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Internalization of FimH + Escherichia coli by the human mast cell line (HMC‐1 5C6) involves protein kinase C
Author(s) -
Lin TongJun,
Gao Zhimin,
Arock Michel,
Abraham Soman N.
Publication year - 1999
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.66.6.1031
Subject(s) - internalization , biology , protein kinase c , escherichia coli , microbiology and biotechnology , bacteria , kinase , mast cell , cell , biochemistry , immunology , gene , genetics
Rodent mast cells (MC) play critical roles in host defense against bacterial infection. However, bacteria‐mediated signaling mechanisms in MC have not been studied. In addition, the response of human MC to bacteria is not fully investigated. This study examined the interaction between human MC and type 1 fimbriated Escherichia coli and the mechanisms involved using the human MC line HMC‐1 5C6 and human cord blood‐derived MC. These MC internalized significant numbers of FimH + E. coli , but not its isogenic FimH − mutant. In HMC‐1 cells, bacterial internalization was stimulated by protein kinase C (PKC) activation [short‐term phorbol myristate acetate (PMA) treatment] and dramatically decreased by PKC inhibitors or PKC depletion (long‐term PMA treatment). Moreover, bacterial internalization was accompanied by significant expression of PKCβ 1 and δ. Fluorescence microscopy demonstrated accumulation of PKCβ 1 on internalized bacteria. These data indicate that human MC has the capacity to internalize bacteria and PKC may be a critical intracellular mediator of this function. J. Leukoc. Biol. 66: 1031–1038; 1999.