Abstract
Cells catabolize the nutrient molecules and store the free energy in chemical forms such as ATP. ATP releases its chemical energy through catalysis into 2ADP + Pi. Adenylate kinase, an enzyme catalyzing interconversion of AMP, ADP and ATP, is responsible for maintaining the adenine nucleotide balance in cells. It is found in both eukaryotic and prokaryotic cells. In has been reported previously that adenylate kinase is secreted by Pseudomonas aeruginosa and causes toxicity to macrophage during infection and is likely an important virulence factor. During infection, damaged cells could release adenine nucleotides that may participate bacterial infections, regulate the wound healing, and trigger immune reaction of macrophage to clear the infection. This study found that different adenine nucleotides can enhance the migration ability of C2BBe1 and HCT-8 epithelial cells. Massive cell death of macrophage RAW 264.7 could be observed after treatment with P.aeruginosa isolate B136-33 supernatant supplemented with ATP. Moreover, purified adenylate kinase increases the ADP-mediated RAW 264.7 cell death. My study also showed that P. aeruginosa culture supernatant and adenine nucleotides can alter the structure of tight junction and lead to serve damage of C2BBe1 cell monolayer. Together, our finding confirms previous notions that the adenine nucleotides play an important role in cell physiology and bacterial infections.