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Proteomic Approach to Evaluate Mechanisms That Contribute to Food Allergenicity: Comparative 2D-DIGE Analysis of Radioallergosorbent Test Positive and Negative Patients
Author(s) -
Bindukumar Nair,
J. C. Wheeler,
Donald E. Sykes,
P. Brown,
Jessica L. Reynolds,
Ravikumar Aalinkeel,
Supriya D. Mahajan,
Stanley A. Schwartz
Publication year - 2011
Publication title -
international journal of proteomics
Language(s) - English
Resource type - Journals
eISSN - 2090-2174
pISSN - 2090-2166
DOI - 10.1155/2011/673618
Subject(s) - radioallergosorbent test , medicine , test (biology) , food hypersensitivity , immunology , allergy , food allergy , biology , allergen , ecology
Proteomic profiles of RAST + subjects with severe food allergies and RAST − subjects were compared using 2D-DIGE analysis to obtain candidate biomarkers specific to food allergies. Our analysis highlighted 52 proteins that were differentially expressed between the RAST + and RAST − groups of which 37 were successfully identified that include chondroitin sulfates, zinc finger proteins, C-type lectins, retinoic acid binding proteins, heat shock proteins, myosin, cytokines, mast cell expressed proteins, and MAP kinases. Biological network analysis tool Metacore revealed that most of these regulated proteins play a role in immune tolerance, hypersensitivity and modulate cytokine patterns inducing a Th2 response that typically results in IgE-mediated allergic response which has a direct or indirect biological link to food allergy. Identifying unique biomarkers associated with certain allergic phenotypes and potentially cross-reactive proteins through bioinformatics analyses will provide enormous insight into the mechanisms that underlie allergic response in patients with food allergies.

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