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Journal of Lipid Research, Vol. 8, 359-365, July 1967
Copyright © 1967 by Lipid Research, Inc.
Department of Medicine of New York University School of Medicine, New York 10016
A comparison has been made between the conversion of 32P-labeled lysophosphatidyl ethanolamine (LPE) and lysophosphatidyl choline (LPC) to their respective acylated and deacylated derivatives by homogenates of rabbit polymorphonuclear leukocytes and alveolar macrophages.
Synthesis of PE by both homogenates and of PC by macrophage homogenates proceeded to about the same extent and is attributed to direct acylation of the lyso compounds. At higher LPC concentrations formation of PC by leukocytes is far greater than by macrophages. The mechanism of this enhanced synthesis of PC, which is brought out by higher substrate concentrations, is believed to be a transfer of the acyl group of one LPC molecule to another.
Under optimal conditions macrophage homogenates deacylated LPE to a greater extent than LPC, while the reverse was true for leukocyte homogenates.
Albumin inhibited deacylation of LPC and its conversion to PC by leukocytes, perhaps by binding the substrate (2 moles of LPC per mole of albumin). Other effects of albuminstimulation of deacylation and acylation of LPE by macrophages, inhibition of deacylation and acylation of LPE by leukocytesremain unexplained.
Supplementary key words phospholipids lyso compounds metabolism lysophosphatidyl ethanolamine lysophosphatidyl choline rabbit phagocytic cells polymorphonuclear leukocytes alveolar macrophages homogenates
Submitted on January 26, 1967
Accepted on March 15, 1967
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