Characterization and inhibition of a cholecystokinin-inactivating serine peptidase

  • Nature. 1996 Apr 4;380(6573):403-9. doi: 10.1038/380403a0.
C Rose  1 ,  F Vargas ,  P Facchinetti ,  P Bourgeat ,  R B Bambal ,  P B Bishop ,  S M Chan ,  A N Moore ,  C R Ganellin ,  J C Schwartz
Affiliations
  • 1. Unité de Neurobiologie et Pharmacologie de l'INSERM, Centre Paul Broca, Paris, France.
PMID: 8602240 DOI: 10.1038/380403a0
Abstract

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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