Characterization and Inhibition of a cholecystokinin-inactivating serine peptidase
Characterization and Inhibition of a cholecystokinin-inactivating serine peptidase
复制标题
DOI：
10.1038/380403a0
复制
发表时间：
1996-04-04
期刊：
影响因子：
64.8
通讯作者：
Schwartz, JC
中科院分区：
文献类型：
--
作者：
Rose, C;Vargas, F;Schwartz, JC
一种胆囊收缩素（CCK）失活肽酶被纯化并鉴定为三肽基肽酶II（EC 3.4）的膜结合亚型。14. 10），一种以前未知功能的胞质枯草杆菌蛋白酶样肽酶。肽酶被发现在神经元胆囊收缩素，以及在非神经元细胞。布他比德是一种有效的特异性抑制剂，可保护内源性胆囊收缩素免于失活，并显示出由CCKA受体介导的促饱效应。
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.