*FCC-approved units. Non-medicinal ingredients: Microcrystalline cellulose, silicon dioxide. Capsule; hypromellose, sorbitol, silicon dioxide, water.
AOR guarantees that no ingredients not listed on the label have been added to the product. Contains no wheat, gluten, corn, nuts, dairy, soy, eggs, fish or shellfish.
Suggested Use Take one capsule three times a day with food or as directed by a qualified health practitioner.
Main Applications • Anti-Inflammatory • Autoimmune diseases.
Pregnancy / Nursing None.
Cautions None.
*These statements have not been evaluated by the Food and Drug Administration. This product is not intended to diagnose, treat, cure, or prevent any disease.
| Autoimmune disorders are some of the most disabling health conditions we face today. The reason why some of us develop an immune response to our own body remains unclear. We know that autoimmunity runs in families, which indicates that genes may be partly to blame. It is also likely that how our immune system responds to environmental triggers plays a large part in the development of autoimmune conditions. |
| Peptidases are enzymes that are responsible for the breakdown of proteins. Peptidases embedded in cellular membranes cleave foreign proteins in order to present their antigens to immune cells. This activates or inactivates the immune response, making peptidases a key to the modulation of the immune system.
Dipeptidylpeptidase IV (DPP IV) is an essential peptidase for antigen presentation. DPP IV promotes a normal cellular immune response and is important for the production of immune messengers that regulate immunity and inflammation. Preliminary research has shown that DPP IV cleaves and inactivates tumor necrosis factor alpha (TNF-a), regulating the extracellular TNF-a concentration. TNF-a is an immune messenger that promotes inflammation and plays a significant part in autoimmune disorders such as inflammatory bowel disease, rheumatoid arthritis and ankylosing spondylitis.
Over activation of the immune system during an infection can drive the immune system into a state of autoimmunity, which leads to cellular damage and chronic inflammation. Autoimmunity can be promoted through the inappropriate activation of white blood cells by dietary peptide sequences such as gliadins found in gluten.
The problem is made worse by a lack of DPP IV enzyme activity in certain gastrointestinal conditions. Lower peptidase levels reduce the body's ability to metabolize proteins, especially proteins containing proline because DPP IV is needed for their assimilation. This results in the accumulation of undigested peptide fragments, which are thought to elicit an immune response that can inflame the lining of the gastrointestinal tract.
Oral supplementation with DPP IV enzymes prevents the activation of the immune system by breaking down dietary peptides from food - a significant benefit for those suffering from autoimmune diseases.
DPP ZYMETM from AOR is a unique protease formula that provides standardized DPP IV activity.
References
Vojdani A, Bazargan M, Vojdani E, Samadi J, Nourian AA, Eghbalieh N, Cooper EL. Heat shock protein and gliadin peptide promote development of peptidase antibodies in children with autism and patients with autoimmune disease. Clin Diagn Lab Immunol. 2004 May;11(3):515-24.
Sedo A, Malik R. Dipeptidyl peptidase IV-like molecules: homologous proteins or homologous activities? Biochim Biophys Acta. 2001 Dec 17;1550(2):107-16. Review.
Tiruppathi C, Miyamoto Y, Ganapathy V, Leibach FH. Genetic evidence for role of DPP IV in intestinal hydrolysis and assimilation of prolyl peptides. Am J Physiol. 1993 Jul;265(1 Pt 1):G81-9.
Mast cell-derived proteases control allergic inflammation through cleavage of IgE. J Allergy Clin Immunol. 2007 Sep 27 Rauter I, Krauth MT, Westritschnig K, Horak F, Flicker S, Gieras A, Repa A, Balic N, Spitzauer S, Huss-Marp J, Brockow K, Darsow U, Behrendt H, Ring J, Kricek F, Valent P, Valenta R.
BACKGROUND: Cross-linking of mast cell-bound IgE releases proinflammatory mediators, cytokines, and proteolytic enzymes and is a key event in allergic inflammation. OBJECTIVE: We sought to study the effect of proteases released on effector cell activation on receptor-bound IgE and their possible role in the regulation of allergic inflammation. METHODS: Using molar ratios of purified recombinant tryptase and human IgE, we studied whether tryptase can cleave IgE. Similar experiments were performed with mast cell lysates in the presence or absence of protease inhibitors. IgE cleavage products were detected in supernatants of allergen cross-linked, cultivated mast cells and in tissue fluids collected from patients' skin after IgE-mediated degranulation. The effects of protamine, an inhibitor of heparin-dependent proteases on IgE-mediated allergic in vivo skin inflammation in human subjects were studied. RESULTS: We show that beta-tryptase, a major protease released during mast cell activation, cleaves IgE. IgE degradation products were detected in tryptase-containing tissue fluids collected from sites of allergic inflammation. The biologic significance of this mechanism is demonstrated by in vivo experiments showing that protease inhibition enhances allergic skin inflammation. CONCLUSION: We suggest that IgE cleavage by effector cell proteases is a natural mechanism for controlling allergic inflammation. CLINICAL IMPLICATIONS: The finding that effector cell-derived proteases might control allergic inflammation through cleavage of IgE could allow for the development of new therapeutic strategies for allergic disease.
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