Inhibition of TRPM8 function by the prostacyclin receptor requires coupling to Gq/11 proteins.

Prostacyclin TRPM8 inflammatory pain prostacyclin receptor

Journal

British journal of pharmacology
ISSN: 1476-5381
Titre abrégé: Br J Pharmacol
Pays: England
ID NLM: 7502536

Informations de publication

Date de publication:
03 Dec 2023
Historique:
revised: 16 11 2023
received: 18 04 2023
accepted: 21 11 2023
medline: 4 12 2023
pubmed: 4 12 2023
entrez: 4 12 2023
Statut: aheadofprint

Résumé

The Transient Receptor Potential Melastatin subtype 8 (TRPM8) receptor-channel is involved in innocuous cold sensing and has a potent anti-inflammatory action. Its activation by lower temperature or chemical agonists such as menthol and icilin induces analgesic effects, reversing hypersensitivity and reducing chronic pain. On the other hand, prostacyclin (PGI We employed transient expression of human TRPM8 and IP-R in HEK293T cells and performed intracellular calcium and cAMP measurements. Additionally, we cultured neurons from the dorsal root ganglia (DRGs) of mice and determined the increase in intracellular calcium triggered by the TRPM8 agonist, icilin, in the presence of the IP-R agonist, cicaprost, the IP-R antagonist, CAY10441 and the Gq/11 inhibitor YM254890. Our results demonstrate that the activation of IP-R by selective agonists, such as cicaprost, beraprost, and iloprost, inhibits TRPM8 independently of the Gs-cAMP pathway. The potent inhibition of TRPM8 by IP-R involves Gq/11 coupling of IP-R. These effects were also observed in neurons isolated from the DRGs of mice. Our results demonstrate that an unusual signaling pathway of IP-R, namely the coupling to Gq/11 proteins, inhibits TRPM8, which may contribute to a better understanding of the role of TRPM8 and IP-R in the regulation of pain and inflammation.

Sections du résumé

BACKGROUND AND PURPOSE OBJECTIVE
The Transient Receptor Potential Melastatin subtype 8 (TRPM8) receptor-channel is involved in innocuous cold sensing and has a potent anti-inflammatory action. Its activation by lower temperature or chemical agonists such as menthol and icilin induces analgesic effects, reversing hypersensitivity and reducing chronic pain. On the other hand, prostacyclin (PGI
EXPERIMENTAL APPROACH METHODS
We employed transient expression of human TRPM8 and IP-R in HEK293T cells and performed intracellular calcium and cAMP measurements. Additionally, we cultured neurons from the dorsal root ganglia (DRGs) of mice and determined the increase in intracellular calcium triggered by the TRPM8 agonist, icilin, in the presence of the IP-R agonist, cicaprost, the IP-R antagonist, CAY10441 and the Gq/11 inhibitor YM254890.
KEY RESULTS RESULTS
Our results demonstrate that the activation of IP-R by selective agonists, such as cicaprost, beraprost, and iloprost, inhibits TRPM8 independently of the Gs-cAMP pathway. The potent inhibition of TRPM8 by IP-R involves Gq/11 coupling of IP-R. These effects were also observed in neurons isolated from the DRGs of mice.
CONCLUSIONS AND IMPLICATIONS CONCLUSIONS
Our results demonstrate that an unusual signaling pathway of IP-R, namely the coupling to Gq/11 proteins, inhibits TRPM8, which may contribute to a better understanding of the role of TRPM8 and IP-R in the regulation of pain and inflammation.

Identifiants

pubmed: 38044577
doi: 10.1111/bph.16295
doi:

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Informations de copyright

This article is protected by copyright. All rights reserved.

Auteurs

Cosmin Trif (C)

Cell Signalling Research Group, Institute of Biochemistry of the Romanian Academy, Splaiul Independentei 296, 060031, Bucharest, Romania.

Alexandra-Maria Banica (AM)

Cell Signalling Research Group, Institute of Biochemistry of the Romanian Academy, Splaiul Independentei 296, 060031, Bucharest, Romania.

Alexandra Manolache (A)

Department of Anatomy, Physiology, and Biophysics, Faculty of Biology, University of Bucharest, Splaiul Independenţei 91-95, 050095, Bucharest, Romania.

Sorina Andreea Anghel (SA)

Cell Signalling Research Group, Institute of Biochemistry of the Romanian Academy, Splaiul Independentei 296, 060031, Bucharest, Romania.

Debora-Elena Huţanu (DE)

Department of Anatomy, Physiology, and Biophysics, Faculty of Biology, University of Bucharest, Splaiul Independenţei 91-95, 050095, Bucharest, Romania.

Teodora Stratulat (T)

Cell Signalling Research Group, Institute of Biochemistry of the Romanian Academy, Splaiul Independentei 296, 060031, Bucharest, Romania.
Department of Anatomy, Physiology, and Biophysics, Faculty of Biology, University of Bucharest, Splaiul Independenţei 91-95, 050095, Bucharest, Romania.

Rodica Badea (R)

Cell Signalling Research Group, Institute of Biochemistry of the Romanian Academy, Splaiul Independentei 296, 060031, Bucharest, Romania.

George Oprita (G)

Department of Anatomy, Physiology, and Biophysics, Faculty of Biology, University of Bucharest, Splaiul Independenţei 91-95, 050095, Bucharest, Romania.

Tudor Selescu (T)

Department of Anatomy, Physiology, and Biophysics, Faculty of Biology, University of Bucharest, Splaiul Independenţei 91-95, 050095, Bucharest, Romania.

Stefana M Petrescu (SM)

Cell Signalling Research Group, Institute of Biochemistry of the Romanian Academy, Splaiul Independentei 296, 060031, Bucharest, Romania.

Marco Sisignano (M)

Institut für Klinische Pharmakologie, Klinikum der Goethe-Universität, Theodor-Stern-Kai 7, 60596, Frankfurt am Main, Germany.

Stefan Offermanns (S)

Max Planck Institute for Heart and Lung Research, Ludwigstrasse. 43, 61231, Bad Nauheim, Germany.

Alexandru Babes (A)

Department of Anatomy, Physiology, and Biophysics, Faculty of Biology, University of Bucharest, Splaiul Independenţei 91-95, 050095, Bucharest, Romania.

Sorin Tunaru (S)

Cell Signalling Research Group, Institute of Biochemistry of the Romanian Academy, Splaiul Independentei 296, 060031, Bucharest, Romania.
Prothanor Biotech S.R.L, Ing. Ion Zablovschi 81, Sector 1, Bucharest, Romania.

Classifications MeSH