Ontogeny of glutamine synthetase in rat small intestine

Abstract

Glutamine synthetase (GS) is a key enzyme involved in the endogenous biosynthesis of glutamine, an amino acid known to be essential for small intestinal metabolism and function. This study describes the ontogeny of rat small intestinal GS from fetal life through adulthood with enzyme activities, protein immunoblotting, and steady state levels of GS mRNA by RNA gel blots and dot blots. Enzyme activities progressively increased from 21 d of fetal life to 32 d postnatally, then decreased in adulthood. The amount of GS immunoreactive protein in the small intestine increased from fetal life to 10-day-old infants and persisted into adulthood. GS mRNA, as quantified by dot blots was highest at 19 d postnatally. The ontogenic changes in rat small intestinal GS appear to correspond temporally with rapid growth and weaning. The steady increase in GS enzyme activity up to 32 d of age with a subsequent drop in adulthood is not paralleled by an increase in GS mRNA or protein. These findings suggest an apparent complex regulation of the enzyme activity at a transcriptional or translational levels.