Age-related differences in receptors for Escherichia coli heat-stable enterotoxin in the small and large intestine of children.

Escherichia coli that produce heat-stable enterotoxin are a worldwide cause of diarrheal disease, especially in children. We examined small and large intestinal specimens from children of various ages for the presence of E. coli heat-stable entero-toxin receptors and determined whether the number of receptors or the binding affinity of these receptors was related to the age of the child. We observed specific binding of 125I-heat-stable enterotoxin to all small intestinal and colonic specimens. However, a greater number of receptors per microgram of membrane protein were present in infants and the number of receptors rapidly decreased with increasing age. We also observed that increased heat-stable enterotoxin stimulation of guanylate cyclase was correlated with increased receptor density. We suggest that a greater number of gastrointestinal receptors for heat-stable enterotoxin, capable of activating more guanylate cyclase, may contribute to the increased severity of diarrhea noted in young children exposed to enterotoxigenic E. coli

Binding of E. coli heat-stable enterotoxin to rat intestinal brush borders and to basolateral membranes.

We studied the binding of E. coli heat-stable enterotoxin (STa) to rat brush borders (BB) and to basolateral membranes (BLM) using a biologically active monoiodinated radioligand [( 125I]STa) and highly enriched BB and BLM preparations free of other significant organelle contamination. Binding of [125I]STa to BB was specific; time-, temperature-, and pH-dependent; saturable; and partially reversible. Nonlabeled toxin competitively inhibited the binding of radioligand to BB in a dose-related manner. Scatchard analysis revealed a single class of receptors with an apparent affinity constant of 8.7 +/- 1.5 X 10(8) l/mol. Binding was not affected by amino acids, sugars, and lectins. Proteolytic enzymes significantly decreased binding, although several did so by modifying the radioligand. Trypsin inhibited binding without modifying the radioligand thus supporting the proteinaceous nature of the receptor. Since the enrichment in binding activity in the BB over the homogenate was significantly lower than the enrichment in sucrase activity, we concluded that binding activity is probably associated with other membranous domains, but direct examination revealed no binding activity on basolateral membranes