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J. Biol. Chem., Vol. 267, Issue 11, 7402-7405, Apr, 1992
J Eng, WA Kleinman, L Singh, G Singh and JP Raufman
The recent identification in Heloderma horridum venom of exendin-3, a new
member of the glucagon superfamily that acts as a pancreatic secretagogue,
prompted a search for a similar peptide in Heloderma suspectum venom. An
amino acid sequencing assay for peptides containing an amino-terminal
histidine residue (His1) was used to isolate a 39- amino acid peptide,
exendin-4, from H. suspectum venom. Exendin-4 differs from exendin-3 by two
amino acid substitutions, Gly2-Glu3 in place of Ser2-Asp3, but is otherwise
identical. The structural differences make exendin-4 distinct from
exendin-3 in its bioactivity. In dispersed acini from guinea pig pancreas,
natural and synthetic exendin-4 stimulate a monophasic increase in cAMP
beginning at 100 pM that plateaus at 10 nM. The exendin-4-induced increase
in cAMP is inhibited progressively by increasing concentrations of the
exendin receptor antagonist, exendin-(9-39) amide. Unlike exendin-3,
exendin-4 does not stimulate a second rise in acinar cAMP at concentrations
greater than 100 nM, does not stimulate amylase release, and does not
inhibit the binding of radiolabeled vasoactive intestinal peptide to acini.
This indicates that in dispersed pancreatic acini, exendin-4 interacts only
with the recently described exendin receptor.
Isolation and characterization of exendin-4, an exendin-3 analogue, from Heloderma suspectum venom. Further evidence for an exendin receptor on dispersed acini from guinea pig pancreas
Solomon A. Berson Research Laboratory, Veterans Affairs Medical Center, Bronx, New York 10468.
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