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Identification of the protease resistant proteins from the major foods and their interactions to the intestinal mucosa of mouse
Author(s) -
Lee Ju-Young,
Lee Jin-Woo,
Kim Jong Sang,
Lim Jinkyu
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.1025.30
Subject(s) - protease , proteomics , biochemistry , membrane protein , intestinal mucosa , biology , chemistry , microbiology and biotechnology , enzyme , gene , membrane , medicine
Interaction between the food proteins and the intestinal mucosa can trigger many physiological changes including allergic reactions. To mimic the digestive system, the proteins from soy, wheat, potato, rice, egg and milk, were digested with the simulated gastric juice and pancreatic juice to obtain the protease resistant food proteins. The proteins were identified by mass analysis and bioinformatics. Majority of the proteins are already known food allergens, and many of them are storage proteins. The protease resistant proteins were coupled to columns and used to purify the interacting proteins on the intestinal mucosa membrane. The purified proteins were analyzed by LC‐mass spectrometry. As we reported previously, the 32 kDa protein was reproducibly identified. These protease resistant food proteins were assessed for the 3–D structures and found to share structural similarities with each other. A human epithelial cell line, IEC‐2, tested for the interaction with the protease resistant proteins were analyzed by proteomic methods for the identification of the proteins involved in cell signaling. The study showed that the interactions can change the phosphorylation status of the signaling proteins responsible for metabolic turnover, cytoskeletal formation and protein turn‐over. This study was supported by a research grant from KRF (2011‐0012683).