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Entamoeba histolytica : collagen‐induced AP‐1 DNA binding activity
Author(s) -
Pérez Eduardo,
Muñoz Marıća de Lourdes,
Ortega Arturo
Publication year - 1998
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.1574-6968.1998.tb12859.x
Subject(s) - entamoeba histolytica , immunoprecipitation , microbiology and biotechnology , biology , collagenase , paxillin , signal transduction , activator (genetics) , western blot , focal adhesion , receptor , gene , biochemistry , enzyme
Abstract The interaction of Entamoeba histolytica trophozoites with collagen induces the synthesis and release of electron‐dense granules containing a collagenase activity that is an important factor in the pathogenicity of the parasite. The binding is thought to be mediated by an ‘integrin‐like’ collagen receptor. In the signal transduction mechanisms activated by collagen, pp125 FAK and p42 MAPK are involved. Using immunoprecipitation assays coupled to Western blot analysis, we demonstrate here the collagen‐dependent association of paxillin and Src with pp125 FAK . Furthermore, collagen induces a time‐dependent increase in the DNA binding activity of the activator protein 1, which is well correlated with an increase in Fos expression. Our results suggest that a stimulus‐transcription coupling triggered by collagen in E. histolytica trophozoites might activate or repress genes involved in tissue invasiveness.

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