Sequence variation outside the "active" region of dog and rabbit cholecystokinin-58 results in bioactivity differences

Pancreas
Joseph R ReeveS R Vigna

Abstract

We propose that regions outside the bioactive 7-amino acid carboxyl terminus of cholecystokinin (CCK)-58 influence its biological activity. Here we evaluate if sequence variation of the N-terminal regions of rabbit and canine CCK-58 changes their biological activities. Cholecystokinin-like immunoreactivity was purified from rabbit intestinal extracts by reverse phase and ion-exchange high-performance liquid chromatography steps. The peptide was characterized by microsequence and mass spectral characterizations of the intact and tryptic peptides. Canine and rabbit CCK-58 were evaluated for their CCK1 and CCK2 receptor binding, receptor activation, and immunologic properties. The sequence of rabbit CCK-58 differs from that of canine CCK-58 in 9 of the amino terminal 40 residues. Canine CCK-58 was approximately 3-fold more potent than rabbit CCK-58 for CCK1 receptor binding and CCK2 receptor binding, but about the same potency for stimulation of amylase release from purified acinar cells. The canine peptide was 9-fold more immunoreactive than rabbit CCK-58. Canine and rabbit CCK-58 have different biological and immunologic properties that can only result from differences in their N-terminal sequences which influence the properties...Continue Reading

References

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Citations

Oct 10, 2009·American Journal of Physiology. Gastrointestinal and Liver Physiology·David N CriddleJoseph R Reeve
Jan 11, 2008·Current Opinion in Endocrinology, Diabetes, and Obesity·Gary M Green, J R Reeve
Oct 18, 2007·Current Opinion in Endocrinology, Diabetes, and Obesity·Rashmi Chandra, Rodger A Liddle
Aug 15, 2006·Biochemical and Biophysical Research Communications·Joseph R ReeveRobert C Backus
Oct 18, 2007·Current Opinion in Endocrinology, Diabetes, and Obesity
Jan 11, 2008·Current Opinion in Endocrinology, Diabetes, and Obesity

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