Interaction of thymic peptide thymosin α1 with vasoactive intestinal peptide (VIP) receptors
- 1 August 1986
- journal article
- research article
- Published by Portland Press Ltd. in Bioscience Reports
- Vol. 6 (8) , 727-733
- https://doi.org/10.1007/bf01116540
Abstract
Thymic peptide thymosin α1 (10−9 to 3 × 1010−7 M) is shown to inhibit the specific binding of [125I]VIP to rat blood mononuclear cells and liver plasma membranes. Thymosin α1 was 160 and 6250 times less potent that VIP at inhibiting [125I]VIP binding to blood mononuclear cells and liver plasma membranes, respectively. Thymosin α1 (10−10 to 1010−7 M) was weak in stimulating adenylate cyclase activity. Its efficacy is about 25 % and 27 % that of native VIP in blood mononuclear cells and liver plasma membranes, respectively. Thymosin α1 may behave as a partial VIP agonist in rat.This publication has 31 references indexed in Scilit:
- Interaction of vasoactive intestinal peptide (VIP) with human peripheral blood lymphocytes: Specific binding and cyclic AMP productionGeneral Pharmacology: The Vascular System, 1986
- Interaction of PHM, PHI and 24-glutamine PHI with human VIP receptors from colonic epithelium: Comparison with rat intestinal receptorsLife Sciences, 1985
- Structural requirements for VIP interaction with specific receptors in human and rat intestinal membranes: Effect of nine partial sequencesBiochemical and Biophysical Research Communications, 1984
- Interaction of GRF with VIP receptors and stimulation of adenylate cyclase in rat and human intestinal epithelial membranesFEBS Letters, 1983
- Characterization of rat hypothalamic growth hormone-releasing factorNature, 1983
- Growth Hormone-Releasing Factor from a Human Pancreatic Tumor That Caused AcromegalyScience, 1982
- Porcine peptide having N‐terminal histidine and C‐terminal isoleucine amide (PHI)FEBS Letters, 1980
- PURIFICATION AND PROPERTIES OF BOVINE THYMOSIN*Annals of the New York Academy of Sciences, 1975
- Structure of Porcine SecretinEuropean Journal of Biochemistry, 1970
- The Amino Acid Sequence of Glucagon. V. Location of Amide Groups, Acid Degradation Studies and Summary of Sequential EvidenceJournal of the American Chemical Society, 1957