ENDOGENOUS INHIBITOR OF DYNORPHIN CONVERTING ENZYME IN HUMAN CEREBROSPINAL FLUID

摘要

Dynorphin converting enzymes are a recently identified group of proteinases capable of converting the dynorphin-related opioid peptides to enkephalins. These enzymes convert the kappa-receptor specific dynorphins to delta-receptor specific enkephalins, and may play an important role by releasing ligands mediating analgesic activity, and act in drug dependence mechanisms. One of these enzymes is a serine peptidase present in human and rat cerebrospnal fluids (CSF). Little is known about the regulation of the activity of neuropeptide peptidases in the CNS. Recently, we described our preliminary finding of a protein in the CSF possessing inhibitory activity against a dynorphin converting enzyme isolated from CSF. Here, we present a more detailed study on the identification and properties of this inhibitor, which also inhibited other serine proteases such as trypsin, chymotrypsin and plasmin.