Infection with Campylobacter jejuni induces tyrosine-phosphorylated proteins into INT-407 cells |
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Authors: | Biswas Debabrata Niwa Hidekazu Itoh Kikuji |
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Affiliation: | Laboratory of Veterinary Public Health, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Japan. |
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Abstract: | The mechanisms used by Campylobacter jejuni to induce internalization into host intestinal epithelial cells have not been defined. In this study, we obtained evidence that exposure of INT-407 cells to protein kinase inhibitors results in decreased invasion of these cells by C. jejuni in a dose dependent manner. Preincubation of INT-407 cells in the presence of staurosporine, tyrphostin 46 and genistein decreased invasion of these cells by C. jejuni significantly. Moreover, C. jejuni infection of INT-407 cells induced tyrosine phosphorylation of several Triton X-100 soluble proteins with approximate molecular weights of 170, 145, 90, 60 and 55 kDa that were absent or reduced in the presence of genistein in cells after 1 hr of pretreatment. These data suggest that tyrosine protein kinase-linked pathways strongly regulate the internalization of C. jejuni into intestinal epithelial cells. |
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Keywords: | inhibitors phosphorylation campylobacter jejuni invasion tyrosine protein kinase |
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