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AT1 Receptor Interactions

  • Chapter
Angiotensin Vol. I

Part of the book series: Handbook of Experimental Pharmacology ((HEP,volume 163 / 1))

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Abstract

Angiotensin II and antagonist-AT1 receptor interactions have traditionally been studied on isolated tissues in organ bath experiments. Cells that express endogenous or transfected AT1 receptors are now also increasingly used to this end. Angiotensin II and angiotensin III interact with the AT1 receptor in a similar fashion. Other naturally occurring fragments like angiotensin IV or angiotensin-(1–7) display only low affinity for the receptor and the latter even acts as an antagonist. Combination of such structure-activity relationship and receptor mutation studies led to a more complete picture of the molecular events that take place during receptor activation. At least two steps take place: a pre-activation step, in which constraining intramolecular interactions within the receptor are broken by Arg2 of angiotensin II, and a subsequent activation step in which the C-terminal side of the hormone plays an essential role. The outcome is a conformational change in the receptor that promotes its interaction with G proteins. Interaction with nonpeptide, biphenyltetrazole antagonists is also a multi-step process, and a “two-state, two-step” model is proposed in which the initial attraction to the receptor is fairly similar for all antagonists and in which a more stable, tight binding antagonist-receptor complex can be formed subsequently. This explains the often-mentioned distinction between “surmountable” and “insurmountable” antagonists in, e.g. vascular smooth muscle contraction experiments. This tight biding state is unrelated to receptor internalisation, but mutation studies reveal the implication of Lys199. These recent observations comply with the increasing awareness that AT1 receptors and other G protein-linked receptors may adopt a number of agonist- and antagonist-bound conformations and/or states, each with its own characteristic properties.

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Abbreviations

ACE:

Angiotensin-Converting enzyme

Ang:

Angiotensin

CHO-hAT1 cells:

Chinese hamster ovary cells expressing the human AT1 receptor

GPCR:

G protein-coupled receptor

L:

Ligand (antagonist)

N111G mutant:

AT1 receptor mutant in which Asn111 is substituted by Gly

R, R′, R*, RI :

Receptor in stable inactive-, preactivated-, fully active and tight antagonist-binding states, respectively

TM:

Transmembrane-spanning helix

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Authors and Affiliations

  1. Department of Molecular and Biochemical Pharmacology, Institute for Molecular Biology and Biotechnology, Free University of Brussels (VUB), Gebouw E.5.10, Pleinlaan 2, 1050, Brussels, Belgium

    G. Vauquelin & P. Vanderheyden

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  1. G. Vauquelin
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  2. P. Vanderheyden
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  1. Center for Cardiovascular Research (CCR) Institut für Pharmakologie und Toxikologie Charité Campus Mitte, Charité — Universitätsmedizin Berlin, Hessische Strasse 3-4, 10115, Berlin, Germany

    Thomas Unger

  2. Drug Innovation & Approval, Aventis Pharma Deutschland GmbH, Bldg. H 831, Room C 320, 65926, Frankfurt/Main, Germany

    Bernward A. Schölkens

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Vauquelin, G., Vanderheyden, P. (2004). AT1 Receptor Interactions. In: Unger, T., Schölkens, B.A. (eds) Angiotensin Vol. I. Handbook of Experimental Pharmacology, vol 163 / 1. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-18495-6_13

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