NDLI: Exendin-3 , a Novel Peptide from Heloderma horridurn Venom , Interacts with Vasoactive Intestinal Peptide Receptors and a Newly Described Receptor on Dispersed Acini from Guinea Pig Pancreas

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Exendin-3 , a Novel Peptide from Heloderma horridurn Venom , Interacts with Vasoactive Intestinal Peptide Receptors and a Newly Described Receptor on Dispersed Acini from Guinea Pig Pancreas

Content Provider	Semantic Scholar
Author	Jean-Pierre Raufman S. Q. Latika Singh S. Engll, John
Copyright Year	2001
Abstract	Exendin-3 increased cellular cAMP levels and amylase release from dispersed acini from guinea pig pancreas. Low concentrations (0.1-3 nM) caused a 12-fold increase in CAMP, whereas higher concentrations (0.3-3p~) caused an additional 24-fold increase in CAMP. Maximal cAMP with the highest concentration tested was the same as the maximal response with secretin, vasoactive intestinal peptide (VIP), peptide histidine isoleucine, helodermin, or helospectin-I. In terms of amylase release, exendin-3 had the same efficacy but was the least potent of these peptides. Exendin-3-induced increases in amylase release were inhibited by VIP receptor antagonists and the new peptide (>0.1 p ~ ) competed with radiolabeled VIP for binding sites on dispersed acini. Increasing concentrations of an exendin-3 fragment, exendin-3(9-39) amide, did not increase cAMP or amylase release but inhibited the increase in cAMP observed with 0.1-3 nM exendin-3. The fragment did not alter the effects of other peptides that are known to increase acinar CAMP. We conclude that exendin-3 interacts with at least two receptors on guinea pig pancreatic acini; at high concentrations (>lo0 nM) the peptide interacts with VIP receptors, thereby causing a large increase in cAMP and stimulating amylase release; at lower concentrations (0.1-3 nM) the peptide interacts with a putative exendin receptor, thereby causing a smaller increase in cAMP of undetermined function. Exendin3(9-39) amide is a specific exendin receptor antagonist.
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://www.jbc.org/content/266/5/2897.full.pdf
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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