Characterization of the interleukin-1-stimulated phospholipase C activity in human T lymphocytes.
We have previously shown that interleukin-1 (IL-1) rapidly stimulates the hydrolysis of phosphatidylcholine in the human T lymphocyte cell line, Jurkat (Rosoff, et al., Cell 54: 73-81, 1988). This was apparently mediated by a phospholipase-C catalyzed mechanism, occurring initially at the outer plasma membrane. In this report, I have further characterized this activity of IL-1. The hydrolysis of phosphatidylcholine was dependent upon extracellular Ca2+, although it appeared to be relatively independent of Mg2+. The activity was totally inhibited by prior treatment of intact Jurkat cells with trypsin. In addition, treatment of Jurkat cells with a phosphatidylinositol-specific phospholipase C, which selectively removes proteins anchored by glycosyl-phosphatidylinositol linkages, completely blocked the ability of IL-1 to stimulate the hydrolysis of phosphatidylcholine. These data suggest that the initial activity of IL-1 is to stimulate a Ca2+-dependent, glycosyl-PI-anchored phospholipase C, the active site of which is on the extracellular surface.
Rosoff
P M
PM
Department of Physiology, Tufts University School of Medicine, Boston, MA 02111.
D002118:Calcium / Q000502:physiology; D006801:Humans; D007375:Interleukin-1 / Q000494:pharmacology*; D008274:Magnesium / Q000502:physiology; D010716:Phosphatidylinositols / Q000502:physiology; D013601:T-Lymphocytes / Q000201:enzymology*; D014357:Trypsin / Q000494:pharmacology; D014407:Tumor Cells, Cultured; D010738:Type C Phospholipases / Q000378:metabolism*
D007375:Interleukin-1; D010716:Phosphatidylinositols; D010738:Type C Phospholipases; D014357:Trypsin; D008274:Magnesium; D002118:Calcium