J. Lipid Res.
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A more recent version of this article appeared on March 1, 2008

Papers In Press, published online ahead of print December 21, 2007
J. Lipid Res., doi:10.1194/jlr.M700442-JLR200
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Submitted on October 4, 2007
Revised on November 14, 2007
Accepted on December 21, 2007

Ceramide kinase promotes Ca2+ signaling near IgG-opsonized targets and enhances phagolysosomal fusion in COS-1 cells

Vania T. Hinkovska-Galcheva, Andrea Clark, Susan M. Van Way, Ji-Biao Huang, Miki Hiraoka, Akira Abe, Michael Borofsky, Robin G. Kunkel, Thomas P. Shanley, James A. Shayman, Frederick Lanni, Howard R. Petty, and Laurence A. Boxer

Pediatrics/Critical Care Medicine, University of Michigan, Ann Arbor, MI 48109-2200

Corresponding Author: tzgalch{at}umich.edu

ABSTRACT Ceramide-1-phosphate (C1P) is a novel bioactive sphingolipid formed by the phosphorylation of ceramide catalyzed by ceramide kinase (CERK). In this study the mechanism by which increased C1P during phagocytosis enhances phagocytosis and phagolysosome formation in COS-1 cells expressing hCERK was evaluated. Stable transfectants of COS-1 cells expressing FcRIIA or both FcRIIA/hCERK expression vectors were created. Cell fractionation studies demonstrated that hCERK and the transient receptor potential channel (TRPC1) were enriched in caveolae fractions. Our data establish that both CERK and TRPC-1 localize to the caveolar microdomains during phagocytosis and that CERK also co-localizes with EIgG in Fcgamma RIIA-bearing COS-1 cell. Using high-speed fluorescence microscopy, Fcgamma RIIA/hCERK transfected cells displayed Ca2+ sparks around the phagosome. In contrast, cells expressing Fcgamma RIIA under identical conditions displayed little peri-phagosomal Ca2+ signaling. The enhanced Ca2+ signals were accompanied by enhanced phagolysosome formation. However, the addition of pharmacological reagents that inhibit store operated channels (SOC) reduced the phagocytic index and phagolysosomal fusion in hCERK transfected cells. The higher Ca2+ signal observed in hCERK transfected cells as well as the fact that CERK co-localized with EIgG during phagocytosis supports our hypothesis that Ca2+ signaling is an important factor for increasing phagocytosis and is regulated by CERK in a manner that involve SOC/TRPCs.


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