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J. Biol. Chem., Vol. 277, Issue 39, 35906-35914, September 27, 2002

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Activation of Protein Kinase C II by the Stereo-specific Phosphatidylserine Receptor Is Required for Phagocytosis of Apoptotic Thymocytes by Resident Murine Tissue Macrophages^*

Jill C. Todt, Bin Hu, Antonello Punturieri^§, Joanne Sonstein, Timothy Polak, and Jeffrey L. Curtis^§¶**

From the  Division of Pulmonary and Critical Care Medicine, Department of Internal Medicine, the ^¶ Comprehensive Cancer Center, and the  Graduate Program in Immunology, University of Michigan Health Care System and the ^§ Pulmonary and Critical Care Medicine Section, Medical Service, Department of Veterans Affairs Care System, Ann Arbor, Michigan 48105-2303

We showed previously that protein kinase C (PKC) is required for phagocytosis of apoptotic leukocytes by murine alveolar (AMø) and peritoneal macrophages (PMø) and that such phagocytosis is markedly lower in AMø compared with PMø. In this study, we examined the roles of individual PKC isoforms in phagocytosis of apoptotic thymocytes by these two Mø populations. By immunoblotting, AMø expressed equivalent PKC  but lower amounts of other isoforms (, I, II, , , µ, and ), with the greatest difference in II expression. A requirement for PKC II for phagocytosis was demonstrated collectively by phorbol 12-myristate 13-acetate-induced depletion of PKC II, by dose-response to PKC inhibitor Ro-32-0432, and by use of PKC II myristoylated peptide as a blocker. Exposure of PMø to phosphatidylserine (PS) liposomes specifically induced translocation of PKC II and other isoforms to membranes and cytoskeleton. Both AMø and PMø expressed functional PS receptor, blockade of which inhibited PKC II translocation. Our results indicate that murine tissue Mø require PKC II for phagocytosis of apoptotic cells, which differs from the PKC isoform requirement previously described in Mø phagocytosis of other particles, and imply that a crucial action of the PS receptor in this process is PKC II activation.

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