Specific Receptors for des-Asp1-angiotensin II (``Angiotensin III'') in Rat Adrenals

The specific binding of angiotensin II and des-Asp1-angiotensin II (``angiotensin III'') to rat adrenals was studied with the use of the tritiated peptides. The binding sites having maximal affinity for angiotensin II were characterized by an equilibrium dissociation constant of 3.3 to 5.2...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1977-09, Vol.74 (9), p.4029-4032
Main Authors: Devynck, Marie-Aude, Pernollet, Marie-Gabrielle, Matthews, P. Geoffrey, Khosla, Mahesh C., Bumpus, F. Merlin, Meyer, Philippe
Format: Article
Language:English
Subjects:
Adrenal Glands - metabolism
Angiotensin II - analogs & derivatives
Angiotensin II - metabolism
Angiotensin III - metabolism
Animals
Binding sites
Kinetics
Ligands
Medical sciences
Particulate matter
Pharmacology
Radioactive decay
Rats
Receptors
Receptors, Angiotensin - metabolism
Receptors, Cell Surface - metabolism
Renin angiotensin system
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Summary:The specific binding of angiotensin II and des-Asp1-angiotensin II (``angiotensin III'') to rat adrenals was studied with the use of the tritiated peptides. The binding sites having maximal affinity for angiotensin II were characterized by an equilibrium dissociation constant of 3.3 to 5.2 × 10-9M. Angiotensin III was able to interact with these sites, and also with a class of sites with very high affinity, characterized by an equilibrium dissociation constant of 1 to 2 × 10-10M. These sites exhibited a greater affinity for the heptapeptide angiotensin III than for the octapeptide angiotensin II. These findings, together with the known potent aldosterone stimulating effect of angiotensin III and its presence in rat plasma, suggest that this heptapeptide could be the physiologically important steroidogenic angiotensin in this species.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.74.9.4029