Effects of refluxate pH values on duodenogastroesophageal reflux-induced esophageal adenocarcinoma.

AIM: To determine the effects of duodenogastric juice pH on the development of esophageal adenocarcinoma (EAC). METHODS: An animal model of duodenogastroesophageal reflux was established using Sprague-Dawley (SD) rats undergoing esophagoduodenostomy (ED). The development of EAC was investigated in rats exposed to duodenogastric juice of different pH. The rats were divided into three groups: low-pH group (group A), high-pH group (group B) and a sham-operated group as a control (group C) (n = 30 rats in each group). The incidence of esophagitis, Barrett's esophagus (BE), intestinal metaplasia with dysplasia and EAC was observed 40 wk after the treatment. RESULTS: The incidence rate of esophagitis, BE, intestinal metaplasia with dysplasia and EAC was higher in groups A and B compared with the control group after 40 wk (P < 0.01), being 96% and 100% (P > 0.05), 88% and 82.4% (P > 0.05), 20% and 52.1% (P < 0.05), and 8% and 39% (P < 0.05), respectively. CONCLUSION: Non-acidic refluxate increases the occurrence of intestinal metaplasia with dysplasia and EAC while the low-pH gastric juice exerts a protective effect in the presence of duodenal juice. The non-acid reflux is particularly important in the progression from BE to cancer. Therefore, control of duodenal reflux may be an important prophylaxis for EAC.

[Characterization of the ectC gene and its expression product in Halomonas sp. Nj223 from Antarctica deep-sea sediment].

A moderately halophilic bacterium Halomonas sp. NJ223 was isolated from Antarctica deep-sea sediment. This bacterium accumulates ectoine as the main compatible solute in response to severe osmotic stress. Ecoine synthase catalyzes circulation of gamma-N-acetyl-alpha, gamma-diaminobutyric acid (ADABA) to ectoine in the last step of the three enzymatic steps. The gene of ectoine synthase from this strain was amplified by PCR and the DNA sequence of a 393-bp segment was sequenced. The amino acid sequences of this enzyme present high homology to the known sequence. The significance of this gene was proved by the expression in Escherichia coli. Thus, the amplified fragment was cloned into the expression vector pET-his. The insert position, the size and the reading frame were identified by PCR, restriction digestion and the sequence analysis of the recombinant plasmids. SDS-PAGE shows that the relative molecular mass of the expression product was 15 kDa as predicted, which indicated that the recombinant plasmids could express the gene of ectoine synthase. The biosynthetic pathway of ectoine was partially elucidated by renaturation and enzyme activity detection of purified ectoine synthase in vitro. Determination of effect of pH and temperature on enzyme activity shows that the optimal reaction condition of pH was 8.0 and temperature was 25 degrees C.