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J Biol Chem, Vol. 275, Issue 20, 15458-15465, May 19, 2000
From the Interdepartmental Program in Vascular Biology and
Transplantation, Boyer Center for Molecular Medicine, Yale University
School of Medicine, New Haven, Connecticut 06511
Tumor necrosis factor (TNF) and interleukin-1
(IL-1) activate the transcription of both anti-apoptotic and
pro-inflammatory gene products in human endothelial cells (EC) via
NF
A Phosphatidylinositol 3-Kinase/Akt Pathway, Activated by
Tumor Necrosis Factor or Interleukin-1, Inhibits Apoptosis but Does
Not Activate NF
B in Human Endothelial Cells*
B. Here we report that both TNF and IL-1 activate the
anti-apoptotic protein kinase Akt in growth factor and serum-deprived
EC, assessed by Western blotting for phospho-Akt. Phosphorylation of
Akt is blocked by LY294002 or wortmannin, inhibitors of
phosphatidylinositol 3-kinase (PI 3-kinase). Consistent with these
biochemical observations, TNF and IL-1 reduce apoptosis caused by
growth factor and serum deprivation, and this action is also blocked by
LY294002. Although Akt has been reported to activate NFB, LY294002
does not prevent TNF- or IL-1-induced degradation of IB
, 
, or
, transcription of NFB-dependent E-selectin or ICAM-1
promoter-reporter genes, or surface expression of E-selectin or ICAM-1
in human EC. LY294002 potentiates the activation of mitogen-activated
protein kinases and stress-activated protein kinases by TNF and IL-1,
suggesting Akt inhibits these responses. We conclude that TNF and IL-1
activate a PI 3-kinase/Akt anti-apoptotic pathway and that the
anti-apoptotic effects of Akt are independent of NFB. Moreover, the
PI 3-kinase/Akt pathway does not play a major role in the
pro-inflammatory responses of EC to TNF or IL-1.
*
This work was supported by Grant HL-36007 from the National
Institutes of Health and ISIS Pharmaceuticals.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Boyer Center for
Molecular Medicine, Yale University School of Medicine, New Haven, CT
06536-0812. Tel.: 203-737-2292; Fax: 203-737-2293; E-mail: Jordan.Pober@yale.edu.
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