title: Dipeptidyl peptidase-II activity in cultured astroglial cells from neonatal rat brain.
abstract: Astrocytic glial cells in primary culture from neonatal rat brain possess prominent dipeptidyl peptidase-II activity. This enzyme has been previously isolated and purified from whole brain tissue. The glial enzyme characteristically hydrolyzed glycyl-proline-p-nitroanilide (GPN) substrate to release glycyl-proline dipeptide plus p-nitroaniline products. At the enzyme's optimal pH of 5.4, the activities of other tested amino exopeptidases were virtually zero. At pH greater than 8, activity was less than 2% of the activity at pH 5.4, which suggested a paucity of the related enzyme, dipeptidyl peptidase-IV. No competitive inhibition was observed for glycine, proline nor their permuted dipeptides. Glial dipeptidyl peptidase-II activity was strongly inhibited by Hg2+, while other redox sulfhydryl agents were ineffective. Tested cations did not affect activity, except K+ which was mildly inhibitory. Chelating agents were not inhibitory. Of the peptidase inhibitors tested, only phenylmethylsulfonyl fluoride and puromycin were partially inhibitory. We suggest that dipeptidyl peptidase-II may play a role in glial processing of brain peptides which possess an N-terminal penultimate proline residue.
mesh_terms: D000818:Animals; D000831:Animals, Newborn; D001253:Astrocytes / Q000201:enzymology*; D002412:Cations / Q000494:pharmacology; D002478:Cells, Cultured; D002614:Chelating Agents / Q000494:pharmacology; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D010447:Peptide Hydrolases / Q000378:metabolism; D011480:Protease Inhibitors / Q000494:pharmacology; D051381:Rats; D013379:Substrate Specificity; D013439:Sulfhydryl Reagents / Q000494:pharmacology
chemical_list: D002412:Cations; D002614:Chelating Agents; D011480:Protease Inhibitors; D013439:Sulfhydryl Reagents; D010447:Peptide Hydrolases; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; C100151:dipeptidyl peptidase II