Binding sites for vasoactive intestinal polypeptide (VIP) on washed rabbit platelets
The authors have previously reported that VIP elevates intracellular cyclic AMP and inhibits activation of washed rabbit platelets induced by platelet activating factor. They have now examined VIP binding sites on intact rabbit platelets, using (/sup 125/I) VIP. Binding was: (1) saturable; (2) dependent on the temperature and duration of incubation, with maximal binding occurring after 15 min. at 4/sup 0/C; (3) directly proportional to the number of platelets; and (4) reversible. The ED/sub 50/ for the displacement of the binding by unlabeled VIP was 300 nM. The structurally unrelated peptides eledoisin, metenkephalin, neurotensin and insulin, at concentrations up to 5 ..mu..M, did not displace (/sup 125/I)VIP. The homologous peptides, secretin and PHI, however, displaced bound VIP with almost equal potency. They conclude that VIP-binding sites are present on rabbit platelets, that these receptors have relatively low affinity for VIP, and bind secretin and PHI with approximately equal affinity.
- Research Organization:
- Univ. of Oklahoma Health Sciences Center, Oklahoma City
- OSTI ID:
- 6898941
- Report Number(s):
- CONF-8604222-
- Journal Information:
- Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States), Journal Name: Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States) Vol. 45:4; ISSN FEPRA
- Country of Publication:
- United States
- Language:
- English
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59 BASIC BIOLOGICAL SCIENCES
AFFINITY
ANIMALS
BETA DECAY RADIOISOTOPES
BIOCHEMICAL REACTION KINETICS
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BLOOD PLATELETS
BODY FLUIDS
DAYS LIVING RADIOISOTOPES
ELECTRON CAPTURE RADIOISOTOPES
HORMONES
INTERMEDIATE MASS NUCLEI
IODINE 125
IODINE ISOTOPES
ISOTOPE APPLICATIONS
ISOTOPES
KINETICS
MAMMALS
MATERIALS
MEMBRANE PROTEINS
NUCLEI
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
PEPTIDE HORMONES
PROTEINS
RABBITS
RADIOISOTOPES
REACTION KINETICS
RECEPTORS
RESPONSE MODIFYING FACTORS
TEMPERATURE DEPENDENCE
TRACER TECHNIQUES
VERTEBRATES