Open AccessThe Inactivation of [Met5]-Enkephalin by Bestatin-Sensitive Aminopeptidase, Captopril-Sensitive Peptidyl Dipeptidase A and Thiorphan-Sensitive Endopeptidase-24.11 in Mouse Vas Deferens
Author(s) -
Kazuko Aoki,
Midori Kajiwara,
Tetsuo Oka
Publication year - 1986
Publication title -
japanese journal of pharmacology/japanese journal of pharmacology
Language(s) - English
Resource type - Journals
eISSN - 1347-3506
pISSN - 0021-5198
DOI - 10.1254/jjp.40.297
Subject(s) - thiorphan , vas deferens , aminopeptidase , enkephalin , endopeptidase , captopril , chemistry , ileum , leupeptin , endocrinology , medicine , carboxypeptidase , biochemistry , enzyme inhibitor , biology , enzyme , protease , opioid , amino acid , leucine , receptor , blood pressure
The enkephalin-hydrolyzing peptidases in mouse vas deferens were studied and compared with those in guinea pig ileum which had been characterized in the previous study. The present results showed that three distinct peptidases, bestatin-sensitive aminopeptidase, captopril-sensitive peptidyl dipeptidase A, and thiorphan-sensitive endopeptidase-24.11, played a critical role in the inactivation of enkephalin in mouse vas deferens, being consistent with the previous results obtained with guinea pig ileum. However, the data in both previous and present studies showed that the activity of the bestatin-sensitive aminopeptidase relative to that of either the captopril-sensitive peptidyl dipeptidase A or the thiorphan-sensitive endopeptidase-24.11 in guinea pig ileum was higher than that in mouse vas deferens, while the activity of either peptidyl dipeptidase A or endopeptidase-24.11 relative to that of aminopeptidase in mouse vas deferens was higher than that in guinea-pig ileum. In contrast to these three enzymes, both L-tyrosyl-L-tyrosine-sensitive dipeptidyl aminopeptidase and D-phenylalanine-sensitive carboxypeptidase were suggested not to be involved significantly in the inactivation of enkephalin in mouse vas deferens as well as guinea pig ileum.