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J Biol Chem, Vol. 274, Issue 33, 23235-23241, August 13, 1999

CD14-dependent Internalization and Metabolism of Extracellular Phosphatidylinositol by Monocytes

Ping-yuan Wang^§ and Robert S. Munford^¶

From the Departments of  Internal Medicine and ^¶ Microbiology and the ^§ Cell Regulation Graduate Program, The University of Texas Southwestern Medical Center, Dallas, Texas 75235-9113

We report that membrane CD14 (mCD14), a cell surface receptor found principally on leukocytes, can mediate the uptake and metabolism of extracellular phosphatidylinositol (PtdIns). mCD14 facilitates PtdIns internalization, targeting it to intracellular sites where, following stimulation with a calcium ionophore, it can be acted upon by cytosolic phospholipase A₂. The [¹⁴C]arachidonate released from mCD14-acquired [¹⁴C]arachidonyl-PtdIns is either esterified to triacylglycerol and retained in the cell or secreted as free arachidonate or leukotrienes. Although less than 10% of the arachidonate-derived lipids secreted from endogenous cellular stores are 5-lipoxygenase metabolites, over one-half of the secreted ¹⁴C-lipids derived from mCD14-acquired PtdIns are hydroxyeicosatetraenoic acids or leukotriene B₄. mCD14 may allow these highly active blood cells to acquire and use extracellular PtdIns as a source of arachidonate for leukotriene synthesis.

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