Characterization of the First Animal Toxin Acting as an Antagonist on AT1 Receptor.
AT1
Conus miliaris
GPCR
angiotensin
conotoxin
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
24 Jan 2023
24 Jan 2023
Historique:
received:
15
12
2022
revised:
19
01
2023
accepted:
20
01
2023
entrez:
11
2
2023
pubmed:
12
2
2023
medline:
15
2
2023
Statut:
epublish
Résumé
The renin-angiotensin system (RAS) is one of the main regulatory systems of cardiovascular homeostasis. It is mainly composed of angiotensin-converting enzyme (ACE) and angiotensin II receptors AT1 and AT2. ACE and AT1 are targets of choice for the treatment of hypertension, whereas the AT2 receptor is still not exploited due to the lack of knowledge of its physiological properties. Peptide toxins from venoms display multiple biological functions associated with varied chemical and structural properties. If Brazilian viper toxins have been described to inhibit ACE, no animal toxin is known to act on AT1/AT2 receptors. We screened a library of toxins on angiotensin II receptors with a radioligand competition binding assay. Functional characterization of the selected toxin was conducted by measuring second messenger production, G-protein activation and β-arrestin 2 recruitment using bioluminescence resonance energy transfer (BRET) based biosensors. We identified one original toxin, A-CTX-cMila, which is a 7-residues cyclic peptide from
Identifiants
pubmed: 36768653
pii: ijms24032330
doi: 10.3390/ijms24032330
pmc: PMC9916866
pii:
doi:
Substances chimiques
Angiotensin II
11128-99-7
Angiotensin Receptor Antagonists
0
beta-Arrestin 2
0
Peptides
0
Receptor, Angiotensin, Type 1
0
Receptor, Angiotensin, Type 2
0
Receptors, Angiotensin
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
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