Journal
ONCOTARGET
Volume 6, Issue 31, Pages 31916-31926Publisher
IMPACT JOURNALS LLC
DOI: 10.18632/oncotarget.5577
Keywords
gastric carcinogenesis; Helicobacter pylori; phosphatase and tensin homolog; phosphorylation; PI3K/Akt pathway
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Funding
- National Natural Science Foundation of China [81060038, 81460377]
- Natural Science Foundation of Jiangxi Province, China [20142BAB215036, 20151BAB205041]
- Science and Technology Foundation of Department of Education of Jiangxi Province, China [GJJ14169]
- Graduate Innovative Foundation of Jiangxi Province, China [YC10A020]
- National Science and Technology Major Projects program for Major New Drugs Innovation and Development of China [2011ZX09302-007-03]
- Talent 555 Project of Jiangxi Province, China
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Phosphorylation of PTEN at residues Ser380/Thr382/383 leads to loss of phosphatase activity and tumor suppressor function. Here, we found that phosphorylation of PTEN at residues Ser380/Thr382/383 was increased with gastric carcinogenesis, and more importantly, Helicobacter pylori was a trigger of this modification in chronic non-atrophic gastritis. H. pylori could phosphorylate and inactivate PTEN in vivo and in vitro, resulting in survival of gastric epithelial cells. Furthermore, stable expression of dominant-negative mutant PTEN or inhibition of Akt prevented the enhanced survival induced by H. pylori. These results indicate that PTEN phosphorylation at residues Ser380/Thr382/383 is a novel mechanism of PTEN inactivation in gastric carcinogenesis, and H. pylori triggers this modification, resulting in activation of the PI3K/Akt pathway and promotion of cell survival.
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