Increased maternal consumption of methionine as its hydroxyl analog promoted neonatal intestinal growth without compromising maternal energy homeostasis
In order to gain more insight into the adaptative mechanism of intestinal enzymes to dietary factors in rats, modifications in the activities of disaccharidases and aminopeptidase were measured after refeeding of a 70% solution of sucrose for 15 h following a 2-day fast. Mature epithelial cells from the villus and immature cells from the crypt were isolated after sequential removal of the cells along the villus-crypt axis. Synthesis of brush border disaccharidases was determined by measuring [3H]valine incorporation into proteins. 1. In the whole mucosa, a highly significant increase in sucrase and maltase activities and a significant drop in aminopeptidase activity was observed in the brush border membranes after sucrose refeeding. 2. Stimulation of sucrase and maltase activities in sucrose refed rats was produced mainly in the immature cells of the crypt and lower villus compartment. 3. After separation of the brush border proteins by SDS gel electrophoresis from villus and crypt cells of sucrose refed rats, major incorporation of the radioactive precursor occured in the protein bands corresponding to sucrase and maltase activities of the lower villus and crypt cell brush borders. These findings demonstrate that sucrase stimulation by sucrose occurs mainly in the immature epithelial cells and that the substrate induces de novo synthesis of sucrase molecules.