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Recognition and phagocytosis of apoptotic T cells by resident murine tissue macrophages require multiple signal transduction events
Author(s) -
Hu Bin,
Punturieri Antonello,
Todt Jill,
Sonstein Joanne,
Polak Timothy,
Curtis Jeffrey L.
Publication year - 2002
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.71.5.881
Subject(s) - biology , microbiology and biotechnology , phagocytosis , signal transduction , tyrosine phosphorylation , wortmannin , phosphorylation , kinase , calphostin c , ly294002 , staurosporine , protein kinase c , protein kinase b
Macrophages (Mø) ingest apoptotic cells with unique effects on their cytokine production, but the signaling pathways involved are virtually unknown. Signal transduction in response to recognition of apoptotic thymocytes by resident murine alveolar (AMø) or peritoneal (PMø) Mø was studied by in vitro phagocytosis assay. Phagocytosis was decreased in a dose‐dependent and nontoxic manner by inhibiting phosphatidylinosiol 3 kinase (wortmannin and LY294002), protein tyrosine phosphorylation (herbimycin A, genistein, piceatannol, and for AMø only, PP2), and protein kinase C (staurosporine, Gö 6976, and calphostin C). Exposure of Mø to apoptotic or heat‐killed thymocytes, but not to viable thymocytes, activated ERK1/2 rapidly, as detected by specific phosphorylation, but did not activate NF‐κB or MAP kinases p38 or JNK. Mø phagocytosis of apoptotic T cells requires tyrosine, serine/threonine, and lipid phosphorylation. Mø recognition of apoptotic T cells triggers rapid but limited MAP kinase activation.