Influence of duodenal secretions and its components on release and activities of human brush-border enzymes.
The in vitro effects of human duodenal secretions and various combinations of its components on activity and release of enzymes from the human brush border were examined. Sucrase retained activity for 90 min in duodenal secretions, and maltase was almost as stable; lactase lost activity rapidly and alkaline phosphatase was of intermediate stability. Inactivation of lactase could only be partly (50%) attributed to luminal proteases, bile salts and phospholipids played no role. Rate of release of an enzyme from the brush border bore no relationship to its rate of inactivation. When individual proteases were studied, elastase was the most potent for releasing disaccharidases from the brush border; trypsin was ineffective alone but augmented the effect of elastase. Sucrase and maltase were activated by proteolytic release, but activation was abolished by simultaneous exposure of brush borders to bile salts. Lactase was released and rapidly inactivated by proteinases, while alkaline phosphatase appeared to be inactivated without significant release. These results show that there are significant interactions between luminal factors which have been inapparent when studying them in isolation. Loss of functionally useful enzyme does not follow release of sucrase or maltase from the brush border into the lumen but does follow release of lactase. Study of the susceptibility of lactase to inactivation by luminal factors in the various forms of lactose intolerance is warranted.
Young
G P
GP
University of Melbourne, Department of Medicine, Royal Melbourne Hospital, Australia.
Das
L
L
D000469:Alkaline Phosphatase / Q000378:metabolism; D001647:Bile Acids and Salts / Q000494:pharmacology; D004386:Duodenum / Q000378:metabolism*; D004789:Enzyme Activation / Q000187:drug effects; D006801:Humans; D007421:Intestine, Small / Q000648:ultrastructure*; D007700:Kinetics; D008871:Microvilli / Q000201:enzymology*; D010196:Pancreatic Elastase / Q000494:pharmacology; D010743:Phospholipids / Q000494:pharmacology; D011480:Protease Inhibitors / Q000494:pharmacology; D013393:Sucrase / Q000378:metabolism; D014357:Trypsin / Q000494:pharmacology; D000520:alpha-Glucosidases / Q000378:metabolism; D001616:beta-Galactosidase / Q000378:metabolism
D001647:Bile Acids and Salts; D010743:Phospholipids; D011480:Protease Inhibitors; D000469:Alkaline Phosphatase; D000520:alpha-Glucosidases; D001616:beta-Galactosidase; D013393:Sucrase; D010196:Pancreatic Elastase; D014357:Trypsin