Human colostrum contains a great variety of immune peptides[lxviii].  They function as the instruments by which the other components perform their functions.  As this is cutting edge biology, their presence is still not confirmed in bovine colostrum, but it is likely they are present.  One of these is called Defensin.  Defensins are antimicrobial and cytotoxic peptides found in all mammals.  They are also part of the innate immune system which provide nonspecific defense against foreign cells and microorganisms by penetrating the cell membranes and altering membrane permeability or opsonizing the cells for targeting by immune cells.  They are particular effective against cells and microorganisms resistant to TNF-α and NK cytolytic factor[lxix].   Others are called cathelicidin polypeptides and toll-like receptors.  They exist in a bewildering variety of types and subtypes that is beyond the scope of this paper to explore, but they do indicate the marvelous complexity of the immune system and how it is necessary to have all components present for it to work at optimum levels. 

This is why Colostrum IC stands in a class by itself amongst immune products for only it contains all the components of the mammalian immune system as found in colostrum.  Other immune products, such as maitake mushrooms, beta-glycan and others, are one-trick ponies compared to this wondrous panoply of immunity. 

Colostrum IC is made from the highest quality organic colostrum.  It is produced year-round from cows in the Southwest United States, and the colostrum is processed at the only processing plant specifically built to process colostrum.  Colostrum IC is supplied as a liquid spray which is readily absorbed into the bloodstream.  As it is highly concentrated, three sprays supply the same amount of immune factors as are contained in 48 capsules of powdered colostrum.  It is safe for all ages.

To maintain a healthy immune system, use only Colostrum IC.

[i] Heinerman,J. Fascinating Colostrum: An Ancient Food for Modern Times. (1999)

[ii] Sabin, A.B.  Antipoliomyelitic substance in milk from human beings and certain cows.  Journal of Diseases of Children, 80:866 (1950)

[iii] Sabin, A.B.; Fieldsteel, A.H.  Antipoliomyelitic activity of human and bovine colostrum and milk.  Pediatrics 29(1):105-115 (1962)

[iv] Cesarone, MR, et al.  Prevention of influenza episodes with colostrum compared with vaccination in healthy and high-risk cardiovascular subjects: the epidemiologic study in San Valentino.  Clinical and Applied Thrombosis/Hemostasis 13(2):130-136 (2007).  Colostrum proved to be three times more effective than vaccination in preventing influenza both in healthy subjects and high-risk cardiovascular patients, and is very cost-effective.

[v] Korhonen, H, et al.  Milk immunoglobulins and complement factors.  British Journal of Nutrition 84(Suppl. 1):S75-S80 (2000).  In bovine colostrum IgG1 accounts of 75% of the total Ig, followed by IgM, IgA and IgG2.

[vi] Akita, EM, Li-Chan, EC.  Isolation of bovine immunoglobulin G subclasses from milk, colostrum, and whey using immobilized egg yolk antibodies.  Journal of Dairy Science 81(1):54-63 (1998).  Both IgG1 and IgG2 subclasses of IgG were isolated from bovine colostrum and milk.  Removal of IgG1 and IgG2 also resulted in the removal of all IgG activity from the colostrum and milk.

[vii] Mach, JP, et al.  IgA with "secretory piece" in bovine colostrum and saliva.  Nature 223(209):952-955 (1969).  Secretory IgA found in bovine colostrum.

[viii] Keller, MA, et al.  IgD in human colostrum.  Pediatric Research 19(1):122-126 (1985).  Concentrations of IgD in human colostrum were measured in a range from 2.2-410 μg/dl (mean concentration 35 µg/dl). 

[ix] Thatcher, EF, Gershwin, LJ.  Colostral transfer of bovine immunoglobulin E and dynamics of serum IgE in calves.  Veterinary Immunology and Immunopathology 20(4):325-334 (1989).  Blood serum levels of IgE in calves was high for the first week postpartum, after which levels declined until 12 weeks of age, when they began to increase again.  This suggests that passive transfer of IgE from the mother via colostrum is important in providing the calf immune protection during the first weeks of life.

[x] Seto, A, et al.  Immunoglobulin M associated with secretory component and immunoglobulin A deficiency in bovine colostrum.  American Journal of Veterinary Research 38(11):1895-1896 (1977).  IgM was found in bovine colostrum associated with the secretory component of sIgA.

[xi] Lonnerdal, B, Iyer, S.  Lactoferrin: molecular structure and biological function.  Annual Review of Nutrition 15:93-110 (1995).  Lactoferrin, as an iron-binding protein, has a role in bacteriostatic activity by withholding iron from iron-requiring bacteria.  Its presence in the granules of neutrophils indicates it has a role in immune responses to infections.  It also appears to function as a growth factor and bactericidal agent.

[xii] Artym, J.  [Antitumor and chemopreventive activity of lactoferrin]  Post?py Higieny i Medycyny Doświadczalnej 60:352-369 (2006).  Lactoferrin has direct anti-tumor activity, including lytic (causes tumor cells to burst), pro-apoptotic (causes programmed cell death of tumor cells), anti-proliferative, anti-angiogenic (prevents the growth of blood vessels into the tumor), anti-oxidant and chemopreventive properties. 

[xiii] Britigan, BE, Serody, JS, Cohen, MS.  The role of lactoferrin as an anti-inflammatory molecule.  Advances in Experimental Medicine and Biology 357:143-156 (1994).  The iron-lactoferrin complex can both promote and inhibit free radical production by neutrophils and monocytes.  Generally it plays an anti-inflammatory role in infections.

[xiv] Artym, J, Zimecki, M.  [The role of lactoferrin in the proper development of newborns]  Post?py Higieny i Medycyny Doświadczalnej 59:421-432 (2005).  Lactoferrin has an immunotropic effect on the newborn, stimulating both local and systemic immune responses.  It also plays a role in the absorption of nutrients, particular metal ions such as iron, manganese and zinc.  It stimulates the proliferation of gut endothelial cells and gut-associated lymphatic follicles.  In addition, it controls the proper composition of gut flora, suppressing the growth of pathogenic bacteria while promoting the growth and colonization of beneficial bacteria.

[xv] Ward, PP, Uribe-Luna S, Conneely, OM.  Lactoferrin and host defense.  Biochemistry and Cell Biology 80(1):95-102 (2002).  Lactoferrin is found at mucosal surfaces throughout the body where it functions as a prominent component of the first line of host defense against infection and inflammation.

[xvi] Weinberg, ED.  Human lactoferrin: a novel therapeutic with broad spectrum potential.  Journal of Pharmacy and Pharmacology 53(10):1303-1310.  Lactoferrin is a broad spectrum antimicrobial with antibacterial, antimycotic, antiviral, antineoplastic and anti-inflammatory activity.

[xvii] Lonnerdal, B.  Nutritional and physiologic significance of human milk proteins.  American Journal of Clinical Nutrition 77(6):1537S-1543S (2003).  Lactoferrin is a milk protein with immunomodulatory effects.

[xviii] Superti, F, et al.  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 (1997).

[xix] Jenssen, H.  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 (2005).

[xx] Pietrantoni, A, et al.  Bovine lactoferrin peptidic fragments involved in inhibition of Echovirus 6 in vitro infection.  Antiviral Research 69(2):98-106 (2006).

[xxi] Weng, TY, et al.  Lactoferrin inhibits enterovirus 71 infection by binding to VP1 protein and host cells.  Antiviral Research 67(1):31-37 (2005).

[xxii] Drobni, P, Naslund, J, Evander, M.  Lactoferrin inhibits human papilloma virus binding and uptake in vitro.  Antiviral Research 64(1):63-68 (2004).

[xxiii] McCann, KB, et al.  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 (2003).

[xxiv] Murphy, ME, et al.  Characterization of in vitro and in vivo antiviral activity of lactoferrin and ribavirin upon hanta virus.  Journal of Veterinary Medicine and Science 63(6):637-645 (2001).

[xxv] Arnold, D, et al.  Antiadenovirus activity of milk proteins: lactoferrin prevents viral infection.  Antiviral Research 53(2):153-158 (2002).

[xxvi] van der Strate, BW, et al.  Antiviral activities of lactoferrin.  Antiviral Research 52(3):225-239 (2001).

[xxvii] Waarts, BL, et al.  Antiviral activity of human lactoferrin: inhibition of alpha virus interaction with heparan sulfate.  Virology 333(2):284-292 (2005).

[xxviii] Seganti, L, et al.  Antiviral activity of lactoferrin towards naked viruses.  Biometals 17(3):295-299 (2004).

[xxix] Nozaki, A, et al.  Identification of a lactoferrin-derived peptide possessing binding activity to hepatitis C virus E2 envelope protein.  Journal of Biological Chemistry 278(12):10162-10173 (2003).

[xxx] Kawasaki, Y, et al.  Inhibition by kappa-casein glycomacropeptide and lactoferrin of influenza virus hemagglutination.  Bioscience, Biotechnology, and Biochemistry 57(7):1214-1215 (1993).

[xxxi] Ng, TB, et al.  Inhibition of human immunodeficiency virus type 1 reverse transcriptase, protease and integrase by bovine milk proteins.  Life Science 69(19):2217-2223 (2001).

[xxxii] Ohashi, A, et al.  New functions of lactoferrin and beta-casein in mammalian milk as cysteine protease inhibitors.  Biochemistry and Biophysics Research Communications 306(1):98-103 (2003).

[xxxiii] Dial, EJ, et al.  Antibiotic properties of bovine lactoferrin on Helicobacter pylori.  Digestive Diseases and Sciences 43(12):2750-2756 (1998).

[xxxiv] Janusz, M, et al. 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):427-436 (1986).

[xxxv] Wieczorek, Z, et al.  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 (1989).

[xxxvi] Julius, MH, Janusz, M, Lisowski, J.  A colostral protein that induces the growth and differentiation of resting B lymphocytes.  Journal of Immunology 140(5):1366-371 (1988).

[xxxvii] See, DM, et al.  The role of natural killer cells in viral infections.  Scandinavian Journal of Immunology 46(3):217-224 (1997).

[xxxviii] Inglot, A.D, Janusz, M, Lisowski, J.  Colostrinine: a proline-rich polypeptide from ovine colostrum is a modest cytokine inducer in human leukocytes.  Archivum immunologiae et therapiae experimentalis (Warszava) 44(4):215-224 (1996).

[xxxix] Blach-Olszewska, Z, Janusz, M.  Stimulatory effect of ovine colostrinine (a proline-rich polypeptide) on interferons and tumor necrosis factor production by murine resident peritoneal cells.  Archivum immunologiae et therapiae experimentalis (Warszava) 45(1):43-47 (1997).

[xl] Kruzel, ML, et al.  Towards an understanding of biological role of colostrinin peptides.  Journal of Molecular Neuroscience 17(3):379-389 (2001).

[xli] Kubis, A, et al.  Studies on the mechanism of action of a proline-rich polypeptide complex (PRP): effect on the stage of cell differentiation.  Peptides 26(11):2188-2192 (2005).

[xlii] Janusz, M, Lisowski, J.  Proline-rich polypeptide (PRP)--an immunomodulatory peptide from ovine colostrum.  Archivum immunologiae et therapiae experimentalis (Warszava) 41(5-6):275-279 (1993).

[xliii] Chan, MC, et al.  Proinflammatory cytokine responses induced by influenza A (H5N1) viruses in primary human alveolar and bronchial epithelial cells.  Respiratory Research 6:135 (2005).

[xliv] Paulik, S, et al.  [Lysozyme in the colostrum and blood of calves and dairy cows]  Veterinarni Medicina 30(1):21-28 (1985).  In first colostrum the lysozyme concentration fluctuated within the range of 0.15 to 0.65 μg/ml, with an average of 0.30 μg/ml. The concentration of lysozyme and immunoglobulins of the IgG and IgM class in colostrum showed a contrary trend in first and second milk yield, with a tendency towards increase for lysozyme and towards decrease for immunoglobulins.

[xlv] Ellison, RT, III; Giehl, TJ.  Killing of gram-negative bacteria by lactoferrin and lysozyme.  Journal of Clinical Investigation 88(4):1080-1091 (1991).

[xlvi] Erhardt, G, Meyer, F, Senft, B.  Growth inhibition of Staphylococcus aureus after experimental infection of the udder by high and low concentration of lactoferrin and lysozyme in milk.  Acta Microbiologica Polonica 30(3):239-246 (1981).

[xlvii] Kussendrager, KD, van Hooijdonk, AC.  Lactoperoxidase: physico-chemical properties, occurrence, mechanism of action and applications.  British Journal of Nutrition 84(Suppl 1):S19-S25 (2000).

[xlviii] Thomas, EL, et al.  Inhibition of Streptococcus mutans by the lactoperoxidase antimicrobial system.  Infection and Immunity 39(2):767-778 (1983).

[xlix] Gerson, C, et al.  The lactoperoxidase system functions in bacterial clearance of airways.  American Journal of Respiratory Cell and Molecular Biology 22(6):665-671 (2000).

[l] Wijkstrom-Frei, C, et al.  Lactoperoxidase and Human Airway Host Defense.  American Journal of Respiratory Cell and Molecular Biology 29(2):206-212 (2003).

[li] Bocci, V, et al.  What is the role of cytokines in human colostrum?  Journal of Biological Regulators and Homeostatic Agents 5(4):121-124 (1991).

[lii] Hagiwara, K, et al.  Detection of cytokines in bovine colostrum.  Veterinary Immunology and Immunopathology 76(3-4):183-190 (2000).  ELISA specific for bovine cytokines detected five cytokines in bovine colostrum: IL-1β, IL-6, INF-α, INF-γ, and IL-1 ra (receptor antagonist).

[liii] Hagiwara, K, et al.  Oral administration of IL-1 beta enhanced the proliferation of lymphocytes and the O(2)(-) production of neutrophils in newborn calf.  Veterinary Immunology and Immunopathology 81(1-2):59-69 (2001).

[liv] Rudloff, HE, et al.  Interleukin-6 in human milk.  Journal of Reproductive Immunology 23(1):13-20 (1993).

[lv] Hashira, S, et al.  Interleukin 8 in the human colostrum.  Biology of the Neonate 82(1):34-38 (2002).

[lvi] Garofalo, R, et al.  Interleukin-10 in human milk.  Pediatric Research 37(4pt1):444-449 (1995).

[lvii] Bryan, DL, et al.  Interleukin-12 in human milk.  Pediatric Research 45(6):858-859 (1999). 

[lviii] Takahata, Y, et al.  Interleukin-18 in human milk.  Pediatric Research 50(2):268-272 (2001).

[lix] Brinkman, V, et al.  Interferon alpha increases the frequency of interferon gamma-producing human CD4+ T cells.  Journal of Experimental Medicine 178(5):1655-1663 (1993).

[lx] Lawson, JW, et al.  Interferon synthesis by human colostral leucocytes.  Archives of Diseases of Children 54(2):127-130 (1979).

[lxi] Bottcher, MF, Jenmalm, MC, Bjorksten, B.  Cytokine, chemokine and secretory IgA levels in human milk in relation to atopic disease and IgA production in infants.  Pediatric Allergy and Immunology 14(1):35-41 (2003).

[lxii] Takahata, Y, et al.  Detection of interferon-gamma-inducible chemokines in human milk.  Acta Paediatrica 92(6):659-665 (2003).

[lxiii] Rudloff, HE, et al.  Tumor necrosis factor-alpha in human milk.  Pediatric Research 31(1):29-33 (1992). 

[lxiv] Buescher, ES, McWilliams-Koeppen, P.  Soluble tumor necrosis factor-alpha (TNF-alpha) receptors in human colostrum and milk bind to TNF-alpha and neutralize TNF-alpha bioactivity.  Pediatric Research 44(1):37-42 (1998).

[lxv] Brock, JH, et al.  Bactericidal and hemolytic activity of complement in bovine colostrum and serum: effect of proteolytic enzymes and ethylene glycol tetraacetic acid (EGTA).  Annales d’Immunologie  126C(4):439-451 (1975).

[lxvi] Yamada, M, et al.  Identification of low-abundance proteins of bovine colostral and mature milk using two-dimensional electrophoresis followed by microsequencing and mass spectrometry.  Electrophoresis 23(7-8):1153-1160 (2002).

[lxvii] Yu, VY. Scientific rationale and benefits of nucleotide supplementation of infant formula. Journal of Paediatrics and Child Health 38:543–549 (2002).

[lxviii] Armogida, SA, et al.  Identification and quantification of innate immune system mediators in human breast milk.  Allergy and Asthma Proceedings 25(5):297-304 (2004)

[lxix] Lehrer, RI, Lichtenstein, AK, Ganz, T.  Defensins: antimicrobial and cytotoxic peptides of mammalian cells.  Annual Reviews of Immunology 11:105-128 (1993).

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