Nature (London), 1996-04, Vol.380 (6573), p.403-409
1996
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Details
- Autor(en) / Beteiligte
- Titel
- Characterization and inhibition of a cholecystokinin-inactivating serine peptidase
- Ist Teil von
- Nature (London), 1996-04, Vol.380 (6573), p.403-409
- Ort / Verlag
- London: Nature Publishing
- Erscheinungsjahr
- 1996
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- A cholecystokinin (CCK)-inactivating peptidase was purified and identified as a membrane-bound isoform of tripeptidyl peptidase II (EC 3.4.14.10), a cytosolic subtilisin-like peptidase of previously unknown functions. The peptidase was found in neurons responding to cholecystokinin, as well as in non-neuronal cells. Butabindide, a potent and specific inhibitor, was designed and shown to protect endogenous cholecystokinin from inactivation and to display pro-satiating effects mediated by the CCKA receptor.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0028-0836eISSN: 1476-4687DOI: 10.1038/380403a0Titel-ID: cdi_proquest_miscellaneous_77966614
- Format
- –
- Schlagworte
- Amino Acid Sequence, Aminopeptidases, Analytical, structural and metabolic biochemistry, Animals, Base Sequence, Biological and medical sciences, Catalysis, Cell Membrane - enzymology, Cerebral Cortex - enzymology, Cholecystokinin - antagonists & inhibitors, Dipeptidyl-Peptidases and Tripeptidyl-Peptidases, DNA, Enzymes and enzyme inhibitors, Fundamental and applied biological sciences. Psychology, Humans, Hydrolases, Hydrolysis, Inactivation, Indoles - chemical synthesis, Indoles - pharmacology, Membranes, Mice, Molecular Sequence Data, Neurons, Peptide Fragments - metabolism, Peptides, Protease Inhibitors - chemical synthesis, Protease Inhibitors - metabolism, Rats, Sequence Homology, Amino Acid, Serine Endopeptidases - chemical synthesis, Serine Endopeptidases - isolation & purification, Serine Endopeptidases - metabolism, Substrate Specificity, Type C Phospholipases - metabolism