Glucose up-regulates expression of the differentiation-associated brush border binding site for enterotoxigenic Escherichia coli colonization factor antigen I in cultured human enterocyte-like cells
| Autor: | Marie-Hélène Coconnier, Alain L. Servin, F Duigou, Marie-Françoise Bernet-Camard, Sophie Kernéis |
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| Rok vydání: | 1997 |
| Předmět: |
Brush border
Enterocyte Cellular differentiation Immunology Biology medicine.disease_cause complex mixtures Microbiology Bacterial Proteins Antigen Enterotoxigenic Escherichia coli Intestine Small Escherichia coli Tumor Cells Cultured medicine Humans Binding site Binding Sites Microvilli Molecular biology Up-Regulation Glucose Infectious Diseases medicine.anatomical_structure Cell culture Parasitology Fimbriae Proteins Research Article |
| Zdroj: | Infection and Immunity. 65:1299-1306 |
| ISSN: | 1098-5522 0019-9567 |
| Popis: | The association of enterotoxigenic Escherichia coli expressing colonization factor antigen I (CFA/I) with the cultured human colon adenocarcinoma cell, a model of the mature enterocyte of the small intestine, is dependent on the binding of CFA/I to a brush border-associated component. Binding of the purified radiolabeled [125I]CFA/I- and 14C-labeled CFA/I-positive bacteria could be displaced by an increasing concentration of unlabeled CFA/I. Moreover, we showed that expression of the specific CFA/I binding developed as a function of cell differentiation in Caco-2 cells, whereas expression of the nonspecific binding did not. Expression of the brush border differentiation-associated component acting as a binding site for CFA/I was up-regulated by glucose. Indeed, the enterocyte-like HT-29 glc- cell subpopulation not expressing the CFA/I binding site when cultured in dialyzed serum and hexose-free medium regained the ability to bind CFA/I when the cells were returned to culture medium containing glucose. Furthermore, expression of the brush border-associated CFA/I binding site in the enterocyte-like Caco-2 cells was repressed when the cells were cultured in hexose-free conditions. |
| Databáze: | OpenAIRE |
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