Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1988-12-19
pubmed:abstractText
Inactivation of dynorphin-(1-8) in three in vitro isolated preparations, guinea-pig ileum, mouse vas deferens and rabbit vas deferens, was estimated by employing the relatively specific inhibitors of enkephalin-hydrolyzing enzymes. All three enzyme inhibitors, amastatin, captopril and phosphoramidon, significantly enhanced the inhibitory potency of dynorphin-(1-8) in the three isolated preparations. The magnitude of the enhancement of the dynorphin potency by captopril was significantly higher than that by either amastatin or phosphoramidon in guinea-pig ileum; that by amastatin was significantly higher than that by either captopril or phosphoramidon in rabbit vas deferens; and that by amastatin was similar to that by captopril, but significantly higher than that by phosphoramidon in mouse vas deferens. The Ke values of three antagonists, naloxone, Mr 2266 and ICI 154129, against dynorphin-(1-8) in the presence of the three peptidase inhibitors indicated that dynorphin-(1-8) acted on kappa receptors in guinea-pig ileum and on both kappa and delta receptors in mouse vas deferens. Since amastatin, captopril and phosphoramidon produced the naloxone-reversible inhibition of contractions of guinea-pig ileum in the presence of dynorphin-(1-8), all three dynorphin-inactivating enzymes were indicated to be located very close to kappa receptors.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Aminopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/Anti-Bacterial Agents, http://linkedlifedata.com/resource/pubmed/chemical/Captopril, http://linkedlifedata.com/resource/pubmed/chemical/Dynorphins, http://linkedlifedata.com/resource/pubmed/chemical/Glycopeptides, http://linkedlifedata.com/resource/pubmed/chemical/Hypothalamic Hormones, http://linkedlifedata.com/resource/pubmed/chemical/Neprilysin, http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides, http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments, http://linkedlifedata.com/resource/pubmed/chemical/Peptides, http://linkedlifedata.com/resource/pubmed/chemical/Peptidyl-Dipeptidase A, http://linkedlifedata.com/resource/pubmed/chemical/Protease Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/amastatin, http://linkedlifedata.com/resource/pubmed/chemical/dynorphin (1-8), http://linkedlifedata.com/resource/pubmed/chemical/phosphoramidon
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-5198
pubmed:author
pubmed:issnType
Print
pubmed:volume
47
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
417-23
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:2903264-Aminopeptidases, pubmed-meshheading:2903264-Animals, pubmed-meshheading:2903264-Anti-Bacterial Agents, pubmed-meshheading:2903264-Captopril, pubmed-meshheading:2903264-Dynorphins, pubmed-meshheading:2903264-Glycopeptides, pubmed-meshheading:2903264-Guinea Pigs, pubmed-meshheading:2903264-Hypothalamic Hormones, pubmed-meshheading:2903264-Male, pubmed-meshheading:2903264-Mice, pubmed-meshheading:2903264-Mice, Inbred ICR, pubmed-meshheading:2903264-Muscle, Smooth, pubmed-meshheading:2903264-Muscle Contraction, pubmed-meshheading:2903264-Neprilysin, pubmed-meshheading:2903264-Oligopeptides, pubmed-meshheading:2903264-Peptide Fragments, pubmed-meshheading:2903264-Peptides, pubmed-meshheading:2903264-Peptidyl-Dipeptidase A, pubmed-meshheading:2903264-Protease Inhibitors, pubmed-meshheading:2903264-Rabbits
pubmed:year
1988
pubmed:articleTitle
Inactivation of dynorphin-(1-8) in isolated preparations by three peptidases.
pubmed:affiliation
Department of Pharmacology, School of Medicine, Tokai University, Isehara, Japan.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't