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Subtractive hybridization analysis of gastric diseases‐associated Helicobacter pylori identifies peptidyl‐prolyl isomerase as a potential marker for gastric cancer
Author(s) -
Gong Yuehua,
Chen Moye,
Xu Ying,
Dong Nannan,
Sang Zhikun,
Liu Jun,
Yuan Yuan
Publication year - 2011
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2011.02296.x
Subject(s) - helicobacter pylori , suppression subtractive hybridization , cancer , biology , caga , gastritis , chronic gastritis , gene , genetics , complementary dna , cdna library , virulence
Helicobacter pylori , a microaerophilic Gram‐negative bacterium, is known to cause chronic gastritis, peptic ulcer and gastric cancer. Genes that are present in certain isolates may determine strain‐specific traits such as disease association and drug resistance. In order to understand the pathogenic mechanisms of gastric diseases, identify molecular markers of the diseases associated with H. pylori strains and provide clues for target treatment of H. pylori ‐related diseases, a subtracted DNA library was constructed from a gastric cancer‐associated H. pylori strain and a superficial gastritis‐associated H. pylori strain by suppression subtractive hybridization. The presence of gastric cancer‐specific genes was identified by dot blot hybridization, DNA sequencing and PCR‐based screening. Twelve gastric cancer‐specific high‐copy genes and nine low‐copy genes were found in gastric cancer compared with the superficial gastritis strain. These genes were confirmed by PCR analysis of H. pylori isolates. Notably, peptidyl‐prolyl cis–trans isomerase (PPIase) was detected positively in 11 out of 22 (50%) gastric cancer‐associated H. pylori s trains. In contrast, <24% of the H. pylori strains from superficial gastritis showed positive results. Given the potential role of PPIases in cell growth, apoptosis and oncogenic transformation, our results suggest that PPIase may represent a novel marker and potential therapeutic target for gastric cancer.

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