Exposure of hamster pancreatic islets to hyaluronidase during isolation by means of
collagenase inhibits the insulinotropic action of several chemically different sulfonylureas,leucine,
and glucagon without affecting glucose-stimulated insulin secretion. This inhibition
is reversible for tolbutamide and leucine but irreversible for glucagon. Hyaluronidase
inhibits reversibly the insulinotropic action of tolbutamide without affecting that
of glucose also in mouse and rat isolated pancreatic islets. These findings suggest
the existence of functionally related pancreatic beta cell receptors for tolbutamide
and leucine different from those for glucose and glucagon and illustrate the potential
usefulness of hyaluronidase as an enzymatic probe applicable toward investigating
the cellular mechanism of action of key insulinotropic agents.
Hyaluronidase - Insulinotropic Agents - Isolated Pancreatic Islets - Stimulated Insulin
Secretion - Pancreatic Beta Cell Receptors
