Abstract:
:Examining the actions of L-364,718 on rat pancreatic acini, we found that L-364,718 causes persistent inhibition of cholecystokinin (CCK)-8-stimulated enzyme secretion in acini that were first incubated with L-364,718, washed repeatedly, and then reincubated with CCK-8. This inhibition is maximal after as little as 5 s of first incubation with L-364,718, is unaltered by reducing the temperature of the first incubation from 37 to 4 degrees C and is specific for CCK-8 in that carbachol-stimulated enzyme secretion is unaltered. The inhibitory potency of L-364,718 added to the first incubation followed by washing and reincubation with CCK-8 is nearly the same as when L-364,718 is added together with CCK-8 in the same incubation. The persistent inhibitory action of L-364,718 is not attributable to residual free L-364,718 in the bulk phase of the second incubation medium. In addition, L-364,718 does not cause persistent inhibition by binding irreversibly to CCK receptors because the binding reaction is completely reversible and the persistent inhibition can be surmounted with appropriate concentrations of CCK-8. When acini are first incubated with L-364,718 and washed repeatedly, approximately 0.2% of the original L-364,718 remains trapped in a microenvironment within the acini. This trapping presumably results in a sufficiently high concentration of L-364,718 to produce its persistent, albeit surmountable inhibition.
journal_name
Pancreasjournal_title
Pancreasauthors
Bhat ST,Talkad VD,Pollo DA,Gardner JDdoi
10.1097/00006676-199401000-00015subject
Has Abstractpub_date
1994-01-01 00:00:00pages
101-8issue
1eissn
0885-3177issn
1536-4828journal_volume
9pub_type
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