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헬리코박터 파이로리의 병원성 단백질, CagA에 대한 분자 독성학적 측면에서의 고찰
김병주(Byung J. Kim),정화진(Hwa Jin Jung),황지나(Jee Na Hwang),강석하(Seok Ha Kang),오세진(Se-Jin Oh),서영록(Young Rok Seo) 한국독성학회 2004 Toxicological Research Vol.20 No.3
Helicobacter pylori (H. pylori) infects more than half of the people in the world as a major<br/> microbe to cause most of gastric diseases. Recently, cytotoxin associated-antigen A (CagA) is believed as<br/> one of the most important virulence factors of H. pylori. Molecular toxicological pathway of CagA is necessary<br/> to investigate for understanding the pathological and toxicological aspects of H. pylori, since this virulence<br/> protein harasses intercellular processes of host cells to get profit for the survival of H. pylori. CagA is<br/> coded from cag pathogenicity island (cag PAI) and translocated into host cells by Type 4 secretion system<br/> (TFSS). Tyrosine phosphorylation of CagA targets Src homology 2-containing phosphotyrosine phosphatase<br/> (SHP-2) to form a CagA-SHP-2 complex. This complex depends on the similarity of sequence<br/> between EPIYA motif and Src homology 2 domain (SH2 domain) of CagA. The generation of growth factors<br/> is an essential role of CagA in protecting and healing gastric mucosa for the survival of H. pylori. On<br/> the other hand, the activation of IL-8 by CagA induces neutrophils generating inflammation and free radicals.<br/> Indeed, free radicals are well known carcinogen to induce DNA damage. In addition, the transduction<br/> of mitogen-activation signal by CagA is one of the interesting features to understand how to cause cancer.<br/> The relationship between cancer and inflammation with CagA was mainly discussed in this review.
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