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Overexpression of alanine-glyoxylate aminotransferase 2 protects from asymmetric dimethylarginine-induced endothelial dysfunction and aortic remodeling. / Rodionov, Roman N.; Jarzebska, Natalia; Burdin, Dmitrii; Todorov, Vladimir; Martens-Lobenhoffer, Jens; Hofmann, Anja; Kolouschek, Anne; Cordasic, Nada; Jacobi, Johannes; Rubets, Elena; Morawietz, Henning; O’Sullivan, John F.; Markov, Alexander G.; Bornstein, Stefan R.; Hilgers, Karl; Maas, Renke; Pfluecke, Christian; Chen, Ying Jie; Bode-Böger, Stefanie M.; Hugo, Christian P.M.; Hohenstein, Bernd; Weiss, Norbert.

в: Scientific Reports, Том 12, № 1, 9381, 12.2022.

Результаты исследований: Научные публикации в периодических изданияхстатьяРецензирование

Harvard

Rodionov, RN, Jarzebska, N, Burdin, D, Todorov, V, Martens-Lobenhoffer, J, Hofmann, A, Kolouschek, A, Cordasic, N, Jacobi, J, Rubets, E, Morawietz, H, O’Sullivan, JF, Markov, AG, Bornstein, SR, Hilgers, K, Maas, R, Pfluecke, C, Chen, YJ, Bode-Böger, SM, Hugo, CPM, Hohenstein, B & Weiss, N 2022, 'Overexpression of alanine-glyoxylate aminotransferase 2 protects from asymmetric dimethylarginine-induced endothelial dysfunction and aortic remodeling', Scientific Reports, Том. 12, № 1, 9381. https://doi.org/10.1038/s41598-022-13169-2

APA

Rodionov, R. N., Jarzebska, N., Burdin, D., Todorov, V., Martens-Lobenhoffer, J., Hofmann, A., Kolouschek, A., Cordasic, N., Jacobi, J., Rubets, E., Morawietz, H., O’Sullivan, J. F., Markov, A. G., Bornstein, S. R., Hilgers, K., Maas, R., Pfluecke, C., Chen, Y. J., Bode-Böger, S. M., ... Weiss, N. (2022). Overexpression of alanine-glyoxylate aminotransferase 2 protects from asymmetric dimethylarginine-induced endothelial dysfunction and aortic remodeling. Scientific Reports, 12(1), [9381]. https://doi.org/10.1038/s41598-022-13169-2

Vancouver

Author

Rodionov, Roman N. ; Jarzebska, Natalia ; Burdin, Dmitrii ; Todorov, Vladimir ; Martens-Lobenhoffer, Jens ; Hofmann, Anja ; Kolouschek, Anne ; Cordasic, Nada ; Jacobi, Johannes ; Rubets, Elena ; Morawietz, Henning ; O’Sullivan, John F. ; Markov, Alexander G. ; Bornstein, Stefan R. ; Hilgers, Karl ; Maas, Renke ; Pfluecke, Christian ; Chen, Ying Jie ; Bode-Böger, Stefanie M. ; Hugo, Christian P.M. ; Hohenstein, Bernd ; Weiss, Norbert. / Overexpression of alanine-glyoxylate aminotransferase 2 protects from asymmetric dimethylarginine-induced endothelial dysfunction and aortic remodeling. в: Scientific Reports. 2022 ; Том 12, № 1.

BibTeX

@article{f20c63fe2f224246a9d595c13b0d9d82,
title = "Overexpression of alanine-glyoxylate aminotransferase 2 protects from asymmetric dimethylarginine-induced endothelial dysfunction and aortic remodeling",
abstract = "Elevated plasma concentrations of asymmetric dimethylarginine (ADMA) are associated with an increased risk of mortality and adverse cardiovascular outcomes. ADMA can be metabolized by dimethylarginine dimethylaminohydrolases (DDAHs) and by alanine-glyoxylate aminotransferase 2 (AGXT2). Deletion of DDAH1 in mice leads to elevation of ADMA in plasma and increase in blood pressure, while overexpression of human DDAH1 is associated with a lower plasma ADMA concentration and protective cardiovascular effects. The possible role of alternative metabolism of ADMA by AGXT2 remains to be elucidated. The goal of the current study was to test the hypothesis that transgenic overexpression of AGXT2 leads to lowering of plasma levels of ADMA and protection from vascular damage in the setting of DDAH1 deficiency. We generated transgenic mice (TG) with ubiquitous overexpression of AGXT2. qPCR and Western Blot confirmed the expression of the transgene. Systemic ADMA levels were decreased by 15% in TG mice. In comparison with wild type animals plasma levels of asymmetric dimethylguanidino valeric acid (ADGV), the AGXT2 associated metabolite of ADMA, were six times higher. We crossed AGXT2 TG mice with DDAH1 knockout mice and observed that upregulation of AGXT2 lowers plasma ADMA and pulse pressure and protects the mice from endothelial dysfunction and adverse aortic remodeling. Upregulation of AGXT2 led to lowering of ADMA levels and protection from ADMA-induced vascular damage in the setting of DDAH1 deficiency. This is especially important, because all the efforts to develop pharmacological ADMA-lowering interventions by means of upregulation of DDAHs have been unsuccessful.",
keywords = "Amidohydrolases/genetics, Animals, Aorta/metabolism, Arginine/analogs & derivatives, Blood Pressure, Mice, Transaminases/genetics, Vascular Diseases",
author = "Rodionov, {Roman N.} and Natalia Jarzebska and Dmitrii Burdin and Vladimir Todorov and Jens Martens-Lobenhoffer and Anja Hofmann and Anne Kolouschek and Nada Cordasic and Johannes Jacobi and Elena Rubets and Henning Morawietz and O{\textquoteright}Sullivan, {John F.} and Markov, {Alexander G.} and Bornstein, {Stefan R.} and Karl Hilgers and Renke Maas and Christian Pfluecke and Chen, {Ying Jie} and Bode-B{\"o}ger, {Stefanie M.} and Hugo, {Christian P.M.} and Bernd Hohenstein and Norbert Weiss",
note = "Rodionov, R.N., Jarzebska, N., Burdin, D. et al. Overexpression of alanine-glyoxylate aminotransferase 2 protects from asymmetric dimethylarginine-induced endothelial dysfunction and aortic remodeling. Sci Rep 12, 9381 (2022). https://doi.org/10.1038/s41598-022-13169-2",
year = "2022",
month = dec,
doi = "10.1038/s41598-022-13169-2",
language = "English",
volume = "12",
journal = "Scientific Reports",
issn = "2045-2322",
publisher = "Nature Publishing Group",
number = "1",

}

RIS

TY - JOUR

T1 - Overexpression of alanine-glyoxylate aminotransferase 2 protects from asymmetric dimethylarginine-induced endothelial dysfunction and aortic remodeling

AU - Rodionov, Roman N.

AU - Jarzebska, Natalia

AU - Burdin, Dmitrii

AU - Todorov, Vladimir

AU - Martens-Lobenhoffer, Jens

AU - Hofmann, Anja

AU - Kolouschek, Anne

AU - Cordasic, Nada

AU - Jacobi, Johannes

AU - Rubets, Elena

AU - Morawietz, Henning

AU - O’Sullivan, John F.

AU - Markov, Alexander G.

AU - Bornstein, Stefan R.

AU - Hilgers, Karl

AU - Maas, Renke

AU - Pfluecke, Christian

AU - Chen, Ying Jie

AU - Bode-Böger, Stefanie M.

AU - Hugo, Christian P.M.

AU - Hohenstein, Bernd

AU - Weiss, Norbert

N1 - Rodionov, R.N., Jarzebska, N., Burdin, D. et al. Overexpression of alanine-glyoxylate aminotransferase 2 protects from asymmetric dimethylarginine-induced endothelial dysfunction and aortic remodeling. Sci Rep 12, 9381 (2022). https://doi.org/10.1038/s41598-022-13169-2

PY - 2022/12

Y1 - 2022/12

N2 - Elevated plasma concentrations of asymmetric dimethylarginine (ADMA) are associated with an increased risk of mortality and adverse cardiovascular outcomes. ADMA can be metabolized by dimethylarginine dimethylaminohydrolases (DDAHs) and by alanine-glyoxylate aminotransferase 2 (AGXT2). Deletion of DDAH1 in mice leads to elevation of ADMA in plasma and increase in blood pressure, while overexpression of human DDAH1 is associated with a lower plasma ADMA concentration and protective cardiovascular effects. The possible role of alternative metabolism of ADMA by AGXT2 remains to be elucidated. The goal of the current study was to test the hypothesis that transgenic overexpression of AGXT2 leads to lowering of plasma levels of ADMA and protection from vascular damage in the setting of DDAH1 deficiency. We generated transgenic mice (TG) with ubiquitous overexpression of AGXT2. qPCR and Western Blot confirmed the expression of the transgene. Systemic ADMA levels were decreased by 15% in TG mice. In comparison with wild type animals plasma levels of asymmetric dimethylguanidino valeric acid (ADGV), the AGXT2 associated metabolite of ADMA, were six times higher. We crossed AGXT2 TG mice with DDAH1 knockout mice and observed that upregulation of AGXT2 lowers plasma ADMA and pulse pressure and protects the mice from endothelial dysfunction and adverse aortic remodeling. Upregulation of AGXT2 led to lowering of ADMA levels and protection from ADMA-induced vascular damage in the setting of DDAH1 deficiency. This is especially important, because all the efforts to develop pharmacological ADMA-lowering interventions by means of upregulation of DDAHs have been unsuccessful.

AB - Elevated plasma concentrations of asymmetric dimethylarginine (ADMA) are associated with an increased risk of mortality and adverse cardiovascular outcomes. ADMA can be metabolized by dimethylarginine dimethylaminohydrolases (DDAHs) and by alanine-glyoxylate aminotransferase 2 (AGXT2). Deletion of DDAH1 in mice leads to elevation of ADMA in plasma and increase in blood pressure, while overexpression of human DDAH1 is associated with a lower plasma ADMA concentration and protective cardiovascular effects. The possible role of alternative metabolism of ADMA by AGXT2 remains to be elucidated. The goal of the current study was to test the hypothesis that transgenic overexpression of AGXT2 leads to lowering of plasma levels of ADMA and protection from vascular damage in the setting of DDAH1 deficiency. We generated transgenic mice (TG) with ubiquitous overexpression of AGXT2. qPCR and Western Blot confirmed the expression of the transgene. Systemic ADMA levels were decreased by 15% in TG mice. In comparison with wild type animals plasma levels of asymmetric dimethylguanidino valeric acid (ADGV), the AGXT2 associated metabolite of ADMA, were six times higher. We crossed AGXT2 TG mice with DDAH1 knockout mice and observed that upregulation of AGXT2 lowers plasma ADMA and pulse pressure and protects the mice from endothelial dysfunction and adverse aortic remodeling. Upregulation of AGXT2 led to lowering of ADMA levels and protection from ADMA-induced vascular damage in the setting of DDAH1 deficiency. This is especially important, because all the efforts to develop pharmacological ADMA-lowering interventions by means of upregulation of DDAHs have been unsuccessful.

KW - Amidohydrolases/genetics

KW - Animals

KW - Aorta/metabolism

KW - Arginine/analogs & derivatives

KW - Blood Pressure

KW - Mice

KW - Transaminases/genetics

KW - Vascular Diseases

UR - http://www.scopus.com/inward/record.url?scp=85131470400&partnerID=8YFLogxK

UR - https://www.mendeley.com/catalogue/246019e6-0f7a-3b0a-b9a7-71a4c48cec4c/

U2 - 10.1038/s41598-022-13169-2

DO - 10.1038/s41598-022-13169-2

M3 - Article

C2 - 35672381

AN - SCOPUS:85131470400

VL - 12

JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

IS - 1

M1 - 9381

ER -

ID: 99049548