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Am J Physiol Cell Physiol 266: C1093-C1104, 1994;
0363-6143/94 $5.00
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AJP - Cell Physiology, Vol 266, Issue 4 C1093-C1104, Copyright © 1994 by American Physiological Society

ARTICLES

Interleukin-1 stimulates phosphatidic acid-mediated phospholipase D activity in human mesangial cells

S. L. Bursten and W. E. Harris
Second Messenger and Lipid Biochemistry Laboratory, Cell Therapeutics, Inc., Seattle, Washington 98119.

Previous studies suggest that signal transduction mediated by interleukin-1 (IL-1), acting through an IL-1 receptor type found on T-cells and mesangial cells, may use phosphatidylethanolamine (PE) as a signaling molecule. Evidence presented here indicates that stimulation of human mesangial cells by IL-1 results in activation of a phospholipase D (PLD) that hydrolyzes PE to phosphatidic acid (PA). PLD acts on a subfraction of PE enriched in 1-o-alkyl and 1-o-alkenyl, sn-2-unsaturated species, generating a unique PA subspecies 30-120 s after stimulation. This PA species is subsequently converted to diradylglycerols by phosphatidate phosphohydrolase. The PE-directed PLD activity is abolished by antibodies against the IL-1 type I receptor and against IL-1. This specific PLD activity is also stimulated by low concentrations of 1,2-sn-dilinoleoyl PA, but not by high concentrations of 1-palmitoyl or 1-oleoyl lyso-PA. Blockade of PLD activation by IL-1 antibodies or antibody against the IL-1 receptor is bypassed by stimulation of human mesangial cells with 1,2-sn-dilinoleoyl PA. A novel system of signal cytokine mediation through PA self-amplification is indicated.


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