Please use this identifier to cite or link to this item:
Title: Loss of Parkin impairs mitochondrial function and leads to muscle atrophy
Authors: Peker, Nesibe
Donipadi, Vinay
Sharma, Mridula
McFarlane, Craig
Kambadur, Ravi
Keywords: Science::Biological sciences
Issue Date: 2018
Source: Peker, N., Donipadi, V., Sharma, M., McFarlane, C., & Kambadur, R. (2018). Loss of Parkin impairs mitochondrial function and leads to muscle atrophy. American Journal of Physiology - Cell Physiology, 315(2), C164-C185. doi:10.1152/ajpcell.00064.2017
Journal: American Journal of Physiology - Cell Physiology
Abstract: Parkinson's disease is a neurodegenerative disease characterized by tremors, muscle stiffness, and muscle weakness. Molecular genetic analysis has confirmed that mutations in PARKIN and PINK1 genes, which play major roles in mitochondrial quality control and mitophagy, are frequently associated with Parkinson's disease. PARKIN is an E3 ubiquitin ligase that translocates to mitochondria during loss of mitochondrial membrane potential to increase mitophagy. Although muscle dysfunction is noted in Parkinson's disease, little is known about the involvement of PARKIN in the muscle phenotype of Parkinson's disease. In this study, we report that the mitochondrial uncoupler CCCP promotes PINK1/PARKIN-mediated mitophagy in myogenic C2C12 cells. As a result of this excess mitophagy, we show that CCCP treatment of myotubes leads to the development of myotube atrophy in vitro. Surprisingly, we also found that siRNA-mediated knockdown of Parkin results in impaired mitochondrial turnover. In addition, knockdown of Parkin led to myotubular atrophy in vitro. Consistent with these in vitro results, Parkin knockout muscles showed impaired mitochondrial function and smaller myofiber area, suggesting that Parkin function is required for post-natal skeletal muscle growth and development.
ISSN: 0363-6143
DOI: 10.1152/ajpcell.00064.2017
Schools: School of Biological Sciences 
Rights: © 2018 The American Physiological Society. All rights reserved. This paper was published in American Journal of Physiology - Cell Physiology and is made available with permission of The American Physiological Society.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

Files in This Item:
File Description SizeFormat 
Nesibe Peker 104970_2_merged_1521219388 (1) 0.pdf963.3 kBAdobe PDFThumbnail

Citations 10

Updated on Feb 17, 2024

Web of ScienceTM
Citations 10

Updated on Oct 27, 2023

Page view(s)

Updated on Feb 20, 2024

Download(s) 50

Updated on Feb 20, 2024

Google ScholarTM




Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.