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Article ; Online: Oxidative Post-Translational Modifications: A Focus on Cysteine

Bibli, Sofia-Iris / Fleming, Ingrid

2021 Volume 35, Issue 18, Page(s) 1494–1514

Abstract: Significance: ...

Abstract	Significance:
MeSH term(s)	Cystathionine gamma-Lyase/metabolism ; Cysteine/metabolism ; Endothelial Cells/metabolism ; Endothelium/metabolism ; Hydrogen Sulfide/metabolism ; Oxidation-Reduction ; Oxidative Stress ; Protein Processing, Post-Translational ; Sulfur
Chemical Substances	sulfur-32 ; Sulfur (70FD1KFU70) ; Cystathionine gamma-Lyase (EC 4.4.1.1) ; Cysteine (K848JZ4886) ; Hydrogen Sulfide (YY9FVM7NSN)
Language	English
Publishing date	2021-09-29
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1483836-9
ISSN	1557-7716 ; 1523-0864
ISSN (online)	1557-7716
ISSN	1523-0864
DOI	10.1089/ars.2021.0162
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Article ; Online: Loss of cardiac mitochondrial complex I persulfidation impairs NAD+ homeostasis in aging

Maria-Kyriaki Drekolia / Christina Karantanou / Ilka Wittig / Yuanyuan Li / Dominik C. Fuhrmann / Bernhard Brüne / Antonia Katsouda / Jiong Hu / Andreas Papapetropoulos / Sofia-Iris Bibli

Redox Biology, Vol 69, Iss , Pp 103014- (2024)

2024

Abstract: Protein persulfidation is a significant post-translational modification that involves addition of a sulfur atom to the cysteine thiol group and is facilitated by sulfide species. Persulfidation targets reactive cysteine residues within proteins, ... ...

Abstract	Protein persulfidation is a significant post-translational modification that involves addition of a sulfur atom to the cysteine thiol group and is facilitated by sulfide species. Persulfidation targets reactive cysteine residues within proteins, influencing their structure and/or function across various biological systems. This modification is evolutionarily conserved and plays a crucial role in preventing irreversible cysteine overoxidation, a process that becomes prominent with aging. While, persulfidation decreases with age, its levels in the aged heart and the functional implications of such a reduction in cardiac metabolism remain unknown. Here we interrogated the cardiac persulfydome in wild-type adult mice and age-matched mice lacking the two sulfide generating enzymes, namely cystathionine gamma lyase (CSE) and 3-mercaptopyruvate sulfurtransferase (3MST). Our findings revealed that cardiac persulfidated proteins in wild type hearts are less abundant compared to those in other organs, with a primary involvement in mitochondrial metabolic processes. We further focused on one specific target, NDUFB7, which undergoes persulfidation by both CSE and 3MST derived sulfide species. In particular, persulfidation of cysteines C80 and C90 in NDUFB7 protects the protein from overoxidation and maintains the complex I activity in cardiomyocytes. As the heart ages, the levels of CSE and 3MST in cardiomyocytes decline, leading to reduced NDUFB7 persulfidation and increased cardiac NADH/NAD+ ratio. Collectively, our data provide compelling evidence for a direct link between cardiac persulfidation and mitochondrial complex I activity, which is compromised in aging.
Keywords	Persulfidation ; Cardiac aging ; CSE ; 3MST ; NDUFB7 ; Medicine (General) ; R5-920 ; Biology (General) ; QH301-705.5
Subject code	572
Language	English
Publishing date	2024-02-01T00:00:00Z
Publisher	Elsevier
Document type	Article ; Online
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Article: Unravelling the impact of aging on the human endothelial lncRNA transcriptome.

Drekolia, Maria-Kyriaki / Talyan, Sweta / Cordellini Emídio, Rebeca / Boon, Reinier Abraham / Guenther, Stefan / Looso, Mario / Dumbović, Gabrijela / Bibli, Sofia-Iris

Frontiers in genetics

2022 Volume 13, Page(s) 1035380

Abstract: The incidence and prevalence of cardiovascular disease is highest among the elderly. There is a need to further understand the mechanisms behind endothelial cell aging in order to achieve vascular rejuvenation and minimize the onset of age-related ... ...

Abstract	The incidence and prevalence of cardiovascular disease is highest among the elderly. There is a need to further understand the mechanisms behind endothelial cell aging in order to achieve vascular rejuvenation and minimize the onset of age-related vascular diseases. Long non-coding RNAs (lncRNAs) have been proposed to regulate numerous processes in the human genome, yet their function in vascular aging and their therapeutic potential remain largely unknown. This is primarily because the majority of studies investigating the impact of aging on lncRNA expression heavily rely on
Language	English
Publishing date	2022-10-21
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2606823-0
ISSN	1664-8021
ISSN	1664-8021
DOI	10.3389/fgene.2022.1035380
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Article ; Online: Endothelial-dependent S-Sulfhydration of tissue factor pathway inhibitor regulates blood coagulation

Janina Wittig / Maria-Kyriaki Drekolia / Anastasia Kyselova / Fredy Delgado Lagos / Magdalena L. Bochenek / Jiong Hu / Katrin Schäfer / Ingrid Fleming / Sofia-Iris Bibli

Redox Biology, Vol 62, Iss , Pp 102694- (2023)

2023

Abstract: Tissue factor pathway inhibitor (TFPI) is an important regulator of coagulation and a link between inflammation and thrombosis. Here we investigated whether endothelial cell-driven oxidative post-translational modifications could have an impact on TFPI ... ...

Abstract	Tissue factor pathway inhibitor (TFPI) is an important regulator of coagulation and a link between inflammation and thrombosis. Here we investigated whether endothelial cell-driven oxidative post-translational modifications could have an impact on TFPI activity. We focused on S-sulfhydration, which is a hydrogen sulfide-dependent post-translational modification that, in endothelial cells, is regulated by the enzyme cystathionine γ-lyase (CSE). The study made use of human primary endothelial cells and blood from healthy individuals or subjects with atherosclerosis as well as from mice lacking endothelial CSE. TFPI was S-sulfhydrated in endothelial cells from healthy individuals and mice, while the loss of endothelial CSE expression/activity reduced its modification. Non-S-sulfhydrated TFPI was no longer able to interact with factor Xa, which facilitated the activation of tissue factor. Similarly, non-S-sulfhydratable TFPI mutants bound less protein S, while supplementation with hydrogen sulfide donors, preserved TFPI activity. Phenotypically, loss of TFPI S-sulfhydration increased clot retraction, suggesting that this post-translational modification is a new endothelial cell-dependent mechanism that contributes to the regulation of blood coagulation.
Keywords	TFPI ; Endothelial CSE ; S-sulfhydration ; Coagulation ; Medicine (General) ; R5-920 ; Biology (General) ; QH301-705.5
Subject code	570
Language	English
Publishing date	2023-06-01T00:00:00Z
Publisher	Elsevier
Document type	Article ; Online
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Article ; Online: Endothelial-dependent S-Sulfhydration of tissue factor pathway inhibitor regulates blood coagulation.

Wittig, Janina / Drekolia, Maria-Kyriaki / Kyselova, Anastasia / Delgado Lagos, Fredy / Bochenek, Magdalena L / Hu, Jiong / Schäfer, Katrin / Fleming, Ingrid / Bibli, Sofia-Iris

Redox biology

2023 Volume 62, Page(s) 102694

Abstract	Tissue factor pathway inhibitor (TFPI) is an important regulator of coagulation and a link between inflammation and thrombosis. Here we investigated whether endothelial cell-driven oxidative post-translational modifications could have an impact on TFPI activity. We focused on S-sulfhydration, which is a hydrogen sulfide-dependent post-translational modification that, in endothelial cells, is regulated by the enzyme cystathionine γ-lyase (CSE). The study made use of human primary endothelial cells and blood from healthy individuals or subjects with atherosclerosis as well as from mice lacking endothelial CSE. TFPI was S-sulfhydrated in endothelial cells from healthy individuals and mice, while the loss of endothelial CSE expression/activity reduced its modification. Non-S-sulfhydrated TFPI was no longer able to interact with factor Xa, which facilitated the activation of tissue factor. Similarly, non-S-sulfhydratable TFPI mutants bound less protein S, while supplementation with hydrogen sulfide donors, preserved TFPI activity. Phenotypically, loss of TFPI S-sulfhydration increased clot retraction, suggesting that this post-translational modification is a new endothelial cell-dependent mechanism that contributes to the regulation of blood coagulation.
MeSH term(s)	Animals ; Humans ; Mice ; Blood Coagulation ; Endothelial Cells/metabolism ; Hydrogen Sulfide/metabolism ; Lipoproteins
Chemical Substances	Hydrogen Sulfide (YY9FVM7NSN) ; lipoprotein-associated coagulation inhibitor ; Lipoproteins
Language	English
Publishing date	2023-04-03
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2701011-9
ISSN	2213-2317 ; 2213-2317
ISSN (online)	2213-2317
ISSN	2213-2317
DOI	10.1016/j.redox.2023.102694
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Loss of cardiac mitochondrial complex I persulfidation impairs NAD

Drekolia, Maria-Kyriaki / Karantanou, Christina / Wittig, Ilka / Li, Yuanyuan / Fuhrmann, Dominik C / Brüne, Bernhard / Katsouda, Antonia / Hu, Jiong / Papapetropoulos, Andreas / Bibli, Sofia-Iris

Redox biology

2023 Volume 69, Page(s) 103014

Abstract	Protein persulfidation is a significant post-translational modification that involves addition of a sulfur atom to the cysteine thiol group and is facilitated by sulfide species. Persulfidation targets reactive cysteine residues within proteins, influencing their structure and/or function across various biological systems. This modification is evolutionarily conserved and plays a crucial role in preventing irreversible cysteine overoxidation, a process that becomes prominent with aging. While, persulfidation decreases with age, its levels in the aged heart and the functional implications of such a reduction in cardiac metabolism remain unknown. Here we interrogated the cardiac persulfydome in wild-type adult mice and age-matched mice lacking the two sulfide generating enzymes, namely cystathionine gamma lyase (CSE) and 3-mercaptopyruvate sulfurtransferase (3MST). Our findings revealed that cardiac persulfidated proteins in wild type hearts are less abundant compared to those in other organs, with a primary involvement in mitochondrial metabolic processes. We further focused on one specific target, NDUFB7, which undergoes persulfidation by both CSE and 3MST derived sulfide species. In particular, persulfidation of cysteines C80 and C90 in NDUFB7 protects the protein from overoxidation and maintains the complex I activity in cardiomyocytes. As the heart ages, the levels of CSE and 3MST in cardiomyocytes decline, leading to reduced NDUFB7 persulfidation and increased cardiac NADH/NAD
MeSH term(s)	Mice ; Animals ; Hydrogen Sulfide/metabolism ; NAD ; Cysteine/metabolism ; Sulfides/metabolism ; Aging/genetics ; Homeostasis
Chemical Substances	Hydrogen Sulfide (YY9FVM7NSN) ; NAD (0U46U6E8UK) ; Cysteine (K848JZ4886) ; Sulfides
Language	English
Publishing date	2023-12-25
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2701011-9
ISSN	2213-2317 ; 2213-2317
ISSN (online)	2213-2317
ISSN	2213-2317
DOI	10.1016/j.redox.2023.103014
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Article ; Online: Regulation of Long Non-Coding RNAs by Statins in Atherosclerosis

Diamantis I. Tsilimigras / Sofia-Iris Bibli / Gerasimos Siasos / Evangelos Oikonomou / Despina N. Perrea / Konstantinos Filis / Dimitrios Tousoulis / Fragiska Sigala

Biomolecules, Vol 11, Iss 623, p

2021 Volume 623

Abstract: Despite increased public health awareness, atherosclerosis remains a leading cause of mortality worldwide. Significant variations in response to statin treatment have been noted among different populations suggesting that the efficacy of statins may be ... ...

Abstract	Despite increased public health awareness, atherosclerosis remains a leading cause of mortality worldwide. Significant variations in response to statin treatment have been noted among different populations suggesting that the efficacy of statins may be altered by both genetic and environmental factors. The existing literature suggests that certain long noncoding RNAs (lncRNAs) might be up- or downregulated among patients with atherosclerosis. LncRNA may act on multiple levels (cholesterol homeostasis, vascular inflammation, and plaque destabilization) and exert atheroprotective or atherogenic effects. To date, only a few studies have investigated the interplay between statins and lncRNAs known to be implicated in atherosclerosis. The current review characterizes the role of lncRNAs in atherosclerosis and summarizes the available evidence related to the effect of statins in regulating lncRNAs.
Keywords	statin ; RNA ; epigenetics ; vascular biology ; Microbiology ; QR1-502
Language	English
Publishing date	2021-04-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
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Article ; Online: Regulation of Long Non-Coding RNAs by Statins in Atherosclerosis.

Tsilimigras, Diamantis I / Bibli, Sofia-Iris / Siasos, Gerasimos / Oikonomou, Evangelos / Perrea, Despina N / Filis, Konstantinos / Tousoulis, Dimitrios / Sigala, Fragiska

Biomolecules

2021 Volume 11, Issue 5

Abstract	Despite increased public health awareness, atherosclerosis remains a leading cause of mortality worldwide. Significant variations in response to statin treatment have been noted among different populations suggesting that the efficacy of statins may be altered by both genetic and environmental factors. The existing literature suggests that certain long noncoding RNAs (lncRNAs) might be up- or downregulated among patients with atherosclerosis. LncRNA may act on multiple levels (cholesterol homeostasis, vascular inflammation, and plaque destabilization) and exert atheroprotective or atherogenic effects. To date, only a few studies have investigated the interplay between statins and lncRNAs known to be implicated in atherosclerosis. The current review characterizes the role of lncRNAs in atherosclerosis and summarizes the available evidence related to the effect of statins in regulating lncRNAs.
Language	English
Publishing date	2021-04-22
Publishing country	Switzerland
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	2701262-1
ISSN	2218-273X ; 2218-273X
ISSN (online)	2218-273X
ISSN	2218-273X
DOI	10.3390/biom11050623
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Article ; Online: MPST sulfurtransferase maintains mitochondrial protein import and cellular bioenergetics to attenuate obesity.

Katsouda, Antonia / Valakos, Dimitrios / Dionellis, Vasilios S / Bibli, Sofia-Iris / Akoumianakis, Ioannis / Karaliota, Sevasti / Zuhra, Karim / Fleming, Ingrid / Nagahara, Noriyuki / Havaki, Sophia / Gorgoulis, Vassilis G / Thanos, Dimitris / Antoniades, Charalambos / Szabo, Csaba / Papapetropoulos, Andreas

The Journal of experimental medicine

2022 Volume 219, Issue 7

Abstract: Given the clinical, economic, and societal impact of obesity, unraveling the mechanisms of adipose tissue expansion remains of fundamental significance. We previously showed that white adipose tissue (WAT) levels of 3-mercaptopyruvate sulfurtransferase ( ... ...

Abstract	Given the clinical, economic, and societal impact of obesity, unraveling the mechanisms of adipose tissue expansion remains of fundamental significance. We previously showed that white adipose tissue (WAT) levels of 3-mercaptopyruvate sulfurtransferase (MPST), a mitochondrial cysteine-catabolizing enzyme that yields pyruvate and sulfide species, are downregulated in obesity. Here, we report that Mpst deletion results in fat accumulation in mice fed a high-fat diet (HFD) through transcriptional and metabolic maladaptation. Mpst-deficient mice on HFD exhibit increased body weight and inguinal WAT mass, reduced metabolic rate, and impaired glucose/insulin tolerance. At the molecular level, Mpst ablation activates HIF1α, downregulates subunits of the translocase of outer/inner membrane (TIM/TOM) complex, and impairs mitochondrial protein import. MPST deficiency suppresses the TCA cycle, oxidative phosphorylation, and fatty acid oxidation, enhancing lipid accumulation. Sulfide donor administration to obese mice reverses the HFD-induced changes. These findings reveal the significance of MPST for white adipose tissue biology and metabolic health and identify a potential new therapeutic target for obesity.
MeSH term(s)	Animals ; Diet, High-Fat ; Energy Metabolism ; Glucose Intolerance ; Mice ; Mice, Inbred C57BL ; Mitochondrial Proteins/metabolism ; Obesity/metabolism ; Sulfides ; Sulfurtransferases/metabolism
Chemical Substances	Mitochondrial Proteins ; Sulfides ; Sulfurtransferases (EC 2.8.1.-)
Language	English
Publishing date	2022-05-26
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	218343-2
ISSN	1540-9538 ; 0022-1007
ISSN (online)	1540-9538
ISSN	0022-1007
DOI	10.1084/jem.20211894
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Article ; Online: Endothelial cells drive organ fibrosis in mice by inducing expression of the transcription factor SOX9.

Trogisch, Felix A / Abouissa, Aya / Keles, Merve / Birke, Anne / Fuhrmann, Manuela / Dittrich, Gesine M / Weinzierl, Nina / Wink, Elvira / Cordero, Julio / Elsherbiny, Adel / Martin-Garrido, Abel / Grein, Steve / Hemanna, Shruthi / Hofmann, Ellen / Nicin, Luka / Bibli, Sofia-Iris / Airik, Rannar / Kispert, Andreas / Kist, Ralf /

Quanchao, Sun / Kürschner, Sina W / Winkler, Manuel / Gretz, Norbert / Mogler, Carolin / Korff, Thomas / Koch, Philipp-Sebastian / Dimmeler, Stefanie / Dobreva, Gergana / Heineke, Joerg

Science translational medicine

2024 Volume 16, Issue 736, Page(s) eabq4581

Abstract: Fibrosis is a hallmark of chronic disease. Although fibroblasts are involved, it is unclear to what extent endothelial cells also might contribute. We detected increased expression of the transcription ... ...

Abstract	Fibrosis is a hallmark of chronic disease. Although fibroblasts are involved, it is unclear to what extent endothelial cells also might contribute. We detected increased expression of the transcription factor
MeSH term(s)	Animals ; Humans ; Mice ; Disease Models, Animal ; Endothelial Cells ; Fibrosis ; Heart Failure ; Intercellular Signaling Peptides and Proteins ; Liver Cirrhosis/complications ; SOX9 Transcription Factor/genetics ; Transcription Factors
Chemical Substances	Intercellular Signaling Peptides and Proteins ; SOX9 protein, human ; SOX9 Transcription Factor ; Transcription Factors ; Sox9 protein, mouse
Language	English
Publishing date	2024-02-28
Publishing country	United States
Document type	Journal Article
ZDB-ID	2518854-9
ISSN	1946-6242 ; 1946-6234
ISSN (online)	1946-6242
ISSN	1946-6234
DOI	10.1126/scitranslmed.abq4581
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