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2‐DE and MS analysis of interactions between Lactobacillus fermentum I5007 and intestinal epithelial cells
Author(s) -
Yang Fang,
Wang Junjun,
Li Xiaojie,
Ying Tianyi,
Qiao Shiyan,
Li Defa,
Wu Guoyao
Publication year - 2007
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.200700166
Subject(s) - biochemistry , lactobacillus fermentum , lactate dehydrogenase , lactobacillus reuteri , biology , dehydrogenase , microbiology and biotechnology , enzyme , lactobacillus plantarum , chemistry , lactobacillus , bacteria , lactic acid , fermentation , genetics
Lactobacillus is a probiotic commonly used for supplementation to human and animal diets. In this study, we used 2‐DE and MS to analyze changes in the proteomes of Lactobacillus and intestinal epithelial cells in two model systems. The in vivo and in vitro models were involved the inoculation of Lactobacillus fermentum I5007 into the rabbit jejunum for 4 h and the culture of the bacterium with Caco‐2 cells for 1 h, respectively. Our results indicate that, after exposure to the intestinal environment, the bacterium exhibited decreases in key enzymes involved in energy metabolism ( e.g. , lactate dehydrogenase, dihydrolipoamide dehydrogenase, and nicotinate phosphoribosyltransferase) and amino acid metabolism ( e.g. , arginyl‐tRNA synthetase and aspartate‐semialdehyde dehydrogenase), but increases in glycoside hydrolase (an enzyme for mucin degradation) and fructose‐6‐phosphate phosphoketolase (an enzyme of the pentose phosphate pathway). In response to an interaction with L. fermentum I5007, Caco‐2 cells showed changes in proteins that were beneficial for gut integrity, including voltage‐dependent anion channel 1, glutathione transferase, and heat shock protein gp96. On the basis of their functions, we suggest that these proteins serve as useful biomarkers for metabolic changes in Lactobacillus and intestinal epithelial cells in response to their interactions.