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PHOSPHORYLATION OF THE C‐TERMINAL DOMAIN OF MUC1 IN INFLAMMATION
Author(s) -
Nguyen Lynne,
Van Eugene,
Tsai Jeffrey
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.lb153
Subject(s) - muc1 , phosphorylation , inflammation , mucin , signal transduction , microbiology and biotechnology , biology , innate immune system , transmembrane protein , kinase , glycoprotein , cancer research , chemistry , receptor , biochemistry , immunology
Mucins are protective glycoproteins in the respiratory, digestive, and urogenital tracts. MUC1 is a large O‐glycosylated transmembrane protein expressed on the apical surface of epithelial tissues. It exhibits structural features of receptors for cytokines and growth factors. Its intracellular cytoplasmic tail contains multiple amino acid sequence motifs that, once phosphorylated, serve as docking sites for protein kinases for signal transduction. Most studies have focused on breast and pancreatic cancer cells in related to overexpression of MUC1. Few have examined phosphorylation in normal epithelial cells in the oral cavity. MUC1 plays a role in the pathogenesis of cancer and innate immunity. The present study was to determine whether MUC1 expressed in oral epithelial cells is phosphorylated in response to pro‐inflammatory mediators of inflammation. EGF, IL‐1‐beta, IFN‐gamma, and LPS was treated in KB and TR146 cells and examined the pro‐inflammatory mediators on the C‐terminal domain of MUC1. The results showed that the C‐terminal domain of MUC1 is phosphorylated in response to treatments of pro‐inflammatory cytokines. It suggests that phosphorylation of MUC1 may function to initiate inflammatory signaling cascades during the early stages of inflammation in response to bacterial infection.