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β-Arrestin prevents cell apoptosis through pro-apoptotic ERK1/2 and p38 MAPKs and anti-apoptotic Akt pathways.

Authors
  • Yang, Xiaohua1
  • Zhou, Gengyin
  • Ren, Tao
  • Li, Hui
  • Zhang, Yanjun
  • Yin, Deling
  • Qian, Haixin
  • Li, Qinchuan
  • 1 Department of General Surgery, The First Affiliated Hospital of Soochow University, Suzhou, 215006, China. , (China)
Type
Published Article
Journal
APOPTOSIS
Publisher
Springer-Verlag
Publication Date
Sep 01, 2012
Volume
17
Issue
9
Pages
1019–1026
Identifiers
DOI: 10.1007/s10495-012-0741-2
PMID: 22699970
Source
Medline
License
Unknown

Abstract

Our previous studies have shown that β-arrestin 2 plays an anti-apoptotic effect. However, the mechanisms by which β-arrestin contribute to anti-apoptotic role remain unclear. In this study, we show that a deficiency of either β-arrestin 1 or β-arrestin 2 significantly increases serum deprivation (SD)-induced percentage of apoptotic cells. β-arrestin 2 deficient-induced apoptosis was inhibited by transfection with β-arrestin 2 full-length plasmid, revealing that SD-induced apoptosis is dependent on β-arrestin 2. Furthermore, in the absence of either β-arrestin 1 or β-arrestin 2 significantly enhances SD-induced the level of pro-apoptotic proteins, including cleaved caspase-3, extracellular-signal regulated kinase 1/2 (ERK1/2) and p38, members of mitogen-activated protein kinases (MAPKs). In addition, a deficiency of either β-arrestin 1 or β-arrestin 2 inhibits phosphorylation of Akt. The SD-induced changes in cleaved caspase-3, ERK1/2 and p38 MAPKs, Akt, and apoptotic cell numbers could be blocked by double knockout of β-arrestin 1/2. Our study thus demonstrates that β-arrestin inhibits cell apoptosis through pro-apoptotic ERK1/2 and p38 MAPKs and anti-apoptotic Akt signaling pathways.

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