Skip to main content
construction release_alert
Scholars@Duke will be undergoing maintenance April 11-15. Some features may be unavailable during this time.
cancel

Characterization of the interleukin-1-stimulated phospholipase C activity in human T lymphocytes.

Publication ,  Journal Article
Rosoff, PM
Published in: Lymphokine Res
1989

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.

Duke Scholars

Published In

Lymphokine Res

ISSN

0277-6766

Publication Date

1989

Volume

8

Issue

4

Start / End Page

407 / 413

Location

United States

Related Subject Headings

  • Type C Phospholipases
  • Tumor Cells, Cultured
  • Trypsin
  • T-Lymphocytes
  • Phosphatidylinositols
  • Magnesium
  • Interleukin-1
  • Humans
  • Calcium
 

Citation

Published In

Lymphokine Res

ISSN

0277-6766

Publication Date

1989

Volume

8

Issue

4

Start / End Page

407 / 413

Location

United States

Related Subject Headings

  • Type C Phospholipases
  • Tumor Cells, Cultured
  • Trypsin
  • T-Lymphocytes
  • Phosphatidylinositols
  • Magnesium
  • Interleukin-1
  • Humans
  • Calcium