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J. Biol. Chem., Vol. 275, Issue 25, 19115-19120, June 23, 2000

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Species Differences between Rat and Mouse CCK_A Receptors Determine the Divergent Acinar Cell Response to the Cholecystokinin Analog JMV-180^*

Baoan Ji, Alan S. Kopin^§, and Craig D. Logsdon^¶

From the  Department of Physiology, University of Michigan, Ann Arbor, Michigan 48109-0622 and ^§ Tupper Research Institute, New England Medical Center, Boston, Massachusetts 02111

The cholecystokinin (CCK) analog JMV-180 acts as a partial agonist in rats and a full agonist in mice. Whether this functional variability is due to species differences in CCK receptor structure or to alterations in the cellular environment is unknown. To address this question, an adenoviral construct encoding the rat CCK_A receptor (AdCCK_AR) was used to express the rat receptor in acini from CCK_A receptor-deficient mice (CCK_AR /). Infection of CCK_AR / acini in vitro with pAdCCK_AR led to a time-dependent increase in ¹²⁵I-CCK₈ binding. The affinity for JMV-180 of the adenovirally transferred rat and the endogenous mouse CCK_A receptors was not different. In native mouse acini, JMV-180 acted as a full agonist (both stimulation and inhibition of amylase release). In contrast, in mouse acini expressing pAdCCK_AR JMV-180 acted as a partial agonist (only stimulation of amylase release). In addition, the pattern of protein synthesis induced by JMV-180 in CCK_AR / mouse acini infected with AdCCK_AR resembled the pattern observed in wild-type rats (lack of inhibition) rather than the respective pattern in wild-type mice (inhibition). These data suggest that species differences in the CCK_A receptor of rats and mice account for the observed divergence in the acinar cell response to JMV-180.

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