JPET xPharm- The Comprehensive Pharmacology Reference

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Pendleton, R. G.
Right arrow Articles by Horner, E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Pendleton, R. G.
Right arrow Articles by Horner, E.
Right arrowPubmed/NCBI databases
*Compound via MeSH
*Substance via MeSH

Studies defining minimal receptor domains for angiotensin II

RG Pendleton, G Gessner and E Horner

Rorer Central Research, King of Prussia, Pennsylvania.

The purpose of this study was to define in a systematic experimental manner the minimal amino acid domain(s) present in the angiotensin II molecule that are required for binding to, as well as activation of, its receptor at physiological concentrations. Although removal of the C- terminal phenylalanine residue markedly reduced affinity for the rabbit adrenal cortical receptor, sequential additions of amino acids beginning with phenylalanine did not result in a molecule with significant receptor affinity until the hexapeptide stage was reached. Similar receptor affinities were obtained with the other two possible 6 amino acid fragments in the molecule. None of the possible pentapeptide fragments were active, as was also the case with representative 4, 3 and 2 amino acid sequences. Of the three hexapeptides, only the one containing phenylalanine as the C-terminal amino acid displayed agonist activity on the rabbit aortic strip. The other two behaved as competitive antagonists. These results indicate that 6 amino acids constitute the minimal receptor binding domain present in the angiotensin II molecule and that phenylalanine is crucial at the C- terminus for activating the receptor.

Volume 250, Issue 1, pp. 31-36, 07/01/1989
Copyright © 1989 by American Society for Pharmacology and Experimental Therapeutics




This article has been cited by other articles:


Home page
 Journal of Renin-Angiotensin-Aldosterone SystemHome page
G. Vauquelin, Y. Michotte, I. Smolders, S. Sarre, G. Ebinger, A. Dupont, and P. Vanderheyden
Cellular targets for angiotensin II fragments: pharmacological and molecular evidence
Journal of Renin-Angiotensin-Aldosterone System, December 1, 2002; 3(4): 195 - 204.
[Abstract] [PDF]

Home page
 Journal of Renin-Angiotensin-Aldosterone SystemHome page
T. Mustafa, Joo Hyung Lee, Siew Yeen Chai, A. L Albiston, S. G McDowall, and F. A. Mendelsohn
Bioactive angiotensin peptides: focus on angiotensin IV
Journal of Renin-Angiotensin-Aldosterone System, December 1, 2001; 2(4): 205 - 210.
[PDF]


Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
All ASPET Journals Molecular Pharmacology Pharmacological Reviews
Molecular Interventions Drug Metabolism and Disposition

Copyright © 1989 by the American Society for Pharmacology and Experimental Therapeutics.