l-Arginine prevents inflammatory and pro-calcific differentiation of interstitial aortic valve cells.


Journal

Atherosclerosis
ISSN: 1879-1484
Titre abrégé: Atherosclerosis
Pays: Ireland
ID NLM: 0242543

Informations de publication

Date de publication:
04 2020
Historique:
received: 01 08 2019
revised: 17 01 2020
accepted: 28 02 2020
pubmed: 15 3 2020
medline: 30 1 2021
entrez: 15 3 2020
Statut: ppublish

Résumé

Reduced bioavailability of nitric oxide (NO) has been implicated in the pathogenesis of calcific aortic stenosis. Herein, we investigated the effects of l-Arginine, the main precursor of NO, on the osteogenic differentiation of aortic interstitial valve cells (VICs). We isolated a clonal population of bovine VICs that expresses osteogenic markers and induces calcification of collagen matrix after stimulation with endotoxin (LPS 500 ng/mL). VICs were treated in vitro with different combinations of LPS ± l-Arginine (50 or 100 mM) and cell extracts were collected to perform proteomic (iTRAQ) and gene expression (RT-PCR) analysis. l-Arginine prevents the over-expression of alkaline phosphatase (ALP, p < 0.001) and reduces matrix calcification (p < 0.05) in VICs treated with LPS. l-Arginine also reduces the over-expression of inflammatory molecules induced by LPS (TNF-alpha, IL-6 and IL-1beta, p < 0.001). The proteomic analysis allowed to identify 49 proteins with an altered expression profile after stimulation with LPS and significantly modified by l-Arginine. These include proteins involved in the redox homeostasis of the cells (i.e. Xanthine Oxidase, Catalase, Aldehyde Oxidase), remodeling of the extracellular matrix (i.e. ADAMTSL4, Basigin, COL3A1) and cellular signaling (i.e. Fibrillin-1, Legumain, S100A13). The RT-PCR analysis confirmed the modifications of Fibrillin-1, ADAMTSL4, Basigin and Xanthine Oxidase, whose expression levels increase after stimulation with LPS and are reduced by l-Arginine (p < 0.05). l-Arginine prevents osteogenic differentiation of VICs and reduces matrix calcification. This effect is achieved through the modulation of proteins involved in the cellular redox system, remodeling of extracellular matrix and inflammatory activation of VICs.

Sections du résumé

BACKGROUND AND AIMS
Reduced bioavailability of nitric oxide (NO) has been implicated in the pathogenesis of calcific aortic stenosis. Herein, we investigated the effects of l-Arginine, the main precursor of NO, on the osteogenic differentiation of aortic interstitial valve cells (VICs).
METHODS
We isolated a clonal population of bovine VICs that expresses osteogenic markers and induces calcification of collagen matrix after stimulation with endotoxin (LPS 500 ng/mL). VICs were treated in vitro with different combinations of LPS ± l-Arginine (50 or 100 mM) and cell extracts were collected to perform proteomic (iTRAQ) and gene expression (RT-PCR) analysis.
RESULTS
l-Arginine prevents the over-expression of alkaline phosphatase (ALP, p < 0.001) and reduces matrix calcification (p < 0.05) in VICs treated with LPS. l-Arginine also reduces the over-expression of inflammatory molecules induced by LPS (TNF-alpha, IL-6 and IL-1beta, p < 0.001). The proteomic analysis allowed to identify 49 proteins with an altered expression profile after stimulation with LPS and significantly modified by l-Arginine. These include proteins involved in the redox homeostasis of the cells (i.e. Xanthine Oxidase, Catalase, Aldehyde Oxidase), remodeling of the extracellular matrix (i.e. ADAMTSL4, Basigin, COL3A1) and cellular signaling (i.e. Fibrillin-1, Legumain, S100A13). The RT-PCR analysis confirmed the modifications of Fibrillin-1, ADAMTSL4, Basigin and Xanthine Oxidase, whose expression levels increase after stimulation with LPS and are reduced by l-Arginine (p < 0.05).
CONCLUSIONS
l-Arginine prevents osteogenic differentiation of VICs and reduces matrix calcification. This effect is achieved through the modulation of proteins involved in the cellular redox system, remodeling of extracellular matrix and inflammatory activation of VICs.

Identifiants

pubmed: 32169720
pii: S0021-9150(20)30115-5
doi: 10.1016/j.atherosclerosis.2020.02.024
pii:
doi:

Substances chimiques

Arginine 94ZLA3W45F
Alkaline Phosphatase EC 3.1.3.1

Types de publication

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

Langues

eng

Sous-ensembles de citation

IM

Pagination

27-35

Informations de copyright

Copyright © 2020 Elsevier B.V. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of competing interest The authors declared they do not have anything to disclose regarding conflict of interest with respect to this manuscript.

Auteurs

Marcello Rattazzi (M)

Department of Medicine, University of Padova, Italy; Medicina Interna I^, Cà Foncello Hospital, Treviso, Italy. Electronic address: marcello.rattazzi@unipd.it.

Maristella Donato (M)

Department of Pharmaceutical and Pharmacological Sciences, University of Padova, Italy.

Elisa Bertacco (E)

Department of Medicine, University of Padova, Italy.

Renato Millioni (R)

Department of Medicine, University of Padova, Italy; Proteomics Center, University of Padova and Azienda Ospedaliera di Padova, Italy.

Cinzia Franchin (C)

Department of Biomedical Sciences, University of Padova, Italy; Proteomics Center, University of Padova and Azienda Ospedaliera di Padova, Italy.

Cinzia Mortarino (C)

Department of Statistical Sciences, University of Padova, Italy.

Elisabetta Faggin (E)

Department of Medicine, University of Padova, Italy.

Chiara Nardin (C)

Department of Medicine, University of Padova, Italy; Medicina Interna I^, Cà Foncello Hospital, Treviso, Italy.

Riccardo Scarpa (R)

Department of Medicine, University of Padova, Italy; Medicina Interna I^, Cà Foncello Hospital, Treviso, Italy.

Francesco Cinetto (F)

Department of Medicine, University of Padova, Italy; Medicina Interna I^, Cà Foncello Hospital, Treviso, Italy.

Carlo Agostini (C)

Department of Medicine, University of Padova, Italy; Medicina Interna I^, Cà Foncello Hospital, Treviso, Italy.

Nicola Ferri (N)

Department of Pharmaceutical and Pharmacological Sciences, University of Padova, Italy.

Paolo Pauletto (P)

ORAS Rehabilitation Hospital, Motta di Livenza, Treviso, Italy.

Giorgio Arrigoni (G)

Department of Biomedical Sciences, University of Padova, Italy; Proteomics Center, University of Padova and Azienda Ospedaliera di Padova, Italy.

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