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Papers In Press, published online ahead of print March 27, 2007
J. Lipid Res., doi:10.1194/jlr.M700083-JLR200
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Biochemistry, Virginia Commonwealth University, Richmond, VA 23298-0614
Corresponding Author: cechalfant{at}vcu.edu
Ceramide kinase (CERK) is a critical mediator of eicosanoid synthesis, and its product, ceramide-1-phosphate (C1P), is required for the production of prostaglandins in response to several inflammatory agonists. In this study, mass spectrometry analysis disclosed that the main forms of C1P in cells were C16:0 C1P and C18:0 C1P suggesting CERK utilized ceramide transported to the trans-golgi apparatus by ceramide transport protein (CERT). To this end, downregulation of CERT by RNA interference technology (RNAi) dramatically reduced the levels of newly synthesized C1P (kinase-derived) as well as significantly reduced the total mass levels of C1P in cells. Confocal microscopy, subcellular fractionation and surface plasmon resonance analysis were utilized to further localize CERK to the trans-Golgi network placing the generation of C1P in the proper intracellular location for recruitment of cPLA2. In conclusion, these results demonstrate that CERK localizes to areas of eicosanoid synthesis and utilizes a ceramide “pool” transported in an active manner via CERT.
Revised on March 23, 2007
Accepted on March 27, 2007
Ceramide kinase utilizes ceramide provided by ceramide transport protein. Localization to subcellular compartments of eicosanoid synthesis
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