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A cloned CCK-A receptor transduces multiple signals in response to full and partial agonists


, : A cloned CCK-A receptor transduces multiple signals in response to full and partial agonists. American Journal of Physiology 265(5 Pt 1): G999-1004

Chinese hamster ovary (CHO) cells, stably transfected with the cloned rat CCK-A receptor, were used to study signal transduction events initiated by cholecystokinin octapeptide (CCK-8) and the partial agonist JMV-180. In single CHO-CCK-A cells loaded with fura-2, superfusion of CCK-8 (10 pM-1 nM) resulted in an increase in intracellular Ca-2+ concentration ((Ca-2+)-i). At CCK-8 concentrations lt 100 pM, the signal consisted of (Ca-2+)-i, oscillations. At higher concentrations, CCK-8 induced a typical biphasic response consisting of a large peak followed by a lower sustained plateau. Superfusion of JMV-180 also resulted in an increase in (Ca-2+)-i; in contrast to acinar cells this increase did not consist exclusively of (Ca-2+)-i oscillations. Both CCK-8 and JMV-180 increased polyphosphoinositide hydrolysis, although JMV-180 stimulated formation of only 10% as much (3H)inositol phosphates. (Ca-2+)-i signals stimulated by both CCK-8 and JMV-180 were blocked by the aminosteroid U-73122. CCK-8 (1-10 nM) increased formation of adenosine 3',5'-cyclic monophosphate (cAMP) and release of arachidonic acid in CHO-CCK cells. These increases were not mimicked by JMV-180 (10 mu-M). Furthermore, no cAMP formation or arachidonate release could be detected when cells were incubated with both JMV-180 and CCK-8. These data indicate that in CHO-CCK-A cells, unlike acinar cells, both CCK-8 and JMV-180 increase (Ca-2+)-i by similar mechanisms. However, the CCK-A receptor can differentially recognize and then activate discrete transduction pathways on binding of these two agonists.

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PMID: 8238528


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