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Title: The angiotensin II receptor of rabbit liver: characterization in isolated hepatocytes and effect of GTP
Authors: Vandekerckhove, A ×
Keppens, Stefaan
De Wulf, H #
Issue Date: Oct-1989
Publisher: BioScientifica Ltd.
Series Title: European journal of endocrinology vol:123 issue:1 pages:131-6
Abstract: A homologous population of specific angiotensin II receptors is present on the cell surface of isolated rabbit hepatocytes. The binding characteristics of [3H]angiotensin II to the cells were: association rate constant (K+1) 0.08 l/nmol per min and dissociation rate constant (K-1) 1.9/min, yielding a dissociation constant (Kd) of 24 nmol/l. A very similar Kd (32 nmol/l) has been derived from saturation binding data which indicate a maximal binding capacity of about 200,000 sites/cell. Analysis of the association binding data to purified liver plasma membranes indicated a Kd of 6 nmol/l in the absence and 30 nmol/l in the presence of GTP. Dissociation was clearly dependent upon the presence of the nucleotide, which shifted the K-1 from 0.12/min to 0.42/min. The studied binding sites are very likely to be involved in the glycogenolytic action of angiotensin II, since a highly significant correlation was established between the biological activity (activation of glycogen phosphorylase) and the binding affinity of a series of agonistic analogues. The reported characteristics of the rabbit hepatic angiotensin II receptors show much similarity with those of rat liver.
ISSN: 0804-4643
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Biochemistry Section (Medicine) (-)
× corresponding author
# (joint) last author

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