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Receptor occupation, calcium mobilization, and amylase release in pancreatic acini: effect of CCK-JMV-180

Receptor occupation, calcium mobilization, and amylase release in pancreatic acini: effect of... cholecystokinin octapeptide; rat; fura- release appears to correlate with occupation of low-affinity CCK receptors. CCK-stimulated mobilization of cellular calcium is believed to be caused by receptor-mediated hydrolysis of phosphatidylinositol (11, 19, 24, 27, 28) and to play an important role in stimulus-secretion coupling in pancreatic acini (11). This calcium mobilization is thought to be caused by occupation of high-affinity CCK receptors because the dose-response curve for calcium mobilization, measured by radioactive calcium outflux (8, 15) or by a calcium-selective fluorescent indicator (1, 16, 23), appears to correlate with the upstroke of the dose-response curve for CCK-stimulated amylase release and with occupation of high-affinity CCK receptors (1, 8, 15, 16, 23). is a synthetic analogue of the COOHterminal heptapeptide of CCK having the structure BocTyr(SO,)-Nle-Gly-Trp-Nle-Asp-2-phenylethyl ester (5). As reported recently (5), is unique in that it can distinguish high-affinity CCK receptors from lowaffinity CCK receptors on the basis of its biological activity and would appear to be a useful tool for examining the relationships between occupation of each class of CCK receptor and the accompanying changes in cellular calcium and enzyme secretion. In the present study, we have examined the relationship of receptor occupation, calcium mobilization, and stimulated amylase http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png AJP - Gastrointestinal and Liver Physiology The American Physiological Society

Receptor occupation, calcium mobilization, and amylase release in pancreatic acini: effect of CCK-JMV-180

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Publisher
The American Physiological Society
Copyright
Copyright © 1989 the American Physiological Society
ISSN
0193-1857
eISSN
1522-1547
Publisher site
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Abstract

cholecystokinin octapeptide; rat; fura- release appears to correlate with occupation of low-affinity CCK receptors. CCK-stimulated mobilization of cellular calcium is believed to be caused by receptor-mediated hydrolysis of phosphatidylinositol (11, 19, 24, 27, 28) and to play an important role in stimulus-secretion coupling in pancreatic acini (11). This calcium mobilization is thought to be caused by occupation of high-affinity CCK receptors because the dose-response curve for calcium mobilization, measured by radioactive calcium outflux (8, 15) or by a calcium-selective fluorescent indicator (1, 16, 23), appears to correlate with the upstroke of the dose-response curve for CCK-stimulated amylase release and with occupation of high-affinity CCK receptors (1, 8, 15, 16, 23). is a synthetic analogue of the COOHterminal heptapeptide of CCK having the structure BocTyr(SO,)-Nle-Gly-Trp-Nle-Asp-2-phenylethyl ester (5). As reported recently (5), is unique in that it can distinguish high-affinity CCK receptors from lowaffinity CCK receptors on the basis of its biological activity and would appear to be a useful tool for examining the relationships between occupation of each class of CCK receptor and the accompanying changes in cellular calcium and enzyme secretion. In the present study, we have examined the relationship of receptor occupation, calcium mobilization, and stimulated amylase

Journal

AJP - Gastrointestinal and Liver Physiology – The American Physiological Society

Published: Aug 1, 1989

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