Takeshi Azuma

TL;DR: Wild-type but not phosphorylation-resistant CagA induced a growth factor–like response in gastric epithelial cells and formed a physical complex with the SRC homology 2 domain (SH2)–containing tyrosine phosphatase SHP-2 in a phosphorylations-dependent manner and stimulated the phosphat enzyme activity.

TL;DR: The results indicate that the potential of individual CagA to perturb host-cell functions is determined by the degree of SHP-2 binding activity, which depends in turn on the number and sequences of tyrosine phosphorylation sites.

TL;DR: First direct evidence is provided for the role of CagA as a bacterium-derived oncop protein (bacterial oncoprotein) that acts in mammals and the importance of CAgA tyrosine phosphorylation, which enables CAGA to deregulate SHP-2, in the development of H. pylori-associated neoplasms is indicated.

TL;DR: It is shown that infection of gastric epithelial cells with 'cag' pathogenicity island (cagPAI)-positive H. pylori induced aberrant expression of activation-induced cytidine deaminase (AID), a member of the cytidine-deaminase family that acts as a DNA- and RNA-editing enzyme, via the IκB kinase–dependent nuclear factor-κB activation pathway.

TL;DR: The findings revealed that PAR1 is a key target of H. pylori CagA in the disorganization of gastric epithelial architecture underlying mucosal damage, inflammation and carcinogenesis.