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Stability of Helicobacter pylori CagA oncoprotein in human gastric epithelial cells
Author(s) -
Ishikawa Susumu,
Ohta Tomomi,
Hatakeyama Masanori
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.06.043
Subject(s) - caga , helicobacter pylori , protein tyrosine phosphatase , biology , carcinogenesis , microbiology and biotechnology , gene , phosphorylation , biochemistry , virulence , genetics
Upon delivery into gastric epithelial cells, Helicobacter pylori cytotoxin‐associated gene A (CagA) binds and deregulates cellular proteins such as Src homology 2 domain‐containing protein tyrosine phosphatase 2 and partitioning‐defective 1 (PAR1), thereby acting as an epigenetic oncoprotein that promotes early phases of gastric cancer development. To elucidate the spatial and temporal contribution of CagA to carcinogenesis, it is crucial to know the stability of CagA in host cells. Here we show that the biological half‐life of CagA is about 200 min in gastric epithelial cells. Furthermore, deletion of the PAR1‐binding sequence accelerates CagA degradation. Thus, CagA is a relatively short half‐life protein whose stability may be modulated through complex formation with PAR1.