Research ExplorerPublicationsFoxO1 regulates asymmetric dimethylarginine via downregulati...

FoxO1 regulates asymmetric dimethylarginine via downregulation of dimethylaminohydrolase 1 in human endothelial cells and subjects with atherosclerosis

Standard

FoxO1 regulates asymmetric dimethylarginine via downregulation of dimethylaminohydrolase 1 in human endothelial cells and subjects with atherosclerosis. / Menghini, Rossella; Casagrande, Viviana; Cardellini, Marina; Ballanti, Marta; Davato, Francesca; Cardolini, Iris; Stoehr, Robert; Fabrizi, Marta; Morelli, Monica; Anemona, Lucia; Bernges, Isabel; Schwedhelm, Edzard; Ippoliti, Arnaldo; Mauriello, Alessandro; Böger, Rainer H; Federici, Massimo.

In: ATHEROSCLEROSIS, Vol. 242, No. 1, 09.2015, p. 230-5.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Menghini, R, Casagrande, V, Cardellini, M, Ballanti, M, Davato, F, Cardolini, I, Stoehr, R, Fabrizi, M, Morelli, M, Anemona, L, Bernges, I, Schwedhelm, E, Ippoliti, A, Mauriello, A, Böger, RH & Federici, M 2015, 'FoxO1 regulates asymmetric dimethylarginine via downregulation of dimethylaminohydrolase 1 in human endothelial cells and subjects with atherosclerosis', ATHEROSCLEROSIS, vol. 242, no. 1, pp. 230-5. https://doi.org/10.1016/j.atherosclerosis.2015.07.026

APA

Menghini, R., Casagrande, V., Cardellini, M., Ballanti, M., Davato, F., Cardolini, I., Stoehr, R., Fabrizi, M., Morelli, M., Anemona, L., Bernges, I., Schwedhelm, E., Ippoliti, A., Mauriello, A., Böger, R. H., & Federici, M. (2015). FoxO1 regulates asymmetric dimethylarginine via downregulation of dimethylaminohydrolase 1 in human endothelial cells and subjects with atherosclerosis. ATHEROSCLEROSIS, 242(1), 230-5. https://doi.org/10.1016/j.atherosclerosis.2015.07.026

Vancouver

Menghini R, Casagrande V, Cardellini M, Ballanti M, Davato F, Cardolini I et al. FoxO1 regulates asymmetric dimethylarginine via downregulation of dimethylaminohydrolase 1 in human endothelial cells and subjects with atherosclerosis. ATHEROSCLEROSIS. 2015 Sep;242(1):230-5. https://doi.org/10.1016/j.atherosclerosis.2015.07.026

Bibtex

@article{475071fcb0374541b0a5a0003735faa9,
title = "FoxO1 regulates asymmetric dimethylarginine via downregulation of dimethylaminohydrolase 1 in human endothelial cells and subjects with atherosclerosis",
abstract = "BACKGROUND AND AIMS: The O subfamily of forkhead (FoxO) 1 is a pivotal element in the regulation of endothelial activation. Compartmentalization and activity of FoxO1 is regulated by post translational modifications, but the implication in endothelial dysfunction and atherosclerosis remain controversial. Our aim was to identify FoxO1 related metabolic signatures in endothelial cells.METHODS AND RESULTS: Using metabolomics in human umbilical endothelial cells (HUVECs) overexpressing the wild type FoxO1 (FoxO1-WT), the acetylation defective mutant (FoxO1-KR), the unphosphorylated nuclear localized mutant (FoxO1-ADA) and the Green Fluorescent Protein (GFP) control vector, we identify metabolic pathways differentially affected by the different FoxO1 localization and activity. Among metabolites, asymmetric dimethylarginine (ADMA) was increased in FoxO1-ADA compared with FoxO1-WT and FoxO1-KR infected cells (p < 0.01). ADMA was further investigated to identify the molecular mechanisms to explain its link to FoxO1. We found that unrestrained FoxO1 activity leads to increase of ADMA via downregulation of its degrading enzyme, dimethylaminohydrolase (DDAH) 1. In human subjects (n = 89) the FoxO1/DDAH1/ADMA pathway marks unstable atherosclerosis.CONCLUSIONS: Our results point to ADMA as a biomarker to track deregulated FoxO1 activity in vivo.",
author = "Rossella Menghini and Viviana Casagrande and Marina Cardellini and Marta Ballanti and Francesca Davato and Iris Cardolini and Robert Stoehr and Marta Fabrizi and Monica Morelli and Lucia Anemona and Isabel Bernges and Edzard Schwedhelm and Arnaldo Ippoliti and Alessandro Mauriello and B{\"o}ger, {Rainer H} and Massimo Federici",
note = "Copyright {\textcopyright} 2015 Elsevier Ireland Ltd. All rights reserved.",
year = "2015",
month = sep,
doi = "10.1016/j.atherosclerosis.2015.07.026",
language = "English",
volume = "242",
pages = "230--5",
journal = "ATHEROSCLEROSIS",
issn = "0021-9150",
publisher = "Elsevier Ireland Ltd",
number = "1",

}

RIS

TY - JOUR

T1 - FoxO1 regulates asymmetric dimethylarginine via downregulation of dimethylaminohydrolase 1 in human endothelial cells and subjects with atherosclerosis

AU - Menghini, Rossella

AU - Casagrande, Viviana

AU - Cardellini, Marina

AU - Ballanti, Marta

AU - Davato, Francesca

AU - Cardolini, Iris

AU - Stoehr, Robert

AU - Fabrizi, Marta

AU - Morelli, Monica

AU - Anemona, Lucia

AU - Bernges, Isabel

AU - Schwedhelm, Edzard

AU - Ippoliti, Arnaldo

AU - Mauriello, Alessandro

AU - Böger, Rainer H

AU - Federici, Massimo

N1 - Copyright © 2015 Elsevier Ireland Ltd. All rights reserved.

PY - 2015/9

Y1 - 2015/9

N2 - BACKGROUND AND AIMS: The O subfamily of forkhead (FoxO) 1 is a pivotal element in the regulation of endothelial activation. Compartmentalization and activity of FoxO1 is regulated by post translational modifications, but the implication in endothelial dysfunction and atherosclerosis remain controversial. Our aim was to identify FoxO1 related metabolic signatures in endothelial cells.METHODS AND RESULTS: Using metabolomics in human umbilical endothelial cells (HUVECs) overexpressing the wild type FoxO1 (FoxO1-WT), the acetylation defective mutant (FoxO1-KR), the unphosphorylated nuclear localized mutant (FoxO1-ADA) and the Green Fluorescent Protein (GFP) control vector, we identify metabolic pathways differentially affected by the different FoxO1 localization and activity. Among metabolites, asymmetric dimethylarginine (ADMA) was increased in FoxO1-ADA compared with FoxO1-WT and FoxO1-KR infected cells (p < 0.01). ADMA was further investigated to identify the molecular mechanisms to explain its link to FoxO1. We found that unrestrained FoxO1 activity leads to increase of ADMA via downregulation of its degrading enzyme, dimethylaminohydrolase (DDAH) 1. In human subjects (n = 89) the FoxO1/DDAH1/ADMA pathway marks unstable atherosclerosis.CONCLUSIONS: Our results point to ADMA as a biomarker to track deregulated FoxO1 activity in vivo.

AB - BACKGROUND AND AIMS: The O subfamily of forkhead (FoxO) 1 is a pivotal element in the regulation of endothelial activation. Compartmentalization and activity of FoxO1 is regulated by post translational modifications, but the implication in endothelial dysfunction and atherosclerosis remain controversial. Our aim was to identify FoxO1 related metabolic signatures in endothelial cells.METHODS AND RESULTS: Using metabolomics in human umbilical endothelial cells (HUVECs) overexpressing the wild type FoxO1 (FoxO1-WT), the acetylation defective mutant (FoxO1-KR), the unphosphorylated nuclear localized mutant (FoxO1-ADA) and the Green Fluorescent Protein (GFP) control vector, we identify metabolic pathways differentially affected by the different FoxO1 localization and activity. Among metabolites, asymmetric dimethylarginine (ADMA) was increased in FoxO1-ADA compared with FoxO1-WT and FoxO1-KR infected cells (p < 0.01). ADMA was further investigated to identify the molecular mechanisms to explain its link to FoxO1. We found that unrestrained FoxO1 activity leads to increase of ADMA via downregulation of its degrading enzyme, dimethylaminohydrolase (DDAH) 1. In human subjects (n = 89) the FoxO1/DDAH1/ADMA pathway marks unstable atherosclerosis.CONCLUSIONS: Our results point to ADMA as a biomarker to track deregulated FoxO1 activity in vivo.

U2 - 10.1016/j.atherosclerosis.2015.07.026

DO - 10.1016/j.atherosclerosis.2015.07.026

M3 - SCORING: Journal article

C2 - 26226438

VL - 242

SP - 230

EP - 235

JO - ATHEROSCLEROSIS

JF - ATHEROSCLEROSIS

SN - 0021-9150

IS - 1

ER -