Interleukin-1β effect on the endogenous ADP-ribosylation and phosphorylation of eukaryotic elongation factor 2

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• 作者：Ebru Hacıosmanoğlu ; Başak Varol ; Bilge Özerman Edis ; Muhammet Bektaş
• 关键词：Diphtheria toxin ; Endogenous ADP ; ribosylation ; Eukaryotic elongation factor 2 ; Interleukin ; 1β ; Phosphorylation ; Protein synthesis
• 刊名：Cytotechnology
• 出版年：2016
• 出版时间：December 2016
• 年：2016
• 卷：68
• 期：6
• 页码：2659-2666
• 全文大小：717 KB
• 刊物类别：Chemistry and Materials Science
• 刊物主题：Chemistry
  Biotechnology
  Biomedicine
  Biochemistry
  
• 出版者：Springer Netherlands
• ISSN：1573-0778
• 卷排序：68

文摘

Eukaryotic elongation factor 2 (eEF2) plays an important role in eukaryotic polypeptide chain elongation. Adenosine diphosphate (ADP)-ribosylation is a post-translational modification reaction that catalyzes the transfer of ADP-ribose group to eEF2 and this causes the inhibition of protein synthesis. Indeed, in the absence of diptheria toxin, endogenous ADP-ribosylation can occur. eEF2 is phosphorylated by eEF2 kinase which prevents binding to ribosomes thus inhibiting its activity. Increase in endogenous ADP-ribosylation level approximately 70–75 % was observed in IL-1β treated HUVECs. Moreover, a 70 % rise of phosphorylation of eEF2 was measured. Alteration of endogenous ADP-ribosylation of eEF2 activity was related with cellular mono-ADP-ribosyltransferases (ADPrT). Increment of endogenous ADP-ribosylation on eEF2 did not seem to occur as a direct effect of IL-1β; it arises from the activation of ADPrT. This 2.5 fold increase was abolished by ADPrT inhibitors. Due to these post-translational modifications, global protein synthesis is inhibited. After dephosphorylation of phospho-eEF2, around 20 % increase in protein synthesis was observed. In conclusion, systemic IL-1β has an important role in the regulation of global protein synthesis.