Histone Acetyltransferase-Dependent Pathways Mediate Upregulation of NADPH Oxidase 5 in Human Macrophages under Inflammatory Conditions: A Potential Mechanism of Reactive Oxygen Species Overproduction in Atherosclerosis.


Journal

Oxidative medicine and cellular longevity
ISSN: 1942-0994
Titre abrégé: Oxid Med Cell Longev
Pays: United States
ID NLM: 101479826

Informations de publication

Date de publication:
2019
Historique:
received: 27 03 2019
revised: 14 06 2019
accepted: 04 07 2019
entrez: 1 10 2019
pubmed: 1 10 2019
medline: 21 3 2020
Statut: epublish

Résumé

Histone acetylation plays a major role in epigenetic regulation of gene expression. Monocyte-derived macrophages express functional NADPH oxidase 5 (Nox5) that contributes to oxidative stress in atherogenesis. The mechanisms of Nox5 regulation are not entirely elucidated. The aim of this study was to investigate the expression pattern of key histone acetyltransferase subtypes (p300, HAT1) in human atherosclerosis and to determine their role in mediating the upregulation of Nox5 in macrophages under inflammatory conditions. Human nonatherosclerotic and atherosclerotic tissue samples were collected in order to determine the expression of p300 and HAT1 isoforms, H3K27ac, and Nox5. In vitro determinations were done on human macrophages exposed to lipopolysaccharide in the absence or presence of histone acetyltransferase inhibitors. Western blot, immunohistochemistry, immunofluorescence, real-time PCR, transfection, and chromatin immunoprecipitation assay were employed. The protein levels of p300 and HAT1 isoforms, H3K27ac, and Nox5 were found significantly elevated in human atherosclerotic specimens. Immunohistochemistry/immunofluorescence staining revealed that p300, HAT1, H3K27ac, H3K9ac, and Nox5 proteins were colocalized in the area of CD45

Identifiants

pubmed: 31565149
doi: 10.1155/2019/3201062
pmc: PMC6745143
doi:

Substances chimiques

Histones 0
Lipopolysaccharides 0
Reactive Oxygen Species 0
NADPH Oxidase 5 EC 1.6.3.-
NOX5 protein, human EC 1.6.3.-
E1A-Associated p300 Protein EC 2.3.1.48
EP300 protein, human EC 2.3.1.48
Histone Acetyltransferases EC 2.3.1.48
histone acetyltransferase type B complex EC 2.3.1.48

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

3201062

Informations de copyright

Copyright © 2019 Mihaela-Loredana Vlad et al.

Déclaration de conflit d'intérêts

The authors declare no conflict of interest.

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Auteurs

Mihaela-Loredana Vlad (ML)

Institute of Cellular Biology and Pathology "Nicolae Simionescu" of the Romanian Academy, Bucharest, Romania.

Simona-Adriana Manea (SA)

Institute of Cellular Biology and Pathology "Nicolae Simionescu" of the Romanian Academy, Bucharest, Romania.

Alexandra-Gela Lazar (AG)

Institute of Cellular Biology and Pathology "Nicolae Simionescu" of the Romanian Academy, Bucharest, Romania.

Monica Raicu (M)

Institute of Cellular Biology and Pathology "Nicolae Simionescu" of the Romanian Academy, Bucharest, Romania.

Horia Muresian (H)

University Hospital Bucharest, Cardiovascular Surgery Department, Bucharest, Romania.

Maya Simionescu (M)

Institute of Cellular Biology and Pathology "Nicolae Simionescu" of the Romanian Academy, Bucharest, Romania.

Adrian Manea (A)

Institute of Cellular Biology and Pathology "Nicolae Simionescu" of the Romanian Academy, Bucharest, Romania.

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Classifications MeSH