Exendin-3, a novel peptide from Heloderma horridum venom, interacts with vasoactive intestinal peptide receptors and a newly described receptor on dispersed acini from guinea pig pancreas. Description of exendin-3(9-39) amide, a specific exendin receptor antagonist.
Open Access
- 1 February 1991
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 266 (5) , 2897-2902
- https://doi.org/10.1016/s0021-9258(18)49932-2
Abstract
No abstract availableKeywords
This publication has 9 references indexed in Scilit:
- Purification and structure of exendin-3, a new pancreatic secretagogue isolated from Heloderma horridum venomJournal of Biological Chemistry, 1990
- Receptors and Cell Activation Associated with Pancreatic Enzyme SecretionAnnual Review of Physiology, 1986
- Comparison of mammalian VIP bioactivities in dispersed acini from guinea pig pancreasRegulatory Peptides, 1986
- Interaction of Growth Hormone-Releasing Factor (GRF) and 14 GRF Analogs with Vasoactive Intestinal Peptide (VIP) Receptors of Rat Pancreas. Discovery of (N-Ac-Tyr1,D-Phe2)-GRF(l-29)-NH2as a VIP Antagonist*Endocrinology, 1985
- Primary structure of helodermin, a VIP‐secretin‐like peptide isolated from Gila monster venomFEBS Letters, 1984
- Amino acid sequences of helospectins, new members of the glucagon superfamily, found in Gila monster venom.Journal of Biological Chemistry, 1984
- Interaction of secretin5–27 and its analogues with hormone receptors on pancreatic aciniBiochimica et Biophysica Acta (BBA) - General Subjects, 1979
- Interaction of porcine vasoactive intestinal peptide with dispersed pancreatic acinar cells from the guinea pig. Binding of radioiodinated peptide.Journal of Biological Chemistry, 1976
- A new and rapid method for the clinical determination of α-amylase activities in human serum and urine. optimal conditionsClinica Chimica Acta; International Journal of Clinical Chemistry, 1969