EFFECT OF GROWTH AND SODIUM-BUTYRATE ON BRUSH-BORDER MEMBRANE-ASSOCIATED HYDROLASES IN HUMAN COLORECTAL-CANCER CELL-LINES

  • 1 January 1985
    • journal article
    • research article
    • Vol. 45  (7) , 2976-2982
Abstract
The activities of brush border membrane-associated hydrolases such as alkaline phosphatase (Alkpase), aminopeptidase, dipeptidyl aminopeptidase IV (DAP-IV), sucrase, lactase and trehalase were studied in 14 different human colorectal cancer cell lines [HRT-18, HCT-48, CaCo-2, HT-29, SW-403, SW-480, SW-116, HCT-116, HCT-116a, HCT-116b, DLD-2, HCT-15, LS174T, LoVo]. The effect of sodium butyrate, a known differentiating agent, and cell growth on the activities of these enzymes was also examined. All 14 cell lines exhibited brush border membrane enzyme activities, and in general, the activity of Alkpase, aminopeptidase and DAP-IV was much higher than the disaccharidases. The specific enzyme activities varied among different cell lines. The induction of Alkpase activity by sodium butyrate occurred in most of the 14 cell lines (2- to 123-fold), while induction of the other enzyme activities was observed in several (1.5- to 3.5-fold). In some instances, butyrate caused a decrease in enzyme activity. There was no statistically significant correlation between the induction of Alkpase activity and that of other enzyme activities by sodium butyrate. Levels of aminopeptidase and DAP-IV activity were dependent on cell density and increased 3- to 4-fold by the 10th day in most of the cell lines. Sodium butyrate altered the subcellular distribution pattern of the disaccharidases, causing a significant increase in activity associated with the soluble (cytoplasmic) fraction. Other enzymes such as Alkpase and DAP-IV continued to be predominantly associated with the membrane fraction in butyrate-treated cells. Brush border membrane hydrolase activity and the effect of sodium butyrate may provide useful information regarding the differentiation of human colorectal cancer cells.