Journal of the Science of Food and Agriculture · 2016 · 19 citations · 21 references
Life SciencesBiochemistryImmunologyAllergyHypersensitivityInflammationAllergic Skin DiseasesBioactive Food ComponentsCellular Immune ResponsesFood AllergensFood AllergyShellfish AllergyAllergic Disease MechanismsFood Allergen ResponsesFood Allergen SensitizationFood Antigen HypersensitivityLipid Peroxidation In Disease PathogenesisLipid Peroxidation MarkersMolecular Basis Of AllergenicityTropomyosin Allergy
BACKGROUND: Malonaldehyde, the primary by-product of lipid peroxidation in food, modifies the structural and functional properties of proteins by cross-linking. The aim of this study was to investigate the effect of malonaldehyde on the allergenicity of shrimp tropomyosin. RESULTS: RBL-2H3 cells, a model of type I allergic reactions, were sensitised with sera from patients allergic to shrimp, and were stimulated with native and cross-linked tropomyosin. Release of inflammatory mediators such as β-hexosaminidase, histamine, tryptase, cysteinyl leukotriene, and prostaglandin D2 was clearly suppressed in a manner that depended on the extent of tropomyosin cross-linking. Release of interleukin-4 (IL-4) and IL-13 was similarly decreased. Notably, cells sensitised with one patient's serum released IL-4 at comparable levels in response to native and cross-linked tropomyosin. CONCLUSION: Cross-linking strongly modulates the ability of shrimp tropomyosin to induce release of inflammatory cytokines and mediators from activated RBL-2H3 cells. © 2016 Society of Chemical Industry.
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