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Reviews
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 Beta Glucan |
WHAT IS BETA 1,3/1,6-D-GLUCANBeta glucans are extracted from the common baker's yeast Saccharomyces cervislae and composed of chains of 20-30 glucose units with side chains of beta 1,3 and beta 1,6 linked D-glucose molecules. The overall effect is that of a tree with a trunk, and conditions to yield pure glucans with their unique structures preserved for mzximum interaction and activation of immune cells. These products contain no yeast cells, are completely safe and have no toxic side effects.
HOW BETA GLUCANS ACTIVATE THE IMMUNE SYSTEMIn the 1960's Nicholas DiLuzio and his collaborators published a number of papers That described the broad spectrum anti bacterial and tumor inhibitory activity of beta glucans. These observations were attributed to augmented host immune defense by mechanisms involving macrophage or phagocyte activation. Phagocytes (monocytes, macrophages, granulocytes), natural killer cells, dendritic cells, and langrehans cells of skin bear specific receptor sites termed dectin-1 (betaGR) that bind beta 1,3 and or beta 1,6 glucans. Phagocytes also express a whole range of receptors that recognize and bind to foreign invaders, such as microbes, viruses, yeasts, parasites and possibly even neoplastic cells. Binding to certain organisms is also facilitated by recognizing serum opsonins or antibodies that have been deposited on their surface. Once the cell receptor binds beta glucans, immune activity is initiated. Activated macrophages undergo morphologic and physiologic changes that result in enhanced phagocytic (scavenger) activity, release certain cytokines or hormone messengers that engage both innate and acquired immune system (see transfer factor). Such cytokines as tumor necrosis factor alpha, interleukin-1 beta and granulocyte - macrophage colony stimulating factor and others profoundly affect local and systemic immunity.
IMMUNO-PHYSIOLOGIC EFFECTS OF BETA GLUCAN ADMINISTRATION
Host Immune Response:The administration of purified yeast glucan to a host rapidly results in an augmented state of hose resistance to a diverse range of microbial pathogens and possibly neoplastic cells. Prior to establishment of such resistance, surface receptors, Dectin-1 on macrophages, monocytes neutrophils, dedritic cells and subpopulation of T cells recognize and bind beta glucan. Lung (alveolar) macrophages, like inflammatory macrophages exhibit the highest surface expression of Dectin-1 (beta GR) glucan receptor and provide an important mechanism for internalization and clearance of particulate pathogenic targets. This indicates a role for the receptor in immune surveillance and control of disease. Yeast type beta glucans are also potent biologic response modifiers. They markedly augment host resistance to a variety of biologic insults by eliciting a cascade of stimulatory events initiated by mononuclear phagocytes. Upon interaction and binding of beta glucan, macrophages produce bactericidal compounds like Iysozyne, reactive oxygen radicals and nitric oxide. In addition, these cells start producing a number of inflammatory cystokines that will interact with the surrounding macrophages and lymphocytes to initiate local and acquired specific immunity. Some of these cytokines are interleukin-1, interleukin-6, and tumor necrosis factor alpha.
Interleukin-1:Upon binding and phagocytosis of glucan by macrophages, these cells release interleukin-1 (IL-1) an immune systems messenger. IL-1 alpha and IL-1 beta are two similar polypeptides involved in inflammatory reactions.
Interleukins-6:Interleukins-6 is a multifunctional protein that plays important roles in host defense, acute phase reactions, immune response and hematopoiesis or production of blood cells.
Tumor Necrosis Factor Alpha:Under experimental conditions, mice administered beta glucan produce tumor necrosis factor (TNF-alpha) in their peritoneal macrophages. Similarly human monocytes stimulated with beta glucan in culture produce TNF-alpha. Studies implicate binding of Dectin-1 the macrophage receptor in production of TNF-alpha, a critical step required for the successful control of many pathogens.
Effect of beta glucan On Antibiotic Therapy:Beta glucan redness need and potentiates antibiotic therapy. When beta glucan was added to antibiotic regimen in animals challenged with different bacterial and fungal pathogens (Stahpylococcus aureus, kiebsiella pneumoniae, Escherchia coli, Candida albicans and others) or viral pathogens such as herpes and murine viral hepatitis, a reduced amount of antibiotics or antivirals were needed to cope with the infection.
Effect of beta glucan on Immune Deficiency:In certain cases of virally induced immune deficiency, beta glucan ameliorated the infectious process in these patients possible by mounting a direct assult against the indigenous viral infection or by mechanisms referred to above preventing over growth of opportunistic pathogens.
Effect of beta glucan on radiations:Under experimental conditions, rodents exposed to lethal and sub-lethal irradiation and administered beta glucan had significantly larger number of survivors. These observations were attributed to the fact that beta glucan is a potent free radical scavenger that protects blood macrophages from free radical attack after radiation exposure thus ensuring immune function. Additionally administration of beta glucan enhanced hemopoietic reconstitution and stimulated production of blood stem cells thus preventing septicemia and resistance to enteric opportunistic pathogens.
Effect of beta glucan on Chemotherapy:Chemotherapy may induce immune suppression and result in subsequent infection with opportunistic infections. Such life threatening conditions may be averted by administration of beta glucan. Leukocytopenia is a decrease in the number of white blood cells due to chemotherapy. Consequently lower dosages of drugs are used which comprise the curative effect of chemotherapy. However, with beta glucan, white blood cell deplection may be avoided in experimental animals. In another experimental model, combination of beta gulcan and interferon-gamma demonstrated synergistic therapeutic effect. Similarly superior synergistic potential of beta glucan in combination with radiation and chemotherapy were reported.
Effect of beta glucan on Wound Healing:The effectiveness of yeast glucan on acceleration of wound healing was evaluated in several experimental animal models. In every instance, animals treated with beta glucan showed more advanced healing. The histological analysis showed that the acceleration of wound healing was mediated by early arrival of macrophages to the wound area in the glucan treated animals.
REFERENCE:
| 01. | Manners DJ, Mason AJ, Patterson JC. The structure of a beta-(1-3)-glucan from yeast cell walls. Biochem. J. 135: 19-30, 1973. |
| 02. | Williams DL, Sherwood ER, Browder JW, etal. Pre clinical safety evaluation of soluble glucan. Int. J. Immunopharmacol. 10: 405-411, 1988. |
| 03. | DI Luzio NR. Pharmacology of the reticuloendothelial system: accent on glucan. In The Reticuloendothelial System in Health and Disease. Reichard S, Escobar M, and Friedman H, eds. New York, Plenum Press, pp 412-421, 1976. |
| 04. | Wooles WR, DI Luzio NR, The phagocytic and proliferative response of reticuloendothelial system following glucan administration. J. Reticuloendothelial Sec. 1: 160, 1964. |
| 05. | Czop LK, Kay j. Isolation and characterization of beta glucan receptors on human mononuclear phagocytes. J. Exp. Med. 173: 1511-1520, 1991. |
| 06. | Taylor PR, Brown GD, Reid DM, Willment JA, etal. The beta-glucan receptor, Dectin-1 is predominantly expressed on the surface of cells of the monocyte/ macrophage and neutrophil lineages. J. Immunol. 169: 3876-3882, 2002. |
| 07. | Brown GD, Taylor PR, Reid DM, Willment JA, etal. Dectin-1 is a major beta-glucan receptor on macrophages. J. Exp. Med. 196: 407-412, 2002. |
| 08. | Herr J, Marshall AS, Caron E, Edwards AD, etal. Derctin-1 utilizes novel mechanisms for yeast phagocytosis in macrophages. Blood Aug 10 (pub ahead of print). |
| 09. | Suzuki I, Tanaka H, Kinoshita A, Oikawa S, etal. Effect of orally administered beta-glucan on macrophage function in mice. Int. J. Immunopharmacol. 12:675-678, 1990. |
| 10. | Kokoshis PL, Williams DL, Cook JA, Di Luzio NR. Increased resistance to Staphylococcus aureus infection and enhaucement in serum lysozyme activity by glucan. Science 24: 1340-1342, 1978. |
| 11. | Di Luzio NR, Williams DL, McNamee RB, Malshet VG. Comparative evaluation of the tumor inhibitory and antibacterial activity of solubilized and particulate glucan. Recent results cancer res. 75: 165-72, 1980. |
| 12. | Reynolds JA, Kastello MD, Harrington DG, Crabbs CL. Glucan-induced enhaucement of host resistance to selected infectious diseases. Infect. Immun. 30: 51-57, 1980. |
| 13. | Williams DL, Sherwood ER, Brewder IW, Mcnamee RB, etal. Effect of glucan on neutrophil dynamics and immune function in Escherichia coli peritonitis. J. Surg. Res. 44: 54-61, 1988. |
| 14. | Williams DL, Di Luzio NR. Glucan-Induced modification of murine Viral hepatitis. Science 208: 67-69, 1980. |
| 15. | Bistoni F, Vecchiarelli A, Cenci E, puccetti P, etal. Evidence for macrophage-mediated protection against lethal Candida albicns infection. Infect. Immun. 51: 668-674, 1986. |
| 16. | Williams DL, Cook JA, Hoffman EO, etal. Protective effect of glucan in experimentally induced candidiasis. J. Reticulocndothelial Soc. 23: 479-490, 1978. |
| 17. | Di Luzio NR, McNamee R, Browder WI, Williams D. Glucan: Inhibition of tumor growth and enhancement of survival in four syngeneic murine tumor models. Cancel Treat. Rep. 62: 1857-1866, 1978. |
| 18. | Di Luzio NR, Williams DL, McNamee RB, etal. Comparative tumor inhibitory and anti-bacterial activity of soluble and particulate glucan. Int. J. Cancer. 24: 773-779, 1979. |
| 19. | Di Luzio NR, McNamee R, Jones E, etal. The employment of glucan and glucan activated macrophages in the enhancement of host resistance to malignancies in experimental animals. In M. D. Fink ed. The Macrophage in Neoplasia, pp. 181-198, Academic Press, New York 1976. |
| 20. | Mansel PWA, etal. Macrophage-mediated destruction of human malignant cells in vivo. J. Natl. Cancer Inst. 54: 571-580, 1975. |
| 21. | Stewart CC, etal. Preliminary observations on the effect of glucan in combination with radiation and chemotherapy in four murine tumors. Cancer Treat. Rep. 62: 1867-1872, 1978. |
| 22. | Di Luzio NR, Cook JA, Cohen C, etal. Enhancement of the inhibitory effect of cyclophosphamide on experimental acute myclogenous leukemia by glucan immunopotentiation and the response of serum lysozyme. In control of Neoplasia by Modulation of the Immune System. Ed. M. Chigiros. New York, Raven press 1978. |
| 23. | Sveinbjornsson B. Inhibition of extablishemtn and growth of mouse liver metastases after treatment with interferon gamma and bet-1,3-glucan. Hepatology 27: 1241-1248, 1998. | | 24. | Gyorgy A. Czop JK. Stimulation of human monocyte beta glucan receptors by glucan particies induces production of UNF alpha and IL-1 beta. J. Immunopharmac. 14:1363-1372, 1992. |
| 25. | Patcheu MI., Mac Vittie TJ. Stimulation of hemopoiesis and euhanced survival following glucan treatment in sub lethally and lethally irradiated mice. Int J. Immunopharmacol. 7:923-923, 1985 |
| 27. | Patchen MI., D' Alesandro MM, Brook I, etal. Glucan: mechanisms involved in its 'radio protective' effect. J. Leukoe Biol. 24:95-105, 1987. |
| 28. | Patchen MI., MacVittie TJ, Brook I. Glucan-induced hemopoietic and immune stimulation: therapeutic effects in sub lethally and lethally irradiated mice. Methods Find. Exp. Chin, Pharmacol. 8:151-155, 1986.
Walk M, Danon D. Promotion of wound healing by yeast glucan evaluated on single animals. Med Biol. 63:73-80, 1985. |
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| Transfer Factor |
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A brief review of the immune system is presented here for a better understanding of the section that follows. Additional information appears in the links section.
THE IMMUNE SYSTEMThe immune system is composed of a global and dynamic collection of highly specialized cells and tissues dispersed through out the body. Within this system is the bone marrow, the white blood cells, the lymph nodes, the spleen, Peyer,s patches the thymus and the mucosal and the gut associated lymphoid tissues.
There are two functional divisions within the immune system, innate and acquired.
INNATE IMMUNITYInnate (natural) immunity derives from all those elements with which an individual is born and are always present and available at very short notice to protect the individual from challenges by foreign material These elements include the skin, the mucous membranes and cough reflex as physical barriers to environmental agents. Chemical influences such as pH, secreted fatty acids and the enzyme lysozyme constitute effective barriers against invasion by many microorganisms.
Numerous internal elements are also features of innate immunity, fever, interferons interleukins, complement, lysozyme in the tears and saliva, acute – phase proteins, beta lysine, polyamines and the kinins. Other internal elements of innate immunity include natural killer cells, granulocytes, macrophages, microglial cells of the central nervous system and the cytotrophoblasts of placental villi. These cells all participate in the destruction and elimination of foreign material that has succeeded in penetrating the physical and chemical barriers of the innate immune system.
ACQUIRED IMMUNITYIn contrast to innate immunity, which is an attribute of every living organism, acquired immunity is a more specialized form. It has developed late in evolution and is found only in vertebrates. The various elements that participate in innate immunity do not exhibit specificity against the foreign agent that they encounter, while acquired immunity always exhibits such specificity. Upon contact with an offending foreign agent that has penetrated the body or after immunization or vaccination, a chain of events leads to the activation of a category of cells called lymphocytes. Upon lymphocyte activation, a second cascade of highly complex events leads to two major types of immune response.
Humoral, antibody or B lymphocyte mediated immunity that generally kill and eliminate extra cellular pyogenic (puss producing) microorganisms and neutralize toxins.
Cellular or cell mediated or T lymphocyte mediated immunity against intracellular pathogens, such as yeast cells, certain bacteria viruses, some protozoans and tumor cells.
It should be mentioned however, that T and B lymphocytes are totally interactive and for the most part cooperate in prompting the immune response. There are two types of T lymphocytes:
T helper-inducer, also known as CD 3 cells.
T suppressor-cytotoxic, also known as CD 8 cells.
Within each T lymphocyte population, there are a number of sub populations each of which may perform a different function. It is important to realize that T cells do not synthesize or secrete antibodies, however, T cells do cooperate with B cells to induce production of antibodies by B cells. During cellular immune activation, certain T cell populations secrete regulatory peptides or hormone like products know as cytokines. The various cell populations and the cytokines orchestrate the immune system to a crescendo that culminates in an immediate or long term, perhaps life long immunity. Variations in the numbers and functions of these cell populations and cytokines involved compared to normal values may be indicative of various diseases, however, diagnosis of any immunologic disorder, requires comprehensive laboratory tests and evaluation.
TRANSFER FACTORS
Transfer factors (T.F.) are low molecular weight peptides or immune messengers that transfer the ability to express cell mediated immunity (or delayed type hypersensitivity) from immune donors to non-immune recipients. H. Sherwood Lawrence demonstrated this passive transfer of immunity (1,2) in 1949. He collected leukocytes from immune donors who demonstrated a positive skin reaction to a specific antigen and prepared extracts from them. He injected the extracts to skin test negative or immune compromised subjects. Subsequently the recipients reverted to skin positive reactions to the same antigens. These experiments thus provided direct and dramatic evidence for transfer of systemic and specific immunity between individuals. Subsequent repetition of these experiments with other antigens and indeed therapeutic trials of transfer of cellular immunity conducted by many investigators have confirmed and extended Lawrence's original observations. The results of these studies appear in thousands of publications a mini review of which appears later (see clinical and therapeutic uses of T.F.). It should be emphasized that transfer factors do not act as drugs for specific disease conditions, however, apparently, they endow the recipient with de novo immune capacity to resist and repel infections. Transfer factors are small peptides composed of number of amino acid residues (66, 67). Multiple combinatorial patterns between these amino acids create a vast number of different T.F. molecules. Such a large number of molecules would then satisfy the notion that a specific T.F. molecule is necessary to transfer immunity to each and every specific antigenic determinant (68). Another words, T.F. transfers immune power to a recipient who will subsequently gain specific immunity.
MECHANISM OF T.F. ACTIONClinical trials have demonstrated that antigen specific T.F. therapy, results in induction of cell mediated immunity and successful response to the corresponding antigen or hostile invaders (38,69,70). The T.F. recipient apparently becomes educated or armed to recognize and repel viral, bacterial, fungal, protozoan and possibly even neoplastic invader. Recent experiments in murine (mice) recipients have shown that in vivo administration of transfer factors endows the recipients' spleen cells with the property of responding to the corresponding antigen in vitro by secreting gamma interferon (71), a product of T helper 1 cells. These experiments demonstrate induction of cell-mediated immunity in the recipient mice, however, the nature of structure of the target molecules or receptors for TF are not known.
An intriguing facet of T.F. is that two opposing antigen specific activities can be detected within the same preparation (72,73). One activity is possessed of helper function (inducer factor), while the opposing activity is possessed of suppressor function (suppressor factor). Since the immune response may be both under active as in various types of immune deficiencies or over active as in allergy or autoimmunity, the inducer/suppressor factors help to maintain an immune regulatory network that keeps the immune system balanced and healthy.
SOURCES OF TRANSFER FACTORThere are many sources of T.F. mammalian, chicken cells or even cells from primitive species. Early researchers prepared T.F. from leukocyte extracts of donors. Specific T.F. for a particular antigen or pathogen can be prepared from immune or vaccinated donor cells. More recently, colostrum extracts have become the preferred source of T. F. Colostrums are rich in T.F. and readily available from commercial sources. Colostrums are the pre milk and the first food given by a mother to the newborn. During the first few days of life, colostrum and later the mother's milk protects the baby from infections while it's own immune system matures.
ORAL TRANSFER FACTORSMost of the original clinical trials with transfer factors (14,38,47,48,49) used parenteral injections to administer T.F. Obviously the oral route would be preferable, however, it was originally assumed that the acidic and enzymatic environment of the gastrointestinal tract would destroy the factors. Experimental (38) and human trials (10,15,32,33,53, also see Biotherapy vol. 9, 1996) have amply demonstrated there is little if any loss of transfer factor activity taken orally.
SPECIES SPECIFICITY AND TRANSFER FACTOR THERAPYTransfer factors made form animal or human sources can transfer immunity to each other. That is, there are no species barriers fro T.F. therapy. Even primitive species have cells from which one can prepare T.F. Therefore larger animal sources provide adequate quantities of T.F. for human use.
RATIONAL FOR TRANSFER FACTOR THERAPYTransfer factor is an immunoregulatory, immunosupportive agent with normalizing effect on aberrant immune response. As such it does not act in the same way as an antibiotic or a chemotherapeutic agent but rather, it may up regulate or down regulate immune responsiveness through its helper/suppressor activities to achieve normalcy. T.F. is an effective and safe product that acts as an adaptogen with broad based immune activity.
CLINICAL AND THERAPEUTIC USES OF TRANSFER FACTORThe Food and Drug Administration have not evaluated the following information. It is not claimed that any product mentioned here can prevent treat or cure any disease. It is not suggested that anyone should replace traditional medical treatment for any product mentioned here. On this website you will read testimonies about nutritional supplements. Please use common sense, information and good judgment to evaluate these products and statements. Testimonies may be based on placebo effect, that means perceived results that are in fact false and therefore of short duration. Some statements and testimonies are made by health professional who may recommend our products and who may have conflict of interest. We advise any and all prospective users of our products to use sound and informed judgment before any purchase. There are currently over 3000 publications dealing with clinical uses of TF. Two recent symposia held by the INTERNATIONAL TRANSFER FACTOR SOCIETY in 1996 and 1999 are excellent sources of information on the clinical and therapeutic uses of TF.
To enhance the immune response, TF has been used for the therapy of viral diseases such as hepatitis (5, 6), chronic hepatitis B (7, 8), hepatitis C (9), herpes infections (10), ocular herpes (11), genital or labial herpes (12), herpes zoster (13, 14), cytomegalovirus (15, 16), Epstein-Bar Virus (17, 18) and, human immunodeficiency virus/AIDS (19-26). Additionally TF has been utilized in the therapy of bacteria such as Mycobacterium leprae (27) Salmonella cholera suis infection (28), Salmonella B (29), severely infected pediatric patients with pneumonia gastrointestinal infections, repetitive urinary tract infections, vulvovaginitis, skin infections, and herpes simplex infections (30), A number of protozoan infections such as Leishmania (31), Cryptosporidiosis in AIDS patients (32, 33), fungal infections such as coccidiomycosis (34), histoplasmosis (35) and candidacies (36, 37, 38, 39). A great amount of literature (40-45), deals with the use of TF for the treatment of chronic fatigue syndrome (CSF). Anti HHV-6 oral TF administered to two CSF patients, significantly improved the clinical manifestations in one patient (46). In our own studies (Youdim S. and Shima G. Unpublished Data), we observed dramatic improvement in the clinical status of patients with high titer antibodies to CMV, EBV and/or HSV treated with non-specific TF, gamma globulin and interferon alpha. These patients manifested symptoms similar to CSF patients. In another series of studies, we (47, 48, 49) treated a group of patients with allergies, dermatitis, multiple chemical sensitivities and environmental illness with non-specific TF in addition to other therapeutic modalities. These measures greatly enhanced their quality of life and relief from their symptoms. Transfer factor was also used with some measure of success to treat atopic dermatitis (49-52), hyper IgE syndrome (49, 53), hypereuosiophilia (54), discoid lupus (55), and rheumatoid arthritis (56, 57). These latter uses of TF are of interest as they point to the immunoregulatory, inducer/suppressor function of TF eluded to earlier (72, 73). A large number of older and recent papers discuss treatment of neurological disorders such as multiple sclerosis (58, 59, 60), amyotrophic lateral sclerosis (61, 62), Guillain-Barre Syndrome (63), autism (64), and senility (65). There are also a great number of publications regarding the use of TF in cancer immune therapy and a vast amount of literature on basic research both of which are outside the scope of this review.
REFERENCES |
| 01. | Lawrence HS. Transfer factor in cellular immunity. Harvey lecture series 68, New York: Academic Press, 239-350, 1974 |
| 02. | Lawrence HS. The transfer in humans of delayed sensitivity to Streptococcal M substance and tuberculin with disrupted leukocytes. J Clin Invest 34: 219-232, 1955 |
| 03. | Transfer factor in the Era of AIDS: The Proceedings of the 9th international Symposium on Transfer Factor, 22-24 June 1995, Bologna, Italy. G Pizza and D. Visa, Guest Eds. Biotherapy 9: 1-187, 1995 |
| 04. | Khan A, Nagata k, hill NO. etal. Management of Viral infections with transfer factor. In Khan A, Kirkpatrick CH, Hill NO, eds. Immune regulators in transfer factor. New York: Academic Press, 501-511, 1974 |
| 05. | Khan A, Nagata k, hill NO. etal. Management of Viral infections with transfer factor. In Khan A, Kirkpatrick CH, Hill NO, eds. Immune regulators in transfer factor. New York: Academic Press, 501-511, 1974 |
| 06. | Shulman ST, Hutio JH, Scott B. Transfer factor therapy of chronic aggressive hepatitis. In Archer MS, Gottlieb AA, Kirkpatrick CH, eds. Transfer factor. Basic properties and clinical applications. New York: Academic Press, 439-448, 1976 |
| 07. | Sumiyama K, Kobayashi M, Miyashiro E: etal. Combination therapy with transfer factor and high dose stronger neo-minophagen C. in chronic Hepatitis B in children (HBw Ag positive). Acta-Paediatr Jap. 33: 327-343, 1991 |
| 08. | Iseki M, Aoyama T, Koizumi Y, Osano M. Effect of transfer factor on chronic Hepatitis B in childhood. Kansenshogaku-Zasshi 63: 1329-1332, 1989 |
| 09. | Langham-Mcnally G, C.C, N. Dopson M.H. Evaluation of specific transfer factor in the treatment of two patients with Hepatitis-C. Two case reports. http://itfs.med.unibo.it/ |
| 10. | Visa D, Vich JM, Phillips J, Rosenfeld F. Orally administered specific transfer factor for the treatment of herpes infections. Lymphokine Res. 4: 27-30, 1985 |
| 11. | Meduri R, Campos E, Scrolli C, etal. Efficacy of transfer factor in treating patients with recurrent ocular herpes infections. Biotherapy 9: 61-66, 1996 |
| 12. | Pizza G, Visa D, De Vinci C. Orally administered HSV-specific transfer factor (TF) prevents genital or labial herpes relapses. Biotherapy 9: 67-72, 1996 |
| 13. | Peetom F, Florey MJ. Transfer factor in the treatment of disseminated herpes zoster (HZ) infection in immune-suppressed patients. In Khan A, Kirkpatrick CH, Hill NO. eds. Immune regulators in transfer factor. New York: Academic Press, 489- , 1974 |
| 14. | Steele WR, Myers MG, Vicent MM. Transfer factor for the prevention of Varicella Zoster infection in childhood Leukemia. N Eng. J. Med. 303: 355-359, 1980 |
| 15. | Jones JF, Wayburn SJ, Fulgitini VA. Treatment of childhood combined Epstein Barr virus/Cytomegalovirus infection with oral bovine transfer factor. Lancet July 18, 1981. |
| 16. | Nkrumah F, Pizza G, Viza D, etal. Regression of Progressive lymphadenopathy in a young child with acute CMV infection following administration of transfer factor with specific anti CMV activity. Lymphok Res. 4: 237-241, 1985. |
| 17. | Neequaye J, Viza D, Pizza G, Levine PH, etal. Specific transfer factor with activity against Epstin-Barr virus reduces late relapse in endemic Burkitt's lymphoma. Anti Canc. Res. 10: 1183-1187, 1990. |
| 18. | Prasad U, bin Jalaludin MA, Rajadurai P, Pizza G, De Vinci C, Vizza D, Levine PH. Transfer factor with anti-EBV avtivity as an adjuvant therapy for nasopharyngeal carcinoma: A pilot study. Biotherapy 9: 109-115, 1996. |
| 19. | Viza D, Lefesvre A, Patrasco M, etal. A preliminary report on three AIDS patients treated with anti-HIV specific transfer factor. J. Exp. Path. 3: 653-659, 1987. |
| 20. | Viza D, Vich JM, Minarro A, etal. Soluble extracts from a lymphoblastoid cell line modulate SAIDS evolution. J. Virol. Meth. 21: 241-253, 1988. |
| 21. | Viza, D. AIDS and transfer factor: Myths, certainties and realities. Biotherapy 9: 17-26, 1996. |
| 22. | Gottlieb AA, Sizemore RC, Gottlieb MS, Kern CH. Rationale and clinical results of using leukocyte-derived immunosupportive therapies in HIV disease. Biotherapy 9: 27-31, 1996. |
| 23. | Fernandez-Ortego C, Dubed M, Ruibal O, Vilarrubia OL, etal. Inhibition of in vitro HIV infection by dialyzable leukocyte extracts. Biotherapy 9:33-40, 1996. |
| 24. | Pizza G, Chiodo F, Colangeli V. etal. Preliminary observation using HIV specific transfer factor in AIDS. Biotherapy 9: 41-47, 1996. |
| 25. | Fudenberg HH, Pizza G, Raise F. etal. Treating AIDS patients with HIV specific transfer factor. Personal communication |
| 26. | Hasting RC, Morales MJ, Shanon EJ. Etal. Preliminary results on the safety and efficacy of transfer factor in leprosy. In Archer MS, Gttlieb AA, Kirkpatrick CH. eds. Transfer factor. Basic properties and clinical applications. New York: academic Press, 465- , 1976. |
| 27. | Arnaudov A, Tziporkov N. Some properties and protective activity of specific DLE against Salmonella cholerae suis infection. Biotherapy 9:105-108, 1996. |
| 28. | Berron R, Almendarez C, Rosiles G. Suppurative adenopathy by salmonella B treated with transfer factor. Case report. http://itfs.med.unibo.it/ |
| 29. | Ayala Dela Cruiz MC, Rodriguez-padilla C, Tamarez-Guerra M. Efficacy of the transfer factor in the severely infected pediatric patient. http://itfs.med.unibo.it/ |
| 30. | Sharma M, Rouzbeh F, Ala F. etal. Transfer factor therapy in human cutaneous leishmania infection (CLI): A double blind clinical trial. In Khan A, Kirkpatrick CH, Hill NO, eds. Immune regulators in transfer factor. New York: Academic Press, 563- ,1974. |
| 31. | Louie E, Borkowsky W, Klesius PH. Treatment of Cryptosporidiosis with oral bovine transfer factor. Clin. Immunol. An Immunopath. 44:329-334, 1987. |
| 32. | Mc Meeking A, Borkowsky W, Klesius PH, etal. A controlled trial of bovine dialyzable leucocyte extract for Cryptosporidiosis in patiens with AIDS. J. Inf. Dis. 161: 108-112, 1990. |
| 33. | Catanzaro A, Spitloer L. Clinical and immunological results of transfer factor therapy in Coccidiodomycosis. In Archer MS, Gottlieb AA, Kirkpatrick Ch. eds. Transfer factor. Basic properties and clinical applications. New York: Academic Press, 477- , 1976. |
| 34. | Graybill Jr, Ellenbogan C, Drossman D, etal. Transfer factor therapy of disseminated Histoplasmosis. In Archer MS, Gottlieb AA, Kirdpatrick CH, eds. Transfer factor. Basic properties and clinical applications. New York: Academic Press, 509- , 1976, |
| 37. | Littman BH, Ross ER, Parkman R, etal. Combination transfer factor-amphotericin B therapy in a case of chronic mucocutaneous candidiasis. A controlled study. In archer MS, Gottlieb AA, Kirpatrick CH. eds. Transfer factor. Basic properties and clinical applications. New York: Academic Press, 495- , 1976. |
| 38. | Ballow M, Hyman L. Immunological reconstitution of chronic mucocutaneous cadidiasis with transfer factor and fetal thymic tissue. In Archer MS, Gottlieb AA, Kirkpatrick CH. eds. Transfer factor. Basic properties and clinical applications. New York: Academic Press, 503- , 1976, |
| 39. | Kirkpatrick CH, Greenburg LE. Treatment of chronic mucocutaneious candidiasis with transfer factor. In: Khan A, Kirkpatrick CH, Hill NO. eds. Immune regulators in transfer factor. New York: Academic Press, 547-559, 1979. |
| 40. | Masi M, De Vinci C, Baricordi OR. Transfer factor in chronic mucocutaneous candidiasis. Biotherapy. 9: 97-103, 1996. |
| 41. | Visa D. Can specific transfer factor be an effective treatment for CFS? The CFIDS chronicle, Physicians forum Fall 1993. |
| 42. | Levine PH. The use of transfer factor in chronic fatigue syndrome: Prospects and problems. Biotherapy. 9: 77-79, 1996. |
| 43. | De Vinci C, Levine PH, Pizza G. etal. Lessons from a pilot study of transfer factor in Chronic Fatigue Syndrome. Biotherapy. 9: 87-90, 1996. |
| 44. | Hana I, Vrubel J., Pekarek J and Cech K. The influence of age on transfer factor treatment of cellular immunodeficiency, chronic fatigue syndrome and/or chronic viral infections. Biotherapy. 9: 91-95, 1996. |
| 45. | Whitaker JA, Dopson MH, Mattman LH. Etal. Preliminary study of transfer factor (TF) in patients with Fibromyalgia (Fm) Chronic Fatigue Syndrome (Cf) and concomitant Lyme Borreliosis. http://itfs.med.unibo.it/ |
| 46. | Fudenburg HH. Therapeutic trial of antgen-specific transfer factor in chronic fatigue immune dysregulation syndrome: evidence of latent virus. http://itfs.med.unibo.it/ |
| 47. | Ablashi DV, Levine PH, De Vinci C. etal. Use of anti HHV-6 transfer factor for the treatment of two patients with chronic fatigue syndrome (CSF). Two case reports. Biotherapy. 9: 81-88, 1996. |
| 48. | Youdim S, Rea WJ, Liang CH. Treatment of environmentally sensitive patients with transfer factor. Part I: Immunologic studies. Clin.Ecol. 7: 55-61, 1990 |
| 49. | Youdim S, Rea WJ. Treatment of environmentally sensitive patients with transfer factor. Part II: Clinical studies and immunological correlates. Clin.Ecol. 7: 62-66, 1990. |
| 50. | Youdim S, Liang CH, Rea WJ. Treatment of environmentally sensitive patients with transfer factor. Part III: Case studies on three patients. Clin.Ecol. 7: 67-72, 1990. |
| 51. | Heim LR. Atopic dermatitis, specific virus infections and Bechet's syndrome, transfer factor therapy. In Khan A, Kirkpatrick CH, Hill NO. eds. Immune regulators in transfer factor. New York: Academic Press, 489- , 1974. |
| 52. | Navaro-Cruz D, Serrano-Miranda E, Orea-s. etal. Transfer factor as a good therapeutic agent in moderate and severe atopic dermatitis. http://itfs.med.unibo.it/ |
| 53. | Cordero-Miranda MA. Serrano-Miranda E. Flores-Sandoval G. etal. Treatment of atopic dermitits with transfer factor and cyclosporine A. http://itfs.med.unibo.it/ |
| 54. | Jones JF, Jeter WS, Hicks MJ. Oral transfer factor (OTF) use in hyper IgE syndrome. In Kirkpatrick CH, Burger DR, Lawrence HS. Eds. Immunobiology of transfer factor. New York: Academic Press, 261-269, 1983, |
| 55. | Ayala-De La Cruz MC, Rodriguez-Padilla C, Tamaz-Guerra R. Management of hypereosinophilia with transfer factor. http://itfs.med.unibo.it/ |
| 56. | Fudenberg HH. Strlkauskas AJ. Goust JM. Etal. Discoid lupus erythmatosus: Dramatic clinical and immunological response to dialyzable leukocyte extract (transfer factor) Trans. Assoc. am. Phys. 94: 279-291, 1981. |
| 57. | Grohn P, Raimo A, Krohn K. The effect of chromatographically purified transfer factor component on juvenile Rheumatoid Arthritis. In Archer MS, Gottleib AA, Kirkpatrick CH. eds. Transfer factor. Basic properties and clinical applications. New York: Academic Press, 613- , 1976. |
| 58. | Cozine WS, Stanfield AB, Stephens C.A.L. Transfer factor immunotherapy of Rheumatoid Arthritis. In Archer MS, Gottlieb AA, Kirkpatrick CH. eds. Transfer factor. Basic properties and clinical applications. New York: Academic Press, 617- , 1976. |
| 59. | Platz P, Casper J, Mogens T. etal. Transfer factor treatment of patients with multiple sclerosis II. Immunological parameters in a long term clinical trial. In Archer MS, Gottlieb AA, Kirkpatrick CH. eds. Transfer factor. Basic properties and clinical applications. New York: Academic Press, 694- , 1976. |
| 60. | McLeod JG, Basten A, Pollard JD. Etal. Transfer factor in the treatment of multiple sclerosis. Clin. Exp. Neurol. 17: 240- , 1980. |
| 61. | Basten A, McLeod JG, Pollard JD. Etal. Transfer factor in the treatment of multiple sclerosis. Lancet 2: 931-934, 1980. |
| 62. | Nevismal O, Pekarek J, Koubek K. etal. Low molecular transfer factor and its use in the treatment of amyotrophic lateral sclerosis. Cesk. Neurol. Neurochir. 54: 220-223, 1990. |
| 63. | Nevismal O. Pekarek J Cech K. An attempt to inhibit the course of amyotrophic lateral sclerosis (ALS) by suppressor factor. Biotherapy. 9: 139-141, 1996. |
| 64. | Khan A, Hill JM, Piga S, Antone Hi AL. Transfer factor in Guillain-Barre syndrome. Arch. Neurol. 36: 1977. |
| 65. | Fudenberg. HH. Dialysable lymphocyte extract (DLyE) in infantile onset autism: A pilot study. Biotherapy. 9: 143-147, 1996. |
| 66. | Huifang W, Guanghua Z, Zhiying Y. etal. Observation of 26 senile cases treated with P-Tfol. http://itfs.med.unibo.it/ |
| 67. | Rozzo JS, Kirkpatrick Ch. Purification of transfer factor. Mol. Immunol. 29: 167-182, 1992 |
| 68. | Kirkpatrick CH. Transfer factors: Identification of conserved sequences in transfer factor molecules. Molecular med. 6: 232-341, 2000. |
| 69. | Dwyer JM. Transfer factor in the age of molecular biology: A review. Biotherapy 9: 7-11, 1996. |
| 70. | Levine AS, Spitler LE, Stites DP, Fudenberg HH. Wiscott-Aldrich syndrome, a genetically determined cellular immunologic deficiency: Clinical and laboratory responses to therapy with transfer factor. Proc. Natl. Acad. Sci. USA 67: 821-828, 1970. |
| 71. | Kirkpatrick CH, Chandler JW, Schimke RN. Chronic mucocutaneous moniliasis with impaired delayed hypersensitivity. Clin. Exp. Immunol. 6: 375-385, 1970 |
| 72. | Alvarez-Thull L, Kirkpatrick CH. Profiles of cytokine production in receipients of transfer factor. Biotherapy 9: 55-59, 1996 |
| 73. | Borkowsky W, Lawrence HS. Antigen-specific inducer factor in human leukocyte dialysis: a product of T helper cells which bind to an anti-V region and anti-Ia region antibodies. In Kirkpatrick CH, Burger DR, Lawrence HS, eds. Immunobiology of transfer factor. New York, Academic Press, 75-89, 1983. |
| 74. | Borkowsky W, Burger J, Pilson R, Lawrence HS. Antigen specific suppressor factor in human leukocyte dialysis: A product of T suppressor cells which binds to anti-V region and anti-Ia region antibodies. In Kirkpatrick CH, Burger DR, Lawrence HS, eds. Immunobiology of transfer factor. New York; Academic Press, 91-114, 1983 |
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| Bovine Immunoglobulin |
1. What is Bovine Immunoglobulin (Ig)Bovine Ig, immunoglobulin concentrate, is a revolutionary new protein source that is based on immunoglobulin derived from serum. It is the first new protein source to come to the protein market in many years. Unlike traditional sources of protein such as casein or whey, bovine Ig is rich in naturally occurring, bioactive proteins such as immunoglobulin and peptides. Proprietary separation and filtration technologies are used to concentrate the bioactive proteins (>85%), which are principally specialized glycoproteins called immunoglobulins(>50%), that are found in serum and serve to protect the body against infection among other roles in the body. The powerful functionality and bioactivity of the proteins and peptides goes beyond the nutritional benefits of an excellent amino acid profile to provide direct immune support, stronger gut barrier function, and protection against over activation of the immune system.
2. Is there science to support the use of bovine Ig in humans?If the processing technology would have existed, this product should have been launched many years ago because the basic science behind the product is recognized in every immunology textbook. Bovine Ig is derived from serum. Serum has two well known characteristics that make it an ideal raw material source for a revolutionary new protein source: 1) Serum contains the humoral immune system. The humoral factors of serum are one of the body’s major defenses against infection; 2) Serum provides the critical factors and nutrients for protein synthesis. It is the gold standard of all natural substances in supporting cell growth, proliferation and wound healing. Cells thrive when the media is supplemented with bovine serum. The origin of the concept for bovine Ig is founded on proven efficacy in food animals. More than 50 studies have been published in animal sciences demonstrating that oral or dietary plasma or serum protein supplementation promotes growth1, particularly lean tissue growth, by both supporting gut barrier function2 and modulating the immune response3.
3. What ensure that bovine Ig is a safe product to use? Bovine Ig consists of naturally occurring proteins that are concentrated using stringent quality control procedures. The raw material is collected in USDA-inspected facilities and approved for use in food products. The purification of the Ig takes place in a closed system, which prevents against contamination. The facility itself is compliant with FDA Good Manufacturing Practices (GMP) for food products. The final product must meet more stringent internal quality standards than the standards for ingredients used in infant formula. A long history of use in the food 3;16;17.supply, the presence of low concentrations of the primary proteins in milk, and published clinical studies in both adults4 and children support the safety of the product5;6.
4. What is the mode of action? Bovine Ig, due to the consistent, high concentration of immunoglobulins and other bioactive proteins and peptides in plasma or serum, has been shown to boost immunity and increase lean tissue accretion in animal studies1;7-13. But, the most exciting aspect of the science is new studies that demonstrate a positive modulation of gut barrier function2;14; 15 and inflammatory cytokine production and expression3;16;17. The effects of bovine Ig on inflammatory cytokine production provides a partial explanation of how bioactive proteins have positive effects on both intestinal permeability and amino acid utilization9. Recent studies of the biological roles of cytokines have opened up a new opportunity towards maximizing protein retention and lean body mass18-25. In bovine Ig or other means to manage cytokines has great potential to reduce the loss of protein through catabolism that is initiated by overstimulation of the immune system.
5. How does bovine Ig compare to other proteins? Like other high quality sources of animal proteins such as meat, milk, or eggs bovine Ig has an excellent amino acid profile. Bovine Ig also has a neutral taste, odor and excellent solubility. However bovine Ig stands alone as a source of proteins and peptides with biological activity and functionality14;30. No other protein source has bioactive immunoglobulins and peptides as its predominant protein component. So bovine Ig differs completely in purpose of use to other protein sources. Proteins like eggs albumin, casein and whey can be used as sole sources of dietary protein due to a highly available, balanced, essential amino acid profile but theses proteins have negligible bioactivity. Bovine Ig, on the other hand, is rich in bioactive proteins, which helps promote amino acid utilization9;11;13. Also, the proteins are relatively large and more complex in structure than whey or casein with a slower rate of digestion, which allows them to retain biological activity and provide amino acids to the body for a longer period of time. Bovine Ig can be combined with whey or other high quality protein sources lower in molecular weight with a more rapid rate of digestion to optimize protein utilization. Retaining biological activity is critical to the dual-benefit of promoting lean tissue growth and amino acid utilization while also supporting immunity.
6. Is bovine Ig broken down by digestion? Immunoglobulin, unlike most proteins, is not completely broken down by digestive processes, which helps it maintain it’s biological activity throughout the GI tract. IgG is stable in mildly acidic conditions (pH of 4) and is not easily hydrolyzed by digestive enzymes. A summary of studies in which the degradation of IgG was studied in various in vitro and in vivo conditions is available. Approximately 20-25% of the immunoglobulin administered survives digestion and degradation. The “survival” of immunoglobulin through the digestive process explains why mothers produce milk enriched with antibodies to protect the neonate, why adults produce and secrete large quantities of immunoglobulin into the digestive tract, and why supplementation has proven to be of benefit to humans and animals.
7. How should bovine Ig be used?For best results, bovine Ig should be consumed in capsules, chewable tablets, protein powders, bars or beverages in a daily serving of 5-10g per day for adults (or 150mg in bovine Ig per kg BW in children) or a rate of 10% of the protein in the product. A level of 2.5 grams per day is recommended for daily immune support. IG is recommended for use in dietary supplements, protein supplements, medical foods and functional foods. The specific applications recommended are products designed for: immunity, gut health, anti-inflammatory products, pre- and post- workout supplements to support recovery; and, with its slow digestion characteristics, bovine Ig is an ideal supplemental protein source for meal replacement products in weight loss. Isoleuine and methionine are the limiting amino acids in bovine Ig. For best results, bovine Ig should be a part of a complete, balanced nutritional program.
REFERENCES:
| 01. | Coffey RD, Cromwell GL. Use of spray-dried animal plasma in diets for weanling pigs. Pig news and Information 2001;22:39-48, |
| 02. | Perez-Bosque A, Amat C, Polo Jet al. Spray-dried animal plasma prevents the effects of Staphylococcus aureus enterotoxin B on intestinal barrier function in weaned rates. J Nutr 2006;136:2838-43. |
| 03. | Perez-Bosque A, Pelegri C, Vicario M et al. Dietary plasma protein affects the immune response of weaned rats challenged with S. aureus Superantigen B. J Nutr 2004;134:2667-72. |
| 04. | Earnest CP, Jordan AN, Safir M, Weaver E, Church TS. Cholesterol –lowering effects of bovine serum immunoglobulin in participants with mild hypercholesterolemia. Am J Clin Nutr 2005;81: 792-8. |
| 05. | Lembcke JL, Peerson JM, Brow KH. Acceptability, safety, and digestibility of spray-dried bovine serum added to diets of recovering malnourished children. J Pediatr Gastroenterol Nutr 1997;25:381-4. |
| 06. | Begin F, Santizo MC, Peerson JM, Torun B; Brown KH. Effects of bovine serum concentrate, with or without supplemental micronutrients, on the growth morbidity, and micronutrient status of young children in a low-income, perl-urban Guatemalan community. Eur J Clin Nutr 2007. |
| 07. | Hansen JA, Nelssen JL, Goodband RD, Weeden TL. Evaluation of animal protein supplements in diets of early-weaned pigs. J Anim Sci1993;71:1853-62. |
| 08. | Jlang R, Chang X, Stoll B et al. Dietary plasma protein reduces small intestinal growth and lamina propria cell density in early weaned pigs. J Nutr 2000;130:21-6. |
| 09. | Jiang R, Chang X, Stoll B et al. Dietary plasma protein is used more efficiently than extruded soy protein for lean tissue growth in early-weaned pigs. J Nutr 2000;130:2016-9. |
| 10. | Kats LJ, elssen JL, okach MD et al. The effects of spray-dried blood on growth performance of the early-weaned pig. J Anim Sci 1995;72:2860-9. |
| 11. | Thomson JE, Jones EE, Eisen EJ. Effects of spray-dried porcine plasma protein on growth traits and nitrogen and energy balance in mice. J Anim Sci 1995;73:2340-6. |
| 12. | Weaver EM, Strohbehn RE, Yoder R, Burleson G. The immunomodulatory effects of plasma fractions in healthy mice. Unpublished 2001. |
| 13. | De Rodas BZ, Sohn KS, Maxwell CV, Spicer LJ. Plasma protein for pigs weaned at 19 to 24 days of age: effect on performance and plasma insulin-like growth factor I, growth hormone, insulin, and glucose concentrations. J Anim Sci 1995;73:3657-65. |
| 14. | Rhoads JM, Chen W, Gookin J et al. Arginine stimulates intestinal cell migration through a focal adhesion kinase dependent mechanism. Gut 2004; 53:514-22. |
| 15. | Hunt EL, Fu Q, Armstrong M et Al. Oral bovine serum concentrate improves cryptosporidial enteritis in calves. Pediatric Nutrition 2001; In pres.. |
| 16. | Bosi P, Casini L, Finamore A et al. Spray-dried plasma improves growth performance and reduces inflammatory status of weaned pigs challenged with enterogtoxigenic Escherichia coli K88. J Anim Sci 2004;82:1764-72. |
| 17. | Nofrarias M, Manzanilla EG, Pujols J et al. Effects of spray-dried porcine plasma and plant extracts on intestinal morphology and on leukocyte cell subsets of weaned pigs. J Anim Sci 2006;84:2735-42. |
| 18. | Brenner IK, Natale VM, Basiliou P, Moldoveanu AL, Shek PN, Shephard RJ. Impact of three different types of exercise on components of the inflammatory response. Eur J Appl Physiol Occup Physiol 1999;80:452-60. |
| 19. | Jeukendrup AE, Vet-Joop K, Sturk A et al. Relationship between gastro-intestinal complaints and endotoxaemia, cytokine release and the acute-phase reaction during and after a long-distance triathlon in highly trained men. Clin Sci (Colch) 2000 Jan; 98(1):47-55 2000;98:47-55. |
| 20. | Maclyntyre DL, Reid WD, McKenzie DC. Delayed muscle soreness. The inflammatory response to muscle injury and its clinical implications. Sports Med 1995;20:24-40. |
| 21. | Mackinnon LT. Chronic exercise training effects on immune function. Med Sci Sports Exerc 2000 Jul; 32 (7 Suppl): S369-7632:S369-S376. |
| 22. | Ostrowski K, Hermann C, Bangash A, Schjerling P, Nielsen JN, Pdersen BK. A trauma-like elevation of plasma cytokines in humans in response to treadmill running. J Physiol 1998;512:889-94. |
| 23. | Pedersen BK, Ostrowski K, Rhode T, Bruunsgaard H. The cytokine response to strenuous exercise. Can J Physiol Pharmacol 1998;76:505-11. |
| 24. | Toft AD, Jensen LB, Bruunsgaard H et al. Cytokine response to eccentric exercise in young and elderly humans. Am J Physiol Cell Physiol 2002;283:C289-C295. |
| 25. | Weinstock C, Konig D, Harinschmarcher R, Keul J, Berg A, Northoff H. Effect of exhaustive exercise strees on the cytokine response. Med Sci Sports Exerc 1197;29:345-54. |
| 26. | Spate U, Schulze PC. Proinflammatory cytokines and skeletal muscle. Curr Opin Clin Nutr Metab Car 2004;7:265-9. |
| 27. | Ji SQ, Neustrom S, Willis GM, Spurlock ME. Proinflammatory cytokines regulate myogenic cell proliferation and fusion but have no impact on myoutube protein metabolism or stress protein expression. J Interferon Cytokine Res 1998;18:879-88.
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| 28. | Johnson R. Inhibition of growth by pro-inflammatory cytokines: an integrated view. J Anim Sci 1997:75:1244-55.
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| 29. | McCracken BA, Spurlock ME, Roos MA, Zuckermann FA, Gaskins HR. Weaning anorexia may contribute to local inflammation in the piglet small intestine. J Nutr 1999;129:613-9. |
| 30. | Rhodas JM, Argenzio RA, Chen W, Fu Q, Weaver EM, Graves LM. L-Arginine (ARG) and serum stimulate intestinal restitution by distinct signaling pathways. Gastroenterology 2000;118:4356. |
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| Lysozyme |
Lysozyme (Lz) is an enzyme of 129 amino acids found in tears, nasal secretions, animal tissues, organs, and serum as well as milk and cervical mucus. The major commercial source of Lz is avian egg white and constitutes about 0.5 % of egg albumin. Lysozyme attacks the cell wall polysaccharides of different bacterial species, especially gram positive infectious organisms such as Staphylococci and Streptococci species and kills them. Gram negative bacterial species such as E.coli and Salmonella are also destroyed by Lz, however, they are not as susceptible as Gram positive bacteria. In humans, Lz is used to treat both viral and bacterial infections.
It has analgistic properties and has been used to potentiate antibiotic therapy. EDTA-tris-lysozyme solutions are effective in the treatment of coliform infections of the bladder in humans. Other benefits of Lz is that it neutralizes acIdic substances released during inflammatory processes and so demonstrates anti inflammatory activity. It also helps in wound healig, phagocytosis and regression of degenerative and necrotic process. Lysozyme-mediated decrease of mast cell degranulation leads to reduction of histamin release and a subsequent anti-edema effect.
It has been suggested that polysaccharides, glycopropteins and glycolipids of the cell membrane can bind Lz in a substrate-specific way. This has led to the hypothesis that Lz has a regulatory function in membrane-dependent cellular processes and in protection against membrane abnormalities associated with neoplastic transformation.
In human investigations, fifteen full-term and 18 premature infants were given egg-white Lz in the milk formula (10 mg/100 ml) from the 1st to the 8th week of age as substitute for the Lz in breast milk (2mg/ml) to stimulate the production of immunoglobins. Thirteen full-term and thirteen premature artificially-fed infants, as well as 20 breast-fed infants, were followed as controls.
Assuming that the infants consumed daily 600-900 ml of milk formula, daily intake of Lz in this study was 60-90 mg. The infants did not show ill-effects. No difference in the production of serum immunoglobulin’s between the Lz group and control group was seen. Secretory IgA was found in stool filtrates of full-term Lz fed infants as well as in breast-fed controls.
In other groups, full-term controls fed artificially without lysozyme, premature controls fed artificially with Lz, only traces of secretory IgA were detected in stool filtrates. Lysozyme feeding partly substituted for passive transfer of secretory IgA from maternal milk. No anitbodies were found in serum of Lz fed children thus indicating the safe use of Lz for humans.
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| Probiotics |
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The term Probiotic literally means 'for life' The World Health organization (WHO) defines a probiotic as live organisms which when taken in adequate amounts confer health benefits on the host. At the time of consumption the organisms should be viable and capable of surviving stomach acidity, gastric and duodenal proteolytic enzymes and adhere to the endothelial colon mucosal cells. There are literally hundreds of different genera and considerably more species of probiotic bacteria of which the Lactobacilli and Bifidobacteria make up the majority of gut microflora.
The health associated benefits of probiotics in food has been known for ages and include:
- Enhanced intestinal immunity. Some 70 % of the immune system cells reside within the colon in a layer of lymphoid tissue called the lamina propia. The friendly bacteria stimulate these cells to promote both local and systemic protection against pathogens.
- Protection against Helicobacter pylori bacteria known to cause ulcers and colon cancer particularly in children.
- Positive effect on diarrhea, inflammatory bowel disease and irritable bowel syndrome.
- Reduction of fever, coughing and runny noses in infants.
- T cell (a population of lymphocytes) response to certain viral respiratory infections.
- T cell production of TNF alpha upon exposure to certain viruses.
- Enhanced phagocytosis by monocytes and neutrophils.
- Stimulation of innate immune response and increased resistance to pathogens.
- Reduced risks of eczema in infants, allergies and arthritis.
- Cholesterol reduction.
- Anti aging.
The positive actions of probiotics are tied to specific strains and specific doses. Thus the primary goal with any probiotic product is to deliver the right bacteria in ideal numbers to the right place in the body. To promote the growth and activity of friendly bacteria a synbiotic combination of probiotics and inulin a prebiotic (see review prebiotics) are offered in IMUNOBIOTICS. Prebiotics prepare the environment for probiotics to flourish and work at their best.
Reference:
01. FAO/WHO. 2001. Health and nutritional properties of probiotics in food including powder milk with live lactic acid bacteria.www.who.int/foodsafety/publications/fs_management/en/probiotics.pdf.
02. Trueman S. Are you pro-biotic? Bugs are finding their way into our food and that's a good thing. Nerac Analyst, March 2007. www.nerac.com/news/marketplace-review/bugs, accessed April 16, 2007.
03. Floch MH, et al. Recommendations for probiotic use. J Clin Gastroenterol 2006 Mar;40(3):275-8.
04. Marteau P, et al. Cellular and physiological effects of probiotics and prebiotics. Mini-Rev Medicinal Chem 2004;4:889-896.
05. Sanders ME. Probiotics: considerations for human health. Nutr Rev 2003;61:91-99.
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06. FAO 2002. Guidelines for the evaluation of probiotics in food. www.fermented-foods.net/wgreport2.pdf
07. Castagliuolo I, et al. Beneficial effect of auto-aggregating Lactobacillus crispatus on experimentally induced colitis in mice. FEMS Immunol Med Microbiol 2005 Feb 1;43(2):197-204.
08. Simakachorn N, et al. Clinical evaluation of the addition of lyophilized, heat-killed Lactobacillus acidophilus LB to oral rehydration therapy in the treatment of acute diarrhea in children. J Ped Gastroenterol Nutr 2000;30:68-72.
09. Zhang L, et al. Alive and dead Lactobacillus rhamnosus GG decrease tumor necrosis factor-alpha-induced interleukin-8 production in Caco-2 cells. J Nutr 2005 Jul;135(7):1752-6.
10. Cruchet S, et al. Effect of the ingestion of a dietary product containing Lactobacillus johnsonii La1 on Helicobacter pylori colonization in children. Nutrition 2003 Sep;19(9):716-21.
11. Gotteland M, et al. Effect of Lactobacillus ingestion on the gastrointestinal mucosal barrier alterations induced by indometacin in humans. Aliment Pharmacol Ther 2001 Jan;15(1):11-7.
12. Peng GC, Hsu CH. The efficacy and safety of heat-killed Lactobacillus paracasei for treatment of perennial allergic rhinitis induced by house-dust mite. Pediatr Allergy Immunol 2005 Aug;16(5):433-8.
13. Rachmilewitz D, et al. Toll-like receptor 9 signaling mediates the anti-inflammatory effects of probiotics in murine experimental colitis. Gastroenterology 2004 Feb;126(2):520-8.
14. Asahara T, et al. Probiotic bifidobacteria protect mice from lethal infection with Shiga toxin-producing Escherichia coli O157:H7. Infect Immun 2004, 72(4):2240-7.
15. Tallon R, et al. Strain- and matrix-dependent adhesion of Lactobacillus plantarum is mediated by proteinaceous bacterial compounds. J Appl Microbiol. 2007 Feb;102(2):442-51.
16. Foligne B, et al. Correlation between in vitro and in vivo immunomodulatory properties of lactic acid bacteria. World J Gastroenterol 2007; 14;13(2):236-43.
17. D'Aimmo MR, et al. Antibiotic resistance of lactic acid bacteria and Bifidobacterium spp. isolated from dairy and pharmaceutical products. Int J Food Microbiol 2007 Apr 1;115(1):35-42. Epub 2007 Jan 2.
18. Sanders ME, et al. Performance of commercial cultures in fluid milk applications. J Dairy Sci 1996 Jun;79(6):943-55.
19. Olivares M, et al. Antimicrobial potential of four Lactobacillus strains isolated from breast milk. J Appl Microbiol 2006 Jul;101(1):72-9.
20. Foligne B, et al. Probiotics in IBD: mucosal and systemic routes of administration may promote similar effects. Gut 2005 May;54(5):727-8.
21. Daniel C, et al. Selecting lactic acid bacteria for their safety and functionality by use of a mouse colitis model. Appl Environ Microbiol 2006 Sep;72(9):5799-805.
22. Masco L, et al. Culture-dependent and culture-independent qualitative analysis of probiotic products claimed to contain bifidobacteria. Int J Food Microbiol. 2005 Jul 15;102(2):221-30.
23. Pot B. Personal communication.
24. Weizman Z, et al. Effect of a probiotic infant formula on infections in child care centers: comparison of two probiotic agents. Pediatrics 2005 Jan;115(1):5-9.
25. O'Mahony L, et al. Lactobacillus and bifidobacterium in irritable bowel syndrome: symptom responses and relationship to cytokine profiles. Gastroenterology 2005 Mar;128(3):541-51.
26. Talarico TL, et al. Production and isolation of reuterin, a growth inhibitor produced by Lactobacillus reuteri. Antimicrob Agents Chemother. 1988 Dec;32(12):1854-8.
27. Guarner F, et al. Should yoghurt cultures be considered probiotic? Br J Nutr. 2005 Jun;93(6):783-6.
28. Klaenhammer TR, et al. Genomic features of lactic acid bacteria effecting bioprocessing and health. FEMS Microbiol Rev. 2005 Aug;29(3):393-409.)
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| Lactoferrin |
Lactoferrin is a glycoprotein and a member of transferrin family capable of binding and transferring iron (Fe3+ ions). It is therefore an iron chelator. Lactoferrin is found in small quantities in milk whey and the exocrine secretions of mammals. It is released from neutrophil granules during inflammation and is the main source of lactoferrin in blood plasma. lactoferrin is considered a multifunctional or multi-tasking protein that influences the immune system at the cellular (lymphocytes, phagocytes, neutrophils, natural killer cells) and molecular (cytokines, interleukins, tumor necrosis factor, granulocyte-monocyte stimulating factor) levels. It plays several biological roles and has antibacterial, antiviral, anti fungal, anti-inflammatory, antioxidant and immunomodulatory activities. It affects growth and proliferation of a variety of infectious agents both Gram- positive (Streptococcus pyogenese, Staphylococcus aureus, Listeria monocytogenese) and Gram negative (E. coli, Pseudomonas aeruginosa, Yersinia enterocolica) and other bacteria. It is of interest that while lactoferrin inhibits growth of iron-dependant bacteria, in certain cases in contrast it may serve as an iron donor, and in this manner support the growth of some beneficial bacteria with low iron demands such as Lactobacillus and Bifidobacterium species.
The bacterial growth inhibitory activity of lactoferrin due to its iron binding properties makes it of grate importance in SUPPRETION OF BACTERIAL BIOFILM FORMATION discussed bellow.
TRANSFERRIN: Transferrin like lactoferrin is an iron binding glycoprotein that constitutes 7.5 to 8% of bovine immunoglobulin (see review bovine immunoglobulin). Similar to lactoferrin, it inhibits multiplication and growth of certain viral, bacterial and fungal organisms by iron inhibition. This property of transferrin has been known for a long time and was shown by this writer in 1968 to inhibit mycobacterial growth as part of his Ph.D. dissertation and by subsequent publications.
BIOFILMS:Antimicrobial factors constitute one arm of the innate immune system which protect
mucosal surfaces from bacterial infections. These factors can rapidly kill bacteria and micro organisms deposited on mucosal surfaces and prevent acute, invasive infections. In many chronic infections, however, bacteria live in complex structures called biofilms. Biofilms are collections of microbial communities encased by a matrix of negatively charged polysaccharides held together by positively charged calcium, magnesium and ironic ions. Within the biofilm the bacteria are protected from immune attack, antibiotics, UV radiation, dehydration, toxic metals and salinity. Further, the matrix allows for free intracellular interactions, exchange of genetic materials, necessary metabolites and nutrients. Given these facts, it is therefore clear that, disruption of biofilm formation from free living independent organisms is of paramount importance in controlling infections. Ample evidence exists that iron binding components of the innate immune system, namely lactoferrin and transferrin (see reviews) fulfill this function. Lactoferrin stimulates twitching, a specialized form of surface motility, causing the bacteria to wander across the surface instead of forming cell clusters and biofilms.
Other chelators such as ethylenediaminetetraacetic acid (EDTA) induce dispersal and killing of certain biofilms such as Staph and Pseudomonas species such as P.aeruginosa an exceptionally vicious and devastating infection. The combination of EDTA and antibiotics are effective biofilm disrupters.
Immunoglobulins (see reviw immunoglobulins), probiotics (see review probiotics and prebiotics-inulin ) and enzymes are other adjunctive therapies that help fight infections and biofilm formation.
REFERENCES:
Lactoferrin References:
| 01. | Adelerova A. Lactoferrin : A review , Veterirarnin Medicina. 2008; 53: 457-468. |
| 02. | Brock, J.H. Lactoferrin in human milk: its role in iron absorption and protection against enteric infection in the newborn infant. Archives of Disease in childhood. 1980; 46: 231-240. |
| 03. | Petschow B.W., Talbott R.D., Batman R.P. Ability of Lactoferin to Promote growth of Bifidobacterium species invitro is independent of receptor binding capacity and iron saturation level. J. Medical Microbiology. 1999; 48: 541-549. |
| 04. | Sherman M.P., Bennett S.H., Hwang, F.F. Yu C. Neonatal small bowel epithelia: enhancing anti-bacterial defense with Lactoferrin and Lactobacillus GG. Biomedicals. 2004; 17: 285-289. |
| 05. | Legrand, D. (2003) Lactoferrin and host defense: an overview of its immuno-modulating and anti-inflammatory properties. Sixth International Conference on Lactofferin: Structure, Function and Applications - Capri, 5-9 May, 2003. |
| 06. | Artym, J.: M.: Paprocka, M. & Kruzel, M.L. (2003) Orally administered lactoferrin restores humoral immune response in immunocompromise mice. Immunlogy Letters 89(1): 9-15. |
| 07. | Kuhara, T: Ligo , T. Ushida, Y.:Sekine, K.; Terada, N. Okamura, H. & Tsuda, H. (2001) Orally administered lactoferrin exerts an antimetastatic effects and enhances production of IL-18 in the intestinal epithelium. Nutrition and Cancer 38: 192-199. |
| 08. | Adamik B,Zimecki M, Wlasczyk A, et al. Lactoferrin effects on the in vitro immune response in critically ill patients.Arch Immunol Ther Exp (Warcz). 1998; 46:169-176 |
| 09. | Baveye S Elass E, Mazurier J, et al. Lactoferrin: a multifunctional glycoprotein involved in the modulation of the inflammatory process. Clin Chem Lab Med.1999; 1999; 37:281-286. |
| 10. | Britigan BE, Serody JS, Cohen MS. The role of lactoferrin as an anti-inflammatory molecule. Adv Exp Med Biol. 1994; 357:143-156. |
| 11. | Ikeda M, Nozak A, Sugiyama K , et al. Characterization of antiviral activity of lactoferrin against hepatitis C virus infection in human cultured cells. Virus Res. 2000; 66:51-63. |
| 12. | Levay PF, Viljoen M. Lactoferrin: A general review. Haemtologica. 1995; 80: 252-267. |
| 13. | Lonnerdal B, Iyer S. Lactoferrin: molecular structure and biological function. Annu Rev Nutr . 1995; 15:93-110. |
| 14. | Swart PJ, Kuipers EM, Smit C, et al. Lactoferrin. Antiviral activity of lactoferrin. Adv Exp Med Biol. 1998; 443:205-213. |
| 15. | Trumpler U, Straub PW, Rosenmund A. Antibacterial prophylaxis with lactoferrin in neutropenic patients.Eur J Clin Microbiol Infect Dis.1989; 8:310-313. |
| 16. | Vorland LH. Lactoferrin: a multifunctional glycoprotein. APMIS. 1999; 107:971-981. |
| 17. | Vorland LH.Ulvatne H, Andersen J, et al. Antibacterial effects of lactoferrin B. Scand J Infect Dis.1999; 31:179-184. |
| 18. | Zimecki M, Wlaszczyk A, Cheneau P, et al. Immunoregulatory effects of a nutritional preparation containing bovine lactoferrin taken orally by healthy individuals. Arch Immunol Ther Exp (Warcz). 1998; 46:231-240. |
Transferring References:
| 01. | Martin CM, Jandl JH. Inhibition of virus multiplication by transferrin in M.J. Seven and L. A. Johnson, Editors. Metal binding in medicine, 335 J.B. Lippincott, Philadelphia, 1960. |
| 02. | Martin CM, Jandl JH, Findland M. Enhancement of acute bacterial infections in rats and mice by iron and their inhibition by human transferrin . J Infec Disease. 1963; 112: 158-163. |
| 03. | Youdim S. In vivo and in vitro action of ionic iron and chelating agents on Mycobacterial growth. Ph. D. dissertation 1968 |
| 04. | Youdim S. In vitro effect of iron salts and chelating agents on serum tuberculostasis. Am. Rev. Resp Dis.1969; 99:925. |
| 05. | Sutcliffe MC, Savage, AM. Transferrin- dependent growth inhibition of yeast-phase Histoplasma capsulatum by human serum and lymph. J.Infec Disease.1980; 142: 209-
219. |
| 06. | Thomas HL, Biggers CJ, Simonton PR. Bacteriostatic inhibition of Klebsiella pneumoniae by three human transferrins. Annals Human Biol. 1977; 4: 281-284. |
Bioflm References:
| 01. | Singh PK, Parsek MR, Greenberg EP, Welsh MJ. A component of innate immunity prevents bacterial biofilm development. Nature.2002; 30: 417 (6888): 552-555. |
| 02. | Arsalan SY, Leung KP, Wu CD. The effect of lactoferrin on oral bacterial attachment. Oral Microbiol Immunol.2009; 24 (5):411-416.
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| 03. | Goller CC, Romeo T. Environmental influences on biofilm development. Curr Top Microbiol Immunol. 2008; 322: 37-66.
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| 04. | Weinberger ED. Suppression of bacterial biofilm formation by iron limitation. Med Hypotheses 2004; 63: 863-865. |
| 05. | Otto M. Staphylococcal biofilms. Curr Top Microbiol Immunol. 2008; 322:207-228. |
| 06. | Costerton JW, Montanaro L, Arciola CR. Biofolm in implant infections: its production and regulation. 2007; 9: 757-763 |
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| D-Ribose |
D-Ribose (or simply ribose) is a simple, 5-carbon monosaccharide, or pentose sugar. It is used by all the cells of the body and is an essential compound in energy metabolism. Ribose also provides the structural backbone of our genetic material, DNA and RNA, certain vitamins and other important cellular compounds.
Who needs supplemental ribose?Everyone needs ribose. It is an essential ingredient in stimulating natural energy production. Research has shown that ribose promotes cardiovascular health, reduces cardiac stress associated with strenuous activity and helps athletes reach new heights. Ribose helps hearts and muscles maintain healthy energy levels, and it accelerates energy recovery when tissues are stressed by strenuous exercise, overwork, or disease. Whether you are a trained athlete, a weekend warrior or are concerned about your cardiovascular health, ribose may help give the energy boost your body needs.
How is ribose made in the body?All the necessary compounds for life are made in the body through a series of complicated biochemical metabolic pathways. Ribose is no different. In the body, ribose is made from glucose (a simple 6-carbon sugar) through a metabolic pathway called the Pentose Phosphate Pathway (PPP) or Hexose Monophosphate Shunt (HMS). Unfortunately, in heart and muscle cells important enzymes that regulate the activity of this pathway are lacking. As such, forming ribose in heart and muscle cells is a slow process. This delay in ribose synthesis in heart and muscle tissues also delays energy recovery when energy pools have been depleted by disease or exercise.
How does the body derive cellular energy from ribose?The physiologically functional form of ribose, called 5-phosphoribosyl-1-pyrophosphate (PRPP), regulates the metabolic pathway that synthesizes energy compounds in all living tissue. This pathway is called the Purine Nucleotide Pathway (PNP). If PRPP is not available in sufficient quantity, energy synthesis slows and tissue recovery is delayed.
How does taking supplemental ribose aid in increasing cellular energy?If the cellular energy pool is depleted by disease, overwork, or exercise it must be replaced. PRPP is required to stimulate the metabolic pathway used by the body to replenish these energy pools. Supplemental ribose bypasses the slow and rate limiting Pentose Phosphate Pathway, forms PRPP very quickly, and accelerates the process of energy synthesis.
What will ribose do for someone concerned about cardiovascular health?
Numerous medical studies conducted in the U.S. and Europe have shown that energy levels in the heart can be dramatically lowered by exercise, decreased blood flow associated with certain cardiac diseases, or by changes in normal cellular energy metabolism. Depleted cardiac energy stores may be associated with increased cardiac stress, reduced blood flow to the periphery of the body, fatigue, and decreased exercise tolerance. Ribose is the key nutrient for quickly restoring cardiac energy.
What is the recommended daily dosage of ribose?For energy enhancement, ½ to 1 teaspoon (about 2 – 5 grams) is generally adequate. Ribose is mildly sweet and completely soluble. It mixes easily with your favorite juice, milk or other cold foods to maximize athletic performance, or to keep energy pools high during strenuous activity, slightly larger doses may be required. Ribose should be taken just before and just after exercise or activity. For extended exercise, an additional 1 – 2 grams per hour of exercise or activity may be helpful.
Are there any side effects associated with taking ribose?There are two known side effects of taking ribose in doses of 10 grams or more on an empty stomach. The first is a transient hypoglycemia (low blood sugar) that can be eliminated by taking larger doses of ribose with other carbohydrates (such as in juice). The second side effect that may occur in some individuals is loose stools. This side effect has only been reported when very large doses, greater than 10 grams, are taken. Total daily intake of ribose should be limited to 20 grams, or approximately 4 rounded teaspoonfuls. Ribose should be taken in doses up to 5 grams (approximately 1 rounded teaspoon) at a time. Multiple 5- gram doses separated by 30 – 45 minutes can be taken without side effects.
What will ribose do for someone who exercises on a regular basis?Scientific research shows that three or four workouts per week may not allow enough rest time between sessions for heart and muscle energy pools to return to normal levels. Taking ribose shortens the time needed by heart and muscle tissue to replace energy that is lost through vigorous exercise. Keeping energy pools full helps to keep hearts and muscles in good physiological condition, increase power and endurance, and reduce fatigue. Recent research has also shown that ribose supplementation during exercise reduces free radical formation and lowers cardiac stress associated with hypoxia.
Does ribose work with creatine or other supplements?Ribose can increase the effect of creatine and other energy supplements by keeping the energy pool at full capacity. Creatine works by recycling energy that is already present in the tissue. Another supplement, carnitine, aids in fatty acid metabolism. Others, such as pyruvate and coenzyme Q10, also help to recycle energy. None of these other supplements, however, help to actually make the energy compounds the cell needs to maintain a healthy energy pool. Only ribose performs this important metabolic function. Unless there are adequate levels of energy to work with, no other supplement can be fully effective. Keep this in mind: Ribose helps the body actually make energy, while other supplements may help the body use energy more efficiently.
Why is the use of ribose on the rise?Traditionally, ribose has been very expensive to produce making it difficult to offer as a nutritional supplement. New technology has brought production costs down. Ribose is safe and proven effective by many clinical and laboratory studies. Over 70 scientific publications describe the beneficial effects of ribose in hearts and muscles.
Energy Claims
- Ribose speeds energy recovery.
- Ribose increases energy reserves.
- Ribose builds ATP in heart and muscle.
- Ribose maintains healthy energy levels in heart and muscle.
References:?
1. Pauly DF, CJ Pepine. D-ribose as a supplement for cardiac energy metabolism. J Cardiovasc Pharmacol Therapeut, 5(4):249-258, 2000.?
2. Wagner DR, U Gresser, N Zollner. Effects of oral ribose on muscle metabolism during bicycle ergometer in AMPD-deficient patients. Ann Nutr Metab, 35:297-302, 1991.?
3. Zarzeczny R, JJ Brault, KA Abraham, CR Hancock, RL Terjung. Influence of ribose on adenine salvage after intense muscle contractions. J Appl Physiol, 91:1775-1781, 2001.
4. Brault JJ, RL Terjung. Purine salvage to adenine nucleotides in different skeletal muscle fiber types. J Appl Physiol, 91:231-238, 2001.?
5. Gallagher PM, DL Williamson, MP Godard, J Witter, SW Trappe. Effects of ribose supplementation on adenine nucleotide concentration in skeletal muscle following high-intensity exercise. Med Sci Sport Exc, 33(5 suppl), 2001.?
6. Skadhauge-Jensen L, J Bangsbo, Y Hellsten. Availability of ribose is limiting for ATP reynsthesis in human skeletal muscle after high-intensity training. Med Sci Sport Exc, 33(5 suppl), 2001.?
7. Wagner DR, N Zollner. McArdle's disease: Successful symptomatic therapy by high dose oral administration of ribose. Klin Wochenschr 69:92, 1991.?
8. Zollner N, S Reiter, M Gross, D Pongratz, CD Reimers, K Gerbitz, I Paetzke, T Deufel, G Hubner. Myoadenylate deaminase deficiency: Successful symptomatic therapy by high dose oral administration of ribose. Klin Wochenschr 64:1281-1290, 1986.?
9. Patten BM. Beneficial effect of D-ribose in patient with myoadenylate deaminase deficiency. The Lancet, May:1071, 1982.
Cramping and Soreness Claims
• Ribose relieves post-exertional muscle cramping and soreness.
References:
1. Wagner DR, N Zollner. McArdle's disease: Successful symptomatic therapy by high dose oral administration of ribose. Klin Wochenschr 69:92, 1991.?
2. Zollner N, S Reiter, M Gross, D Pongratz, CD Reimers, K Gerbitz, I Paetzke, T Deufel, G Hubner. Myoadenylate deaminase deficiency: Successful symptomatic therapy by high dose oral administration of ribose. Klin Wochenschr 64:1281-1290, 1986.?
3. Wagner DR, U Gresser, N Zollner. Effects of oral ribose on muscle metabolism during bicycle ergometer in AMPD-deficient patients. Ann Nutr Metab, 35:297-302, 1991.
Heart and Quality of Life Claims
- Quality of life is enhanced by taking ribose.?• Ribose increases tolerance to cardiac stress.?• Ribose improves exercise tolerance and physical function.
- Ribose provides healthy levels of cardiac energy needed to maintain normal heart function.
References:
1. Omran H, S Illien. Ribose improves myocardial function and quality of life in congestive heart failure patients. J Mol Cell Cardiol, 33(6):A173, 2001.?
2. Pauly DF, CJ Pepine. D-ribose as a supplement for cardiac energy metabolism. J Cardiovasc Pharmacol Therapeut, 5(4):249-258, 2000.?
3. Illien S, H Omran, D MacCarter, JA St. Cyr. Ribose improves myocardial function in congestive heart failure. FASEB J, 15(5):A1142, 2001.
4. Pliml W, T von Arnim, A Stablein, H Hofmann, H-G Zimmer, E Erdmann. Effects of ribose on exercise-induced ischemia in stable coronary artery disease. The Lancet, 340:507-510, 1992.?
5. Grant GF, RW Gracy. Therapeutic nutraceutical treatments for osteoarthritis and ischemia. Exp Opin Ther Patents, 10(1):1-10, 2000.
Physical Performance Claims
- Ribose improves physical performance.?• Ribose increases athletic performance.
References:
1. Williamson DL, MP Goddard, SW Trappe. Effects of ribose supplementation on performance during repeated high-intensity cycle sprints. Med Sci Sport Exc, 33(5 suppl), 2001?
2. Van Gammeren D, D Falk, J Antonio. The effects of four weeks of ribose supplementation on body composition and exercise performance in healthy, young, male recreational bodybuilders: A double-blind, placebo controlled trial. Cur Therapeut Res, 63(8):486-495. 2002.?
3. Patten BM. Beneficial effect of D-ribose in patient with myoadenylate deaminase deficiency. The Lancet, May:1071, 1982.
Metabolic Stress Claims
- Ribose decreases free radical formation during exercise.
- Ribose increases the hypoxic threshold of tissue.
- Ribose increases cardiac efficiency and lowers stress during exercise.
References:?
1. Seifert JG, A Subudhi, M-X Fu, KL Riska, JC John. The effects of ribose ingestion on indices of free radical production during hypoxic exercise. Free Rad Biol Med, 33(Suppl 1):S269, 2002.
2. Segal S, J Foley. The metabolism of D-ribose in man. J Clin Invest, 37: 719-735, 1958.?
3. Bierman EL, EM Baker, IC Plough, WH Hall. Metabolism of D-ribose in diabetes mellitus. Diabetes, 8(6):455-458, 1959.
4. Steinberg T, RL Poucher, RK Sarin, RB Rees, G Gwinup. Oran administration of D-ribose in diabetes mellitus. Diabetes, 19(10):11-16, 1970.?
5. Zimmer H-G, H Ibel. Ribose accelerates the repletion of the ATP pool during recovery from reversible ischemia of the rat myocardium. J Mol Cell Cardiol, 16:863-866, 1984
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| Coenzyme Q10 |
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Coenzyme Q10, Acetyle L-Carnitine, L-Carnosine, Cretine Monohydrate, Alpha Lipoic Acid and D-Ribose (see review D-Ribose) and Ascorbic Acid are all components of Maxi Energy. These ingredients contribute to enhanced mitochondrial function and increased cellular energy. Mitochondria are small membrane bound organelles found in most eukaryotic cells. They are known as cellular power plants because they generate most of the cell’s supply of adenosine triphosphate (ATP) used as a source of chemical energy.
Coenzyme Q10 is a vitamin like substance manufactured by all cells in the body. It also plays a crucial role in energy production and is one of body’s most powerful antioxidants that protect the mitochondria and cell membranes against free radicals and oxidative damage. CoQ10 may also boost immune function, prevent proliferation of cancer cells and prevent heart disease due to atherosclerosis. Consumption of many anti cholesterol statins such as Pravachol, Lipitor, Mevacor and zocor cause CoQ10 deficiency. It is therefore suggested that patients taking these drugs should receive CoQ10 supplementation. Other benefits of CoQ10 are neuro-protective effect on brain cells and possible amelioration of Parkinson’s disease, production of the high-energy phosphate, adenosine triphosphate (ATP) and other life sustaining functions.
Alpha Lipoic Acid (ALA) is a fatty acid found naturally inside every cell of the body. It plays a crucial role in energy producing structures of the cells. ALA is a strong and versatile antioxidant. It may also improve immune function due to its ability to promote secretion of interleukin-2 (IL-2). Interleukin-2 is an immune modulator released by a population of T lymphocytes in response to antigenic stimulation. It increases proliferation and activity of other T and B lymphocytes. ALA is also able to recycle other antioxidants, including vitamins C and E, CoQ10 and glutathione.
Acetyle L-Carnitine (ALC) is a modified amino acid which like alpha lipoic acid (ALA) enhances energy production in the cells by carrying fatty acids into mitochondria where it is converted into energy. ALC may also be of value to treat depressed male sexual function, mood, physical and mental fatigue. While by itself, it is not an antioxidant, ALC works well in combination with ALA to improve both the activity and cognitive function of old rats. Experimental work showed that after just a month, older rats whose diet was supplemented with these two compounds were about twice as active as control rats, which remained largely inactive. The researchers noted that the brain of the research animals looked better and they were full of energy. “Every thing we looked at looks more like a young animal. Supplementation with ALA and ALC also improver both spatial and temporal memory. Pictures of brain cells show less decay in old rats fed a supplemented diet. It appears that these compounds can mask the metabolic problems caused by cellular aging and the natural oxidative process the researchers wrote. The implications of these findings suggest ALA and ALC regenerate aging cells and delay senescence.
Creatine Monohydrate is a nitrogenous organic acid produced in the body from the amino acids argentine, glycine and methionine. Creatine plays a vital role in cellular energy production as creatine phosphate or phosphocreatine in regenerating adenosine triphosphate (ATP) in skeletal muscle. Oral administration of 2-5 grams of creatine per day increases muscle stores and provides significant gain in physical performance in high-intensity exercise and intense training. Phosphocreatine is also used to help generate cellular energy for muscle contractions and acts as a storage form of quick energy. Creatin has been demonstrated to cause moderate increases in strength in people with a variety of neuromuscular and neurodegenerative disorders and may be of use for the treatment of diseases such as arthritis, Parkinson’s disease, Huntington’s disease, muscular dystrophy and mitochondrial diseases. There is also experimental evidence that daily intake (about 5 grams) of creatine improves cognitive ability and memory compared to controls.
L-Carnosine is a dipeptide of the amino acids beta-alanine and histidine highly concentrated in human muscle cells (myocytes) and brain tissues. It is a very powerful anti oxidant and has been proven to scavenge reactive oxygen species. L-carnosine is a modulator of enzyme activity and a heavy metal chelator (see review lactoferrim). Numerous experimental studies indicate L- carnosine protects against radiation damage, improves heart function, promotes wound healing, regenerates and rejuvenates cells approaching senescence (the end of the life cycle of dividing cells) and protects cell membranes from oxidative damage. It is therefore referred to as one of the nutrients for longevity with amazing anti-aging properties. L-carnosine is touted as the anti aging nutrient because of its favorable effects on inhibiting the formation of age inducing substances called “advanced glycation end products’ (AGEs). Glycosylation is the oxidation of proteins which occur when sugar molecules attach to proteins and block their normal metabolic function resulting in cross-linking of proteins. AEGs are abnormal cross-linked and oxidized proteins which are implicated in loss of cell function, genome integrity and accelerated aging. Studies suggest that L- carnosine protects DNA and proteins from cross-linking. Moreover, it also binds to already formed AEGs and inactivates them.
Research has shown that resistance training is associated with periods of intracellular hypoxia (lack of oxygen) and low intracellular PH. L-carnosine acts as a buffer in the muscle keeping PH levels from falling during extensive exercise such as bodybuilding. In a controlled study it was shown that muscle carnosine in bodybuilders was twice that in controls and represented a 20% contribution to muscle buffering capacity. L-carnosine is found in especially high concentrations in nerve cells (neurons) and the brain and is shown to have neuro protective activity. In fact carnosine has shown to reduce and prevent cell damage by beta amyloid, a substance found in the brain of Alzheimer sufferers. A small 2002 study in autistic children reported that over an eight week period, L-Carnosine improved behavior and communications by 16%. Social interaction improved by 27% and, in just four weeks, parents reported an overall improvement that more than doubled through the length of the study. Other benefits of L- Carnosine are retarding skin aging, boost immunity, prevention of atherosclerosis, joint inflammation, anti cancer activity and a super antioxidant.
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| Prebiotics |
INULIN- Fructo-oligofructose and fructo-oligosaccharides (FOS).
Probiotics are a species of health associated intestinal bacteria (see review probiotics) that work synergistically when combined with prebiotics such as inulin. Prebiotics prepare the environment for probiotics to flourish and work at their best.
Inulin/FOS is found in many common fruits and vegetables and can readily be extracted from chicory roots. Inulin is a fiber and sweetener that is used extensively in sugar free, low fat and low calorie carbohydrate foods and beverages.
Clinical studies implicate inulin in a range of whole body benefits that include:
- Boosting levels of benefitial bacteria in the colon and enhance digestive health.
- Stimulate mucosal immunity in the gut.
- Improve calcium absorption.
- Control obesity.
- Possibly control certain types of diabetes.
- Decrease cholesterol levels.
There is also some evidence that inulin – type prebiotics have a positive effect on bowel transit and stool consistency in infants and alleviate existing constipation in adults. Further studies in a population of tube feeding adult patients indicated that addition of FOS to their food increased levels of fecal Bifidobacteria and enhanced quality of life scores. Similarly addition of FOS to infant foods increased the fecal content of Bifidobacteria and the level of intestinal microflora in formula fed infants.
The combination of inulin and probiotics offered in IMMNOBIOTICS provide
an efficient and convenient paired product for the consumer's benefit. It also provides for a functionally superior product compared to individual intake of each ingredient separately.
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