Next Article in Journal
Inflammation during Percutaneous Coronary Intervention—Prognostic Value, Mechanisms and Therapeutic Targets
Previous Article in Journal
Asthmatic Eosinophils Promote Contractility and Migration of Airway Smooth Muscle Cells and Pulmonary Fibroblasts In Vitro
Previous Article in Special Issue
New Insights into the Significance of PARP-1 Activation: Flow Cytometric Detection of Poly(ADP-Ribose) as a Marker of Bovine Intramammary Infection
Article

Silencing of Poly(ADP-Ribose) Polymerase-2 Induces Mitochondrial Reactive Species Production and Mitochondrial Fragmentation

1
Department of Medical Chemistry, Faculty of Medicine, University of Debrecen, H-4032 Debrecen, Hungary
2
Department of Biochemistry and Molecular Biology, Faculty of Medicine, University of Debrecen, H-4032 Debrecen, Hungary
3
Department of Anatomy, Histology and Embryology, Faculty of Medicine, University of Debrecen, H-4032 Debrecen, Hungary
4
Biological Research Center of the Hungarian Academy of Sciences, H-6726 Szeged, Hungary
5
MTA-DE Neuroscience Research Group, H-4032 Debrecen, Hungary
6
MTA-DE Lendület Laboratory of Cellular Metabolism, H-4032 Debrecen, Hungary
7
Research Center for Molecular Medicine, Faculty of Medicine, University of Debrecen, H-4032 Debrecen, Hungary
*
Author to whom correspondence should be addressed.
Academic Editors: Ted M. Dawson and Oleh Khalimonchuk
Cells 2021, 10(6), 1387; https://doi.org/10.3390/cells10061387
Received: 23 January 2021 / Revised: 18 May 2021 / Accepted: 2 June 2021 / Published: 4 June 2021
(This article belongs to the Special Issue Molecular Role of PARP in Health and Disease 2020)
PARP2 is a DNA repair protein. The deletion of PARP2 induces mitochondrial biogenesis and mitochondrial activity by increasing NAD+ levels and inducing SIRT1 activity. We show that the silencing of PARP2 causes mitochondrial fragmentation in myoblasts. We assessed multiple pathways that can lead to mitochondrial fragmentation and ruled out the involvement of mitophagy, the fusion–fission machinery, SIRT1, and mitochondrial unfolded protein response. Nevertheless, mitochondrial fragmentation was reversed by treatment with strong reductants, such as reduced glutathione (GSH), N-acetyl-cysteine (NAC), and a mitochondria-specific antioxidant MitoTEMPO. The effect of MitoTEMPO on mitochondrial morphology indicates the production of reactive oxygen species of mitochondrial origin. Elimination of reactive oxygen species reversed mitochondrial fragmentation in PARP2-silenced cells. View Full-Text
Keywords: PARP2; ARTD2; oxidative stress; mitochondrial biogenesis; skeletal muscle; mitochondrial fragmentation; mitochondrial morphology PARP2; ARTD2; oxidative stress; mitochondrial biogenesis; skeletal muscle; mitochondrial fragmentation; mitochondrial morphology
Show Figures

Figure 1

MDPI and ACS Style

Jankó, L.; Kovács, T.; Laczik, M.; Sári, Z.; Ujlaki, G.; Kis, G.; Horváth, I.; Antal, M.; Vígh, L.; Bálint, B.L.; Uray, K.; Bai, P. Silencing of Poly(ADP-Ribose) Polymerase-2 Induces Mitochondrial Reactive Species Production and Mitochondrial Fragmentation. Cells 2021, 10, 1387. https://doi.org/10.3390/cells10061387

AMA Style

Jankó L, Kovács T, Laczik M, Sári Z, Ujlaki G, Kis G, Horváth I, Antal M, Vígh L, Bálint BL, Uray K, Bai P. Silencing of Poly(ADP-Ribose) Polymerase-2 Induces Mitochondrial Reactive Species Production and Mitochondrial Fragmentation. Cells. 2021; 10(6):1387. https://doi.org/10.3390/cells10061387

Chicago/Turabian Style

Jankó, Laura, Tünde Kovács, Miklós Laczik, Zsanett Sári, Gyula Ujlaki, Gréta Kis, Ibolya Horváth, Miklós Antal, László Vígh, Bálint L. Bálint, Karen Uray, and Péter Bai. 2021. "Silencing of Poly(ADP-Ribose) Polymerase-2 Induces Mitochondrial Reactive Species Production and Mitochondrial Fragmentation" Cells 10, no. 6: 1387. https://doi.org/10.3390/cells10061387

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop