Experimental pancreatitis is mediated by low-affinity cholecystokinin receptors that inhibit digestive enzyme secretion.

Abstract

Rats infused with a supramaximally stimulating dose of the cholecystokinin (CCK) analog caerulein develop acute edematous pancreatitis. Using CCK-JMV-180, a recently developed CCK analog that acts as an agonist at high-affinity CCK receptors but antagonizes the effect of CCK at low-affinity receptors, we have determined that caerulein induces pancreatitis by interacting with low-affinity CCK receptors. Those low-affinity receptors mediate CCK-induced inhibition of digestive enzyme secretion from the pancreas. Our observations, therefore, suggest that this form of experimental pancreatitis results from the inhibition of pancreatic digestive enzyme secretion.

• Authors: A K Saluja, M Saluja, H Printz, A Zavertnik, A Sengupta, M L Steer
• Journal: Proceedings of the National Academy of Sciences of the United States of America (Proc Natl Acad Sci U S A) Vol. 86 Issue 22 Pg. 8968-71 (Nov 1989) ISSN: 0027-8424 [Print] United States
• PMID: 2479032 (Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Receptors, Cholecystokinin
• JMV 180
• Ceruletide
• Amylases
• Sincalide

Topics

• Acute Disease
• Amylases (metabolism)
• Animals
• Ceruletide (toxicity)
• Kinetics
• Male
• Pancreas (drug effects, enzymology, pathology)
• Pancreatitis (chemically induced, metabolism)
• Rats
• Rats, Inbred Strains
• Receptors, Cholecystokinin (drug effects, metabolism)
• Sincalide (analogs & derivatives, pharmacology)