Interaction of physalaemin, substance P, and eledoisin with specific membrane receptors on pancreatic acinar cells.
- 1 November 1979
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 76 (11), 5679-5683
- https://doi.org/10.1073/pnas.76.11.5679
Abstract
125I-labeled physalaemin was prepared and the kinetics, stoichiometry and chemical specificity with which the labeled peptide binds to dispersed acini from guinea pig pancreas were examined. Binding of 125I-labeled physalaemin was saturable, temperature-dependent and reversible and reflected interaction of the labeled peptide with a single class of binding sites on the plasma membrane of pancreatic acinar cells. Each acinar cell possessed approximately 500 binding sites and binding of the tracer to these sites could be inhibited by physalaemin [concentration for half-maximal effect (Kd), 2 nM], substance P (Kd, 5 nM), or eledoisin (Kd, 300 nM) but not by cholecystokinin, caerulein, bombesin, litorin, gastrin, secretin, vasoactive intestinal peptide, glucagon, somatostatin, neurotensin, bovine pancreatic polypeptide, Leu-enkephalin, Met-enkephalin, atropine or carbamylcholine. With physalaemin, substance P and eledoisin, there was a close correlation between the relative potency for inhibition of binding of labeled physalaemin and that for stimulation of amylase secretion. For a given peptide, however, a 3-fold higher concentration was required for half-maximal inhibition of binding than for half-maximal stimulation of amylase secretion, Ca outflux or cyclic GMP accumulation. Dispersed acini from guinea pig pancreas possess a single class of receptors that interact with physalaemin, substance P and eledoisin and occupation of 45% of these receptors will cause a maximal biological response.This publication has 27 references indexed in Scilit:
- Actions of derivatives of cyclic nucleotides on dispersed acini from guinea pig pancreas. Discovery of a competitive antagonist of the action of cholecystokinin.Journal of Biological Chemistry, 1979
- Interaction of bombesin and litorin with specific membrane receptors on pancreatic acinar cellsProceedings of the National Academy of Sciences, 1978
- Effects of calcium and chelating agents on the ability of various agonists to increase cyclic GMP in pancreatic acinar cellsBiochimica et Biophysica Acta (BBA) - General Subjects, 1978
- Actions of peptides isolated from amphibian skin on pancreatic acinar cells.American Journal of Physiology-Endocrinology and Metabolism, 1978
- Mast cell binding of neurotensin. I. Iodination of neurotensin and characterization of the interaction of neurotensin with mast cell receptor sites.Journal of Biological Chemistry, 1977
- Regulation of amylase release from dispersed pancreatic acinar cells.The Journal of Physiology, 1977
- Intermediate role of adenosine 3′:5′-cyclic monophosphate and protein kinase during gonadotropin-induced steroidogenesis in testicular interstitial cellsProceedings of the National Academy of Sciences, 1977
- In vitro action of bombesin and bombesin-like peptides on amylase secretion, calcium efflux, and adenylate cyclase activity in the rat pancreas: a comparison with other secretagogues.JCI Insight, 1976
- Preparation of Iodine-131 Labelled Human Growth Hormone of High Specific ActivityNature, 1962
- An unidentified depressor substance in certain tissue extractsThe Journal of Physiology, 1931