Functional interaction of Escherichia coli heat-labile enterotoxin with blood group A-active glycoconjugates from differentiated HY29 cells

GALVÁN EM, ROTH GA, MONFERRAN CG

The FEBS Journal

Blackwell Synergy

Año: 2006 vol. 273 p. 3444 - 3444

1742-464X

p class="MsoNormal" style="MARGIN: 0cm 0cm 0pt; tab-stops: 21.3pt">Human colon adenocarcinoma cells, HT29-ATCC and the clone HT29-5F7 were cultured in conditions that differentiate cells to a polarized intestinal phenotype. Differentiated cells showed the presence of junctional complexes and intercellular lumina bordered by microvilli. Intestinal brush border hydrolase activities (sucrase, aminopeptidase N, lactase and maltase) were detected mainly in differentiated HT29-ATCC cells compared with the differentiated clone HT29-5F7. The presence of non-GM1 receptors of Escherichia coli heat-labile enterotoxin (LT-I) on both differentiated HT29 cells was indicated by the inability of cholera toxin B subunit (CT-B) to block LT-I binding to cells. Binding of LT-I to cells, when GM1 was blocked by CT-B was characterized by an increased number of LT-I receptors with respect to