Acid sphingomyelinase promotes SGK1-dependent vascular calcification.


Journal

Clinical science (London, England : 1979)
ISSN: 1470-8736
Titre abrégé: Clin Sci (Lond)
Pays: England
ID NLM: 7905731

Informations de publication

Date de publication:
12 02 2021
Historique:
received: 07 09 2020
revised: 07 01 2021
accepted: 21 01 2021
pubmed: 23 1 2021
medline: 8 9 2021
entrez: 22 1 2021
Statut: ppublish

Résumé

In chronic kidney disease (CKD), hyperphosphatemia is a key factor promoting medial vascular calcification, a common complication associated with cardiovascular events and high mortality. Vascular calcification involves osteo-/chondrogenic transdifferentiation of vascular smooth muscle cells (VSMCs), but the complex signaling events inducing pro-calcific pathways are incompletely understood. The present study investigated the role of acid sphingomyelinase (ASM)/ceramide as regulator of VSMC calcification. In vitro, both, bacterial sphingomyelinase and phosphate increased ceramide levels in VSMCs. Bacterial sphingomyelinase as well as ceramide supplementation stimulated osteo-/chondrogenic transdifferentiation during control and high phosphate conditions and augmented phosphate-induced calcification of VSMCs. Silencing of serum- and glucocorticoid-inducible kinase 1 (SGK1) blunted the pro-calcific effects of bacterial sphingomyelinase or ceramide. Asm deficiency blunted vascular calcification in a cholecalciferol-overload mouse model and ex vivo isolated-perfused arteries. In addition, Asm deficiency suppressed phosphate-induced osteo-/chondrogenic signaling and calcification of cultured VSMCs. Treatment with the functional ASM inhibitors amitriptyline or fendiline strongly blunted pro-calcific signaling pathways in vitro and in vivo. In conclusion, ASM/ceramide is a critical upstream regulator of vascular calcification, at least partly, through SGK1-dependent signaling. Thus, ASM inhibition by repurposing functional ASM inhibitors to reduce the progression of vascular calcification during CKD warrants further study.

Identifiants

pubmed: 33479769
pii: 227637
doi: 10.1042/CS20201122
pmc: PMC7859357
doi:

Substances chimiques

Ceramides 0
Immediate-Early Proteins 0
Phosphates 0
Amitriptyline 1806D8D52K
Protein Serine-Threonine Kinases EC 2.7.11.1
serum-glucocorticoid regulated kinase EC 2.7.11.1
Sphingomyelin Phosphodiesterase EC 3.1.4.12
Fendiline S253D559A8

Types de publication

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

Langues

eng

Sous-ensembles de citation

IM

Pagination

515-534

Informations de copyright

© 2021 The Author(s).

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Auteurs

Trang Thi Doan Luong (TTD)

Institute for Physiology and Pathophysiology, Johannes Kepler University Linz, Linz, Austria.

Rashad Tuffaha (R)

Department of Physiology I, Eberhard-Karls University, Tübingen, Germany.

Mirjam Schuchardt (M)

Department of Nephrology and Medical Intensive Care, Charité - Universitätsmedizin Berlin, corporate member of Freie Universität Berlin, Humboldt-Universität zu Berlin, and Berlin Institute of Health, Berlin, Germany.

Barbara Moser (B)

Institute for Physiology and Pathophysiology, Johannes Kepler University Linz, Linz, Austria.

Nadeshda Schelski (N)

Department of Internal Medicine and Cardiology, Campus Virchow-Klinikum, Charité - Universitätsmedizin Berlin, Berlin, Germany.

Beate Boehme (B)

Department of Internal Medicine and Cardiology, Campus Virchow-Klinikum, Charité - Universitätsmedizin Berlin, Berlin, Germany.

Can Gollmann-Tepeköylü (C)

University Clinic of Cardiac Surgery, Medical University of Innsbruck, Innsbruck, Austria.

Clara Schramm (C)

Division of Pathophysiology, Institute for Physiology and Pathophysiology, Johannes Kepler University Linz, Linz, Austria.

Johannes Holfeld (J)

University Clinic of Cardiac Surgery, Medical University of Innsbruck, Innsbruck, Austria.

Burkert Pieske (B)

Department of Internal Medicine and Cardiology, Campus Virchow-Klinikum, Charité - Universitätsmedizin Berlin, Berlin, Germany.
Berlin Institute of Health (BIH), Berlin, Germany.
Department of Internal Medicine and Cardiology, German Heart Center Berlin (DHZB), Berlin, Germany.
DZHK (German Centre for Cardiovascular Research), Partner Site Berlin, Berlin, Germany.

Erich Gulbins (E)

Institute of Molecular Biology, University Hospital Essen, University of Duisburg-Essen, Essen, Germany.

Markus Tölle (M)

Department of Nephrology and Medical Intensive Care, Charité - Universitätsmedizin Berlin, corporate member of Freie Universität Berlin, Humboldt-Universität zu Berlin, and Berlin Institute of Health, Berlin, Germany.

Markus van der Giet (M)

Department of Nephrology and Medical Intensive Care, Charité - Universitätsmedizin Berlin, corporate member of Freie Universität Berlin, Humboldt-Universität zu Berlin, and Berlin Institute of Health, Berlin, Germany.

Florian Lang (F)

Department of Physiology I, Eberhard-Karls University, Tübingen, Germany.

Kai-Uwe Eckardt (KU)

Department of Nephrology and Medical Intensive Care, Charité - Universitätsmedizin Berlin, corporate member of Freie Universität Berlin, Humboldt-Universität zu Berlin, and Berlin Institute of Health, Berlin, Germany.

Jakob Voelkl (J)

Institute for Physiology and Pathophysiology, Johannes Kepler University Linz, Linz, Austria.
Department of Nephrology and Medical Intensive Care, Charité - Universitätsmedizin Berlin, corporate member of Freie Universität Berlin, Humboldt-Universität zu Berlin, and Berlin Institute of Health, Berlin, Germany.
DZHK (German Centre for Cardiovascular Research), Partner Site Berlin, Berlin, Germany.

Ioana Alesutan (I)

Institute for Physiology and Pathophysiology, Johannes Kepler University Linz, Linz, Austria.

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