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Article: Oxidative Stress in Liver Pathophysiology and Disease.

Allameh, Abdolamir / Niayesh-Mehr, Reyhaneh / Aliarab, Azadeh / Sebastiani, Giada / Pantopoulos, Kostas

2023 Volume 12, Issue 9

Abstract: The liver is an organ that is particularly exposed to reactive oxygen species (ROS), which not only arise during metabolic functions but also during the biotransformation of xenobiotics. The disruption of redox balance causes oxidative stress, which ... ...

Abstract	The liver is an organ that is particularly exposed to reactive oxygen species (ROS), which not only arise during metabolic functions but also during the biotransformation of xenobiotics. The disruption of redox balance causes oxidative stress, which affects liver function, modulates inflammatory pathways and contributes to disease. Thus, oxidative stress is implicated in acute liver injury and in the pathogenesis of prevalent infectious or metabolic chronic liver diseases such as viral hepatitis B or C, alcoholic fatty liver disease, non-alcoholic fatty liver disease (NAFLD) and non-alcoholic steatohepatitis (NASH). Moreover, oxidative stress plays a crucial role in liver disease progression to liver fibrosis, cirrhosis and hepatocellular carcinoma (HCC). Herein, we provide an overview on the effects of oxidative stress on liver pathophysiology and the mechanisms by which oxidative stress promotes liver disease.
Language	English
Publishing date	2023-08-22
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2704216-9
ISSN	2076-3921
ISSN	2076-3921
DOI	10.3390/antiox12091653
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Article: Contribution of Autophagy to Epithelial Mesenchymal Transition Induction during Cancer Progression.

Strippoli, Raffaele / Niayesh-Mehr, Reyhaneh / Adelipour, Maryam / Khosravi, Arezoo / Cordani, Marco / Zarrabi, Ali / Allameh, Abdolamir

Cancers

2024 Volume 16, Issue 4

Abstract: Epithelial Mesenchymal Transition (EMT) is a dedifferentiation process implicated in many physio-pathological conditions including tumor transformation. EMT is regulated by several extracellular mediators and under certain conditions it can be reversible. ...

Abstract	Epithelial Mesenchymal Transition (EMT) is a dedifferentiation process implicated in many physio-pathological conditions including tumor transformation. EMT is regulated by several extracellular mediators and under certain conditions it can be reversible. Autophagy is a conserved catabolic process in which intracellular components such as protein/DNA aggregates and abnormal organelles are degraded in specific lysosomes. In cancer, autophagy plays a controversial role, acting in different conditions as both a tumor suppressor and a tumor-promoting mechanism. Experimental evidence shows that deep interrelations exist between EMT and autophagy-related pathways. Although this interplay has already been analyzed in previous studies, understanding mechanisms and the translational implications of autophagy/EMT need further study. The role of autophagy in EMT is not limited to morphological changes, but activation of autophagy could be important to DNA repair/damage system, cell adhesion molecules, and cell proliferation and differentiation processes. Based on this, both autophagy and EMT and related pathways are now considered as targets for cancer therapy. In this review article, the contribution of autophagy to EMT and progression of cancer is discussed. This article also describes the multiple connections between EMT and autophagy and their implication in cancer treatment.
Language	English
Publishing date	2024-02-16
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2527080-1
ISSN	2072-6694
ISSN	2072-6694
DOI	10.3390/cancers16040807
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Article ; Online: Endothelin-1 dependent expression of GAG genes involves NOX and p38 mediated Smad linker region phosphorylation.

Babaahmadi-Rezaei, Hossein / Mohamed, Raafat / Dayati, Parisa / Mehr, Reyhaneh Niayesh / Seif, Faezeh / Sharifat, Narges / Khedri, Azam / Kamato, Danielle / Little, Peter J

Clinical and experimental pharmacology & physiology

2022 Volume 49, Issue 7, Page(s) 710–718

Abstract: Endothelin-1 (ET-1) is implicated in the development of atherosclerosis and mediates glycosaminoglycan (GAG) chain hyperelongation on proteoglycans. Our aim was to identify the ET-1-mediated signalling pathway involving NADPH oxidase (NOX), p38 MAP ... ...

Abstract	Endothelin-1 (ET-1) is implicated in the development of atherosclerosis and mediates glycosaminoglycan (GAG) chain hyperelongation on proteoglycans. Our aim was to identify the ET-1-mediated signalling pathway involving NADPH oxidase (NOX), p38 MAP kinsae and Smad2 linker region phosphorylation (phospho-Smad2L) regulate GAG synthesising enzymes mRNA expression (C4ST-1 and ChSy1) involved in GAG chains hyperelongation in human vascular smooth muscle cells (VSMCs). Signalling intermediates were detected and quantified by Western blotting and the mRNA levels of GAG synthesising enzymes were assessed by quantitative real-time polymerase chain reaction (qRT-PCR). ET-1 treatment of human VSMCs resulted in an increase in phospho-Smad2L level. The TGF-β receptor antagonist, SB431542 and the mixed ET
MeSH term(s)	Bosentan ; Endothelin-1/genetics ; Endothelin-1/metabolism ; Genes, gag ; Glycosaminoglycans/metabolism ; Humans ; NADPH Oxidases/metabolism ; Phosphorylation ; RNA, Messenger/metabolism
Chemical Substances	Endothelin-1 ; Glycosaminoglycans ; RNA, Messenger ; NADPH Oxidases (EC 1.6.3.-) ; Bosentan (Q326023R30)
Language	English
Publishing date	2022-05-17
Publishing country	Australia
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	189277-0
ISSN	1440-1681 ; 0305-1870 ; 0143-9294
ISSN (online)	1440-1681
ISSN	0305-1870 ; 0143-9294
DOI	10.1111/1440-1681.13650
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Article ; Online: Endothelin-1 mediated glycosaminoglycan synthesizing gene expression involves NOX-dependent transactivation of the transforming growth factor-β receptor.

Babaahmadi-Rezaei, Hossein / Little, Peter J / Mohamed, Raafat / Zadeh, Ghorban Mohammad / Kheirollah, Alireza / Mehr, Reyhaneh Niayesh / Kamato, Danielle / Dayati, Parisa

Molecular and cellular biochemistry

2022 Volume 477, Issue 4, Page(s) 981–988

Abstract: G protein-coupled receptor (GPCR) agonist endothelin-1 (ET-1) through transactivation of the transforming growth factor (TGF) β receptor (TGFBR1) stimulates glycosaminoglycan (GAG) elongation on proteoglycans. GPCR agonists thrombin and lysophosphatidic ... ...

Abstract	G protein-coupled receptor (GPCR) agonist endothelin-1 (ET-1) through transactivation of the transforming growth factor (TGF) β receptor (TGFBR1) stimulates glycosaminoglycan (GAG) elongation on proteoglycans. GPCR agonists thrombin and lysophosphatidic acid (LPA) via respective receptors transactivate the TGFBR1 via Rho/ROCK dependent pathways however mechanistic insight for ET-1 transactivation of the TGFBR1 remains unknown. NADPH oxidase (NOX) generates reactive oxygen species (ROS) and is a signalling entity implicated in the pathogenesis of many diseases including atherosclerosis. If implicated in this pathway, NOX/ROS would be a potential therapeutic target. In this study, we investigated the involvement of NOX in ET-1/ET receptor-mediated transactivation of TGFBR1 to stimulate mRNA expression of GAG chain synthesizing enzymes chondroitin 4-O-sulfotransferase 1 (C4ST-1) and chondroitin sulfate synthase 1 (ChSy-1). The invitro model used vascular smooth muscle cells that were treated with pharmacological antagonists in the presence and absence of ET-1 or TGF-β. Proteins and phosphoproteins isolated from treated cells were quantified by western blotting and quantitative real-time PCR was used to assess mRNA expression of GAG synthesizing enzymes. In the presence of diphenyliodonium (DPI) (NOX inhibitor), ET-1 stimulated phospho-Smad2C levels were inhibited. ET-1 mediated mRNA expression of GAG synthesizing enzymes C4ST-1 and ChSy-1 was also blocked by TGBFR1 antagonists, SB431542, broad spectrum ET receptor antagonist bosentan, DPI and ROS scavenger N-acetyl-L-cysteine. This work shows that NOX and ROS play an important role in ET-1 mediated transactivation of the TGFBR1 and downstream gene targets associated with GAG chain elongation. As ROS is involved in GPCR to protein tyrosine kinase receptor transactivation, the NOX/ROS axis presents as the first common biochemical target in all GPCR to kinase receptor transactivation signalling.
MeSH term(s)	Cells, Cultured ; Endothelin-1/genetics ; Endothelin-1/metabolism ; Glycosaminoglycans/metabolism ; Humans ; NADPH Oxidases/genetics ; NADPH Oxidases/metabolism ; Receptor, Transforming Growth Factor-beta Type I/biosynthesis ; Receptor, Transforming Growth Factor-beta Type I/genetics ; Transcriptional Activation
Chemical Substances	Endothelin-1 ; Glycosaminoglycans ; NADPH Oxidases (EC 1.6.3.-) ; Receptor, Transforming Growth Factor-beta Type I (EC 2.7.11.30) ; TGFBR1 protein, human (EC 2.7.11.30)
Language	English
Publishing date	2022-01-04
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	184833-1
ISSN	1573-4919 ; 0300-8177
ISSN (online)	1573-4919
ISSN	0300-8177
DOI	10.1007/s11010-021-04342-8
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Article ; Online: Endothelin-1 increases CHSY-1 expression in aortic endothelial cells via transactivation of transforming growth factor β type I receptor induced by type B receptor endothelin-1.

Seif, Faezeh / Little, Peter J / Niayesh-Mehr, Reyhaneh / Zamanpour, Masoumeh / Babaahmadi-Rezaei, Hossein

The Journal of pharmacy and pharmacology

2019 Volume 71, Issue 6, Page(s) 988–995

Abstract: Objectives: TGF-β through hyperelongation of glycosaminoglycan (GAG) chains leads to binding of low-density lipoproteins to the proteoglycans. The vasoactive peptide, endothelin-1 (ET-1), plays a key role in the development of atherosclerosis. This ... ...

Abstract	Objectives: TGF-β through hyperelongation of glycosaminoglycan (GAG) chains leads to binding of low-density lipoproteins to the proteoglycans. The vasoactive peptide, endothelin-1 (ET-1), plays a key role in the development of atherosclerosis. This study addressed the question whether ET-1 by activating the Rho kinase and cytoskeletal rearrangement can transactivate the TGF-β receptor leading to phosphorylation of the transcription factor Smad2 and increased expression of the GAG chain synthesizing enzyme such as chondroitin synthase-1 (CHSY-1) in bovine aortic endothelial cells (BAECs). Methods: In this study, intermediates in ET-1-induced Smad2C phosphorylation and the protein level of CHSY-1 were identified and quantified by Western blotting. Key findings: Endothelin-1 caused time-dependent phosphorylation of Smad2C which was inhibited in the presence of the endothelin B receptor antagonist, BQ788. The response to ET-1 was inhibited by the Rho/ROCK kinase antagonist, Y27632 and by cytochalasin D, an inhibitor of actin polymerization but the ET-1-mediated pSmad2C was not inhibited by the matrix metalloproteinase (MMP) inhibitor, GM6001. ET-1 increased CHSY-1 protein level, which was inhibited in the presence of BQ788, cytochalasin D and Y27632. Conclusions: Endothelin-1 signalling via the ET
MeSH term(s)	Amides/pharmacology ; Animals ; Aorta/cytology ; Blotting, Western ; Cattle ; Cells, Cultured ; Cytochalasin D/pharmacology ; Endothelial Cells/metabolism ; Endothelin-1/metabolism ; N-Acetylgalactosaminyltransferases/genetics ; Oligopeptides/pharmacology ; Phosphorylation/physiology ; Piperidines/pharmacology ; Pyridines/pharmacology ; Receptor, Endothelin B/drug effects ; Receptor, Endothelin B/metabolism ; Receptor, Transforming Growth Factor-beta Type I/metabolism ; Receptors, Transforming Growth Factor beta/metabolism ; Time Factors ; Transcriptional Activation/physiology ; Transforming Growth Factor beta/metabolism ; rho-Associated Kinases/metabolism
Chemical Substances	Amides ; Endothelin-1 ; Oligopeptides ; Piperidines ; Pyridines ; Receptor, Endothelin B ; Receptors, Transforming Growth Factor beta ; Transforming Growth Factor beta ; Y 27632 (138381-45-0) ; Cytochalasin D (22144-77-0) ; BQ 788 (44OLL8XEJ4) ; N-Acetylgalactosaminyltransferases (EC 2.4.1.-) ; chondroitin synthase (EC 2.4.1.175) ; rho-Associated Kinases (EC 2.7.11.1) ; Receptor, Transforming Growth Factor-beta Type I (EC 2.7.11.30)
Language	English
Publishing date	2019-02-27
Publishing country	England
Document type	Journal Article
ZDB-ID	3107-0
ISSN	2042-7158 ; 0022-3573 ; 0373-1022
ISSN (online)	2042-7158
ISSN	0022-3573 ; 0373-1022
DOI	10.1111/jphp.13081
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Article ; Online: The Effect of Endothelin-1 on Gene Expression of Nicotinamide Adenine Dinucleotide Phosphate (NADPH) Oxidase via Transforming Growth Factor Beta (TGF–β) Receptor in Human Aortic Smooth Muscle Cells

Parisa Dayati / Reyhaneh Niayesh-Mehr / Alireza Jafari / Hossein Babaahmadi-Rezaei

مجله دانشکده پزشکی اصفهان, Vol 36, Iss 474, Pp 344-

2018 Volume 350

Abstract: Background: Nicotinamide adenine dinucleotide phosphate (NADPH) oxidase (Nox) is one of the predominant sources of the production of free oxygen radicals in the vascular wall. Endothelin-1 is a potent vasoconstrictor factor that also has mitogenic ... ...

Abstract	Background: Nicotinamide adenine dinucleotide phosphate (NADPH) oxidase (Nox) is one of the predominant sources of the production of free oxygen radicals in the vascular wall. Endothelin-1 is a potent vasoconstrictor factor that also has mitogenic activity in vascular smooth muscle cells. The activation of transforming growth factor beta (TGF–β) receptor by endothelin-1 plays an important role in cardiovascular diseases. The aim of this study was to investigate the changes of Nox gene expression in smooth muscle cells treated with endothelin-1 in the presence of the transforming growth factor beta-receptor antagonist. Methods: Human aortic smooth muscle cells (HA-SMCs) were treated with endothelin-1 (100 nM) and transforming growth factor beta (2 ng/ml) in the presence and absence of transforming growth factor beta-receptor antagonist. The mRNA expression of Nox1 and Nox4 were assessed using real-time polymerase chain reaction (PCR) technique. Findings: The gene expression of Nox1 increased in the presence of endothelin-1 compared to control group, but there was no change in gene expression of Nox4. Increasing the expression of Nox1 decreased in the presence of transforming growth factor beta-receptor antagonist (10 μM). Conclusion: The results of this study showed that activation of transforming growth factor beta pathway is one of the mechanisms for increasing the mRNA expression of Nox1 by endothelin-1.
Keywords	NADPH oxidase ; Endothelin-1 ; Transforming growth factor beta ; Medicine ; R ; Medicine (General) ; R5-920
Subject code	306
Language	Persian
Publishing date	2018-06-01T00:00:00Z
Publisher	Vesnu Publications
Document type	Article ; Online
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Article ; Online: Reactive Oxygen Species and p38MAPK Have a Role in the Smad2 Linker Region Phosphorylation Induced by TGF-β

Reyhaneh Niayesh Mehr / Alireza Kheirollah / Faezeh Seif / Parisa Dayati / Hossein Babaahmadi Rezaei

Iranian Journal of Medical Sciences, Vol 43, Iss 4, Pp 401-

2018 Volume 408

Abstract: Background: Transforming growth factor-β (TGF-β) in addition to the C-terminal region can phosphorylate receptor-regulated Smads (R-Smads) in their linker region. The aim of the present study was to evaluate the role of signaling mediators such as NAD(P) ... ...

Abstract	Background: Transforming growth factor-β (TGF-β) in addition to the C-terminal region can phosphorylate receptor-regulated Smads (R-Smads) in their linker region. The aim of the present study was to evaluate the role of signaling mediators such as NAD(P)H oxidases (reactive oxygen species [ROS] generators), ROS, and ROS-sensitive p38 mitogen-activated protein kinase (p38MAPK) in this signaling pathway in cultured human vascular smooth muscle cells (VSMCs). Methods: The present in vitro study was performed on human VSMCs. Proteins were detected by western blotting utilizing an anti-phospho-Smad2 (Ser245/250/255) rabbit polyclonal antibody and a horseradish peroxidase-labeled secondary antibody. Glyceraldehyde-3-phosphate dehydrogenase was used as a loading control. The phospho-Smad2 linker region (pSmad2L) was detected in all the experimental groups: a control group (untreated group), a group treated with TGF-β (2 ng/mL), and a group treated with TGF-β plus different inhibitors. The data were normalized and presented as mean ± SEM. The statistical analyses were performed using SPSS, version 16.0, and the nonparametric Kruskal–Wallis test. A P value smaller than 0.05 was considered statistically significant. Results: The VSMCs treated with TGF-β (2 ng/mL) showed a time-dependent increase in the pSmad2L level. The highest level was observed at 15 minutes (P=0.03). The inhibitors of NAD(P) H oxidases (diphenyleneiodonium and apocynin) (P=0.04), ROS scavenger (N-acetylcysteine) (P=0.04), and p38MAPK inhibitor (SB-202190) (P=0.04) were able to reduce the increased level of the pSmad2L by TGF-β. Conclusion: Our results suggested that NAD(P)H oxidases played an important role in the Smad2L phosphorylation in the human VSMCs. Furthermore, our results confirmed that ROS and p38MAPK were involved in this signaling pathway. Thus, TGF-β via a ROS-dependent mechanism can transmit its signals to the pSmad2L.
Keywords	Transforming growth factor beta ; Smad2 protein ; Reactive oxygen species ; NADPH oxidase 4 ; P38 mitogen-activated protein kinases ; Medicine (General) ; R5-920
Subject code	630
Language	English
Publishing date	2018-07-01T00:00:00Z
Publisher	Shiraz University of Medical Sciences
Document type	Article ; Online
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Article: Reactive Oxygen Species and p38MAPK Have a Role in the Smad2 Linker Region Phosphorylation Induced by TGF-β.

Mehr, Reyhaneh Niayesh / Kheirollah, Alireza / Seif, Faezeh / Dayati, Parisa / Babaahmadi-Rezaei, Hossein

Iranian journal of medical sciences

2018 Volume 43, Issue 4, Page(s) 401–408

Abstract	Background: Transforming growth factor-β (TGF-β) in addition to the C-terminal region can phosphorylate receptor-regulated Smads (R-Smads) in their linker region. The aim of the present study was to evaluate the role of signaling mediators such as NAD(P)H oxidases (reactive oxygen species [ROS] generators), ROS, and ROS-sensitive p38 mitogen-activated protein kinase (p38MAPK) in this signaling pathway in cultured human vascular smooth muscle cells (VSMCs). Methods: The present in vitro study was performed on human VSMCs. Proteins were detected by western blotting utilizing an anti-phospho-Smad2 (Ser245/250/255) rabbit polyclonal antibody and a horseradish peroxidase-labeled secondary antibody. Glyceraldehyde-3-phosphate dehydrogenase was used as a loading control. The phospho-Smad2 linker region (pSmad2L) was detected in all the experimental groups: a control group (untreated group), a group treated with TGF-β (2 ng/mL), and a group treated with TGF-β plus different inhibitors. The data were normalized and presented as mean±SEM. The statistical analyses were performed using SPSS, version 16.0, and the nonparametric Kruskal-Wallis test. A P value smaller than 0.05 was considered statistically significant. Results: The VSMCs treated with TGF-β (2 ng/mL) showed a time-dependent increase in the pSmad2L level. The highest level was observed at 15 minutes (P=0.03). The inhibitors of NAD(P)H oxidases (diphenyleneiodonium and apocynin) (P=0.04), ROS scavenger (N-acetylcysteine) (P=0.04), and p38MAPK inhibitor (SB-202190) (P=0.04) were able to reduce the increased level of the pSmad2L by TGF-β. Conclusion: Our results suggested that NAD(P)H oxidases played an important role in the Smad2L phosphorylation in the human VSMCs. Furthermore, our results confirmed that ROS and p38MAPK were involved in this signaling pathway. Thus, TGF-β via a ROS-dependent mechanism can transmit its signals to the pSmad2L.
Language	English
Publishing date	2018-05-29
Publishing country	Iran
Document type	Journal Article
ZDB-ID	603872-4
ISSN	1735-3688 ; 0253-0716
ISSN (online)	1735-3688
ISSN	0253-0716
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Article: Transforming growth factor-β1 mediated CHST11 and CHSY1 mRNA expression is ROS dependent in vascular smooth muscle cells.

Mohamed, Raafat / Dayati, Parisa / Mehr, Reyhaneh Niayesh / Kamato, Danielle / Seif, Faezeh / Babaahmadi-Rezaei, Hossein / Little, Peter J

Journal of cell communication and signaling

2018 Volume 13, Issue 2, Page(s) 225–233

Abstract: Transforming growth factor (TGF)-β1 mediates glycosaminoglycan (GAG) chain hyperelongation on secreted proteoglycans and these modifications are associated with increased lipid binding in the vessel wall and the development of atherosclerosis. In ... ...

Abstract	Transforming growth factor (TGF)-β1 mediates glycosaminoglycan (GAG) chain hyperelongation on secreted proteoglycans and these modifications are associated with increased lipid binding in the vessel wall and the development of atherosclerosis. In vascular smooth muscle cells (VSMCs), TGF-β1 regulated GAG elongation via extracellular signal-regulated kinase (ERK) and p38 as well as Smad2 linker region phosphorylation. In this study, our aim was to identify the TGF-β1 mediated signalling pathway involving reactive oxygen species (ROS) and Smad2 linker region phosphorylation that regulate the mRNA expression of GAG synthesizing enzymes, chondroitin 4-O-sulfotransferase 1 (CHST11) and chondroitin sulfate synthase 1 (CHSY1) which are the rate limiting enzymes involved in GAG chain elongation. Signalling molecules were assessed by western blotting, quantitative real-time PCR was used for analysis of gene expression and intracellular ROS level was measured by a fluorescence based assay. TGF-β1 induced ROS production in VSMCs. Nicotinamide adenine dinucleotide phosphate oxidase (Nox) inhibitors, diphenyleneiodonium (DPI) and apocynin blocked TGF-β1 mediated Smad2 linker region phosphorylation. TGF-β1 treatment increased the mRNA levels of CHST11 and CHSY1. Pharmacological inhibition of Nox blocked TGF-β1 mediated mitogen activated protein kinases (MAPKs) phosphorylation and TGF-β1 stimulated CHST11 and CHSY1 mRNA expression. These findings demonstrated that TGF-β1 mediated expression of CHST11 and CHSY1 can occur via Nox-dependent pathways and Smad2 linker region phosphorylation.
Language	English
Publishing date	2018-11-11
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2299380-0
ISSN	1873-961X ; 1873-9601
ISSN (online)	1873-961X
ISSN	1873-9601
DOI	10.1007/s12079-018-0495-x
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