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Protein kinase C agonists enhance phagocytosis of P. aeruginosa by murine alveolar macrophages
Author(s) -
Heale JohnPaul,
Speert David P.
Publication year - 2001
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 - 10.1189/jlb.69.1.158
Subject(s) - phagocytosis , sodium azide , protein kinase c , biology , macrophage , pseudomonas aeruginosa , microbiology and biotechnology , tumor necrosis factor alpha , in vitro , phenotype , phorbol , kinase , immunology , pharmacology , biochemistry , bacteria , genetics , gene
Pulmonary alveolar macrophages (AMφs) are incompetent to phagocytose unopsonized Pseudomonas aeruginosa , but ingestion by other macrophage phenotypes (i.e., peritoneal macrophages) occurs efficiently. The purpose of this study was to explore factors that might control such phenotypic differences. Our laboratory has demonstrated that AMφs exposed to sodium azide display enhanced phagocytosis of P. aeruginosa . Here we report that the phagocytic‐enhancing effect of sodium azide was abrogated by inhibitors of protein kinase C (PKC). Furthermore, the addition of PKC agonists, such as phorbol myristate acetate (PMA), and tumor necrosis factor α (TNF‐α), mimicked the phagocytic enhancing effect of sodium azide. We conclude that AMφs are normally incompetent to phagocytose P. aeruginosa . Factors that up‐regulate AMφ function (azide, PMA, TNF‐α) can reverse the phagocytic incompetence in vitro . Although these compounds are not appropriate candidate therapeutic agents, their effects provide insights for understanding of the pathways responsible for regulation of P. aeruginosa phagocytosis.