PDGF-induced Akt phosphorylation does not activate NF-κB in human vascular smooth muscle cells and fibroblasts
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- 作者：Rauch ; Bernhard H. ; Weber ; Artur-Aron ; Braun ; Marina ; Zimmermann ; Norbert ; Schrö ; r ; Karsten
- 关键词：Nuclear factor-κ ; B ; Akt phosphorylation ; Cytokine ; Growth factor ; Vascular smooth muscle cell ; EDTA ; ethylenediamine-tetraacetic acid ; Iκ ; B ; inhibitory protein κ ; B ; NF-κ ; B ; nuclear factor κ ; B ; PBS ; phosphate-buffered saline ; PDGF ; plat
- 刊名：FEBS Letters
- 出版年：2000
- 出版时间：September 8, 2000
- 年：2000
- 卷：481
- 期：1
- 页码：3-7
- 全文大小：321 K
文摘
A recent report suggested that platelet-derived growth factor (PDGF) activates nuclear factor-κB (NF-κB) by phosphorylation of the protein kinase Akt [Romashkova and Makarov, Nature 401 (1999) 86–90]. The present study investigates the role of Akt in the activation of NF-κB by tumor necrosis factor-α (TNFα, 10 ng/ml) and PDGF-BB (20 ng/ml) in human vascular smooth muscle cells (SMC), skin and foreskin fibroblasts. TNFα stimulated serine phosphorylation and degradation of the inhibitory protein IκBα and strongly induced nuclear NF-κB translocation and binding activity. PDGF did not induce serine phosphorylation or degradation of IκBα and did not enhance binding activity of NF-κB. In contrast, stimulation with PDGF resulted in a marked phosphorylation of Akt, but no Akt phosphorylation occurred after stimulation with TNFα. These data suggest that Akt phosphorylation is not involved in NF-κB activation in human SMC and fibroblasts.