Abstract:
:Peptide Histidine Isoleucine (PHI) is generally considered a low affinity agonist for Vasoactive Intestinal Peptide (VIP) receptors. In this study, we investigated the presence and characteristics of [125I]PHI binding sites on rat liver membranes. Detergents at nonsolubilizing concentrations (1 mM CHAPS or 0.01% Tween-20) were included in the assay buffer to reduce adsorptive loss of PHI to acceptable levels and permit measurement of PHI-binding to receptors. Under these conditions, binding of PHI to liver membranes was time- and temperature-dependent, reversible and saturable. Unlabeled PHI was 9.7-fold more potent than VIP, and 357-fold more potent than secretin in displacing [125I]-PHI binding. Scatchard analysis suggested the presence of two classes of PHI receptors, with Kd 27 pM and 512 pM. The data from [125I]-PHI and [125I]-VIP binding studies suggested that one class of receptors was PHI-preferring, and the other, equally reactive with PHI and VIP. The concentration of immunoreactive PHI, measured by radioimmunoassay, in blood from the hepatic portal vein of anesthetized rats was 2-fold higher than that from the hepatic vein, suggesting uptake of circulating PHI by the liver.
journal_name
Life Scijournal_title
Life sciencesauthors
Paul S,Chou J,Kubota Edoi
10.1016/0024-3205(87)90661-8subject
Has Abstractpub_date
1987-11-23 00:00:00pages
2373-80issue
21eissn
0024-3205issn
1879-0631pii
0024-3205(87)90661-8journal_volume
41pub_type
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