Inhibition of CD28‐mediated T cell costimulation by the phosphoinositide 3‐kinase inhibitor wortmannin
European Journal of Immunology, ISSN: 1521-4141, Vol: 25, Issue: 2, Page: 526-532
1995
- 85Citations
- 11Captures
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Metrics Details
- Citations85
- Citation Indexes85
- 85
- CrossRef60
- Captures11
- Readers11
- 11
Article Description
T lymphocyte activation requires at least two signals, one via the antigen‐specific T cell receptor and a second via the surface molecule CD28 which provides signals critical to interleukin‐2 (IL‐2) production and T cell proliferation. We have previously shown (Ward S. G., Westwick J., Hall N. and Sansom D. M. Eur. J. Immunol. 1993. 23: 2572) that CD28 stimulates phosphoinositide (PI) 3‐kinase activity, indicating that D‐3 phosphoinositides may act as mediators of CD28‐induced T cell costimulation. Here, we report that immunoprecipitation of CD28 molecules from Jurkat cells stimulated with the CD28‐ligand B7, results in a ligand‐dependent association of CD28 with PI 3‐kinase. This association correlates with the appearance of PI 3‐kinase enzymatic activity in CD28 immunoprecipitates and the formation of D‐3 phosphoinositides. Consistent with the hypothesis that D‐3 phosphoinositides are important mediators of CD28 signaling, treatment of T cells with the PI 3‐kinase inhibitor wortmannin, inhibited both T cell proliferation and production of IL‐2, but not the response of T cells to exogenous IL‐2. Hence, abrogation of PI 3‐kinase activity by wortmannin, appears sufficient to disrupt the costimulatory pathway utilized by CD28, indicating a central role for this enzyme in the CD28 signaling pathway. Copyright © 1995 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim
Bibliographic Details
Wiley
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