Characterization and inhibition of a cholecystokinin-inactivating serine peptidase.
作者信息
Rose C, Vargas F, Facchinetti P, Bourgeat P, Bambal R B, Bishop P B, Chan S M, Moore A N, Ganellin C R, Schwartz J C
机构信息
Unité de Neurobiologie et Pharmacologie de l'INSERM, Centre Paul Broca, Paris, France.
出版信息
Nature. 1996 Apr 4;380(6573):403-9. doi: 10.1038/380403a0.
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.
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