Statin activation of skeletal ryanodine receptors (RyR1) is a class effect but separable from HMG-CoA reductase inhibition.


Journal

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

Informations de publication

Date de publication:
11 2022
Historique:
revised: 20 04 2022
received: 13 07 2021
accepted: 28 04 2022
pubmed: 16 6 2022
medline: 6 10 2022
entrez: 15 6 2022
Statut: ppublish

Résumé

Statins, inhibitors of HMG-CoA reductase, are mainstay treatment for hypercholesterolaemia. However, muscle pain and weakness prevent many patients from benefiting from their cardioprotective effects. We previously demonstrated that simvastatin activates skeletal ryanodine receptors (RyR1), an effect that could be important in initiating myopathy. Using a range of structurally diverse statin analogues, we examined structural features associated with RyR1 activation, aiming to identify statins lacking this property. Compounds were screened for RyR1 activity utilising [ All UK-prescribed statins activated RyR1 at nanomolar concentrations. Cerivastatin, withdrawn from the market due to life-threatening muscle-related side effects, was more effective than currently-prescribed statins and possessed the unique ability to open RyR1 channels independently of cytosolic Ca That cerivastatin activates RyR1 most strongly supports the hypothesis that RyR1 activation is implicated in statin-induced myopathy. Demonstrating that statin regulation of RyR1 and HMG-CoA reductase are separable effects will allow the role of RyR1 in statin-induced myopathy to be further elucidated by the tool compounds we have identified, allowing development of effective cardioprotective statins with improved patient tolerance.

Sections du résumé

BACKGROUND AND PURPOSE
Statins, inhibitors of HMG-CoA reductase, are mainstay treatment for hypercholesterolaemia. However, muscle pain and weakness prevent many patients from benefiting from their cardioprotective effects. We previously demonstrated that simvastatin activates skeletal ryanodine receptors (RyR1), an effect that could be important in initiating myopathy. Using a range of structurally diverse statin analogues, we examined structural features associated with RyR1 activation, aiming to identify statins lacking this property.
EXPERIMENTAL APPROACH
Compounds were screened for RyR1 activity utilising [
KEY RESULTS
All UK-prescribed statins activated RyR1 at nanomolar concentrations. Cerivastatin, withdrawn from the market due to life-threatening muscle-related side effects, was more effective than currently-prescribed statins and possessed the unique ability to open RyR1 channels independently of cytosolic Ca
CONCLUSION AND IMPLICATIONS
That cerivastatin activates RyR1 most strongly supports the hypothesis that RyR1 activation is implicated in statin-induced myopathy. Demonstrating that statin regulation of RyR1 and HMG-CoA reductase are separable effects will allow the role of RyR1 in statin-induced myopathy to be further elucidated by the tool compounds we have identified, allowing development of effective cardioprotective statins with improved patient tolerance.

Identifiants

pubmed: 35703154
doi: 10.1111/bph.15893
pmc: PMC9804224
doi:

Substances chimiques

Acyl Coenzyme A 0
Hydroxymethylglutaryl-CoA Reductase Inhibitors 0
Ryanodine Receptor Calcium Release Channel 0
3-hydroxy-3-methylglutaryl-coenzyme A 1553-55-5
Ryanodine 15662-33-6
Simvastatin AGG2FN16EV

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

4941-4957

Subventions

Organisme : British Heart Foundation
ID : PG/19/38/34403
Pays : United Kingdom

Informations de copyright

© 2022 The Authors. British Journal of Pharmacology published by John Wiley & Sons Ltd on behalf of British Pharmacological Society.

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Auteurs

Chris Lindsay (C)

Department of Pharmacology, University of Oxford, Oxford, UK.

Maria Musgaard (M)

Structural Bioinformatics and Computational Biochemistry, Department of Biochemistry, University of Oxford, Oxford, UK.
OMass Therapeutics, Oxford, UK.

Angela J Russell (AJ)

Department of Pharmacology, University of Oxford, Oxford, UK.
Department of Chemistry, Chemistry Research Laboratory, University of Oxford, Oxford, UK.

Rebecca Sitsapesan (R)

Department of Pharmacology, University of Oxford, Oxford, UK.

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Classifications MeSH