Abstract
The expression and mode of glycosylation of sucrase-isomaltase (SI) and dipeptidyl peptidase IV (DPP IV) have been studied in HT-29 cells grown with glucose (undifferentiated) or inosine (differentiated) as carbon-source. 10-day-confluent cells were labelled with 35S-methionine, immunoprecipltated with monoclonal antibodies and analysed by SDS-PAGE. The mode of glycosylation was determined by treatment of immunoisolated proteins with endo H, endo F and trifluormethane sulfonic acid (TFMS). In differentiated HT-29 cells biosynthesis and processing of these two markers was as in normal enterocytes, although the level of expression was lower. Undifferentiated HT-29 cells showed a very low level of expression of SI whereas the amount of DPP IV expressed was not appreciably altered. There was however a significant increase in molecular weight of the mature DPP IV in differentiated cells. This size-difference has been shown to be partially due to increased O-linked glycosylation of DPP IV in differentiated HT-29 cells.
Conclusion: The changes observed in the expression and the posttranslational processing of SI and DPP IV thus represent molecular key-events in the differentiation of HT-29 cells and provide us with a working model to study exogenous factors that influence differentiation-state of small intestinal epithelial cells.
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Sterchi, E., Naim, H. & Lentze, M. 48 DIFFERENTIATION OF HT-29 CELLS: EFFECT ON THE BIOSYNTHESIS AND GLYCOSYLATION OF SUCRASE-ISOMALTASE AND DIPEPTIDYL PEPTIDASE IV. Pediatr Res 24, 413 (1988). https://doi.org/10.1203/00006450-198809000-00071
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DOI: https://doi.org/10.1203/00006450-198809000-00071