Research Paper Volume 11, Issue 11 pp 3750—3767
Mitochondrial and autophagic alterations in skin fibroblasts from Parkinson disease patients with Parkin mutations
- 1 Laboratory of Muscle Research and Mitochondrial Function, Institut d’Investigacions Biomèdiques August Pi i Sunyer (IDIBAPS), University of Barcelona (UB), Department of Internal Medicine, Hospital Clínic of Barcelona (HCB), Barcelona 08036, Spain
- 2 Centro de Investigación Biomédica en Red (CIBER) de Enfermedades Raras (CIBERER), Madrid 28029, Spain
- 3 Laboratory of Neurodegenerative Disorders, IDIBAPS, UB, Department of Neurology, HCB, Barcelona 08036, Spain
- 4 CIBER de Enfermedades Neurodegenerativas (CIBERNED), Madrid 28031, Spain
- 5 Cell Death and Proliferation, IDIBAPS, Consejo Superior Investigaciones Científicas (CSIC), Barcelona, Spain
- 6 Liver Unit, HCB, IDIBAPS and CIBER de Enfermedades Hepáticas y Digestivas (CIBEREHD), Barcelona, Spain
- 7 USC Research Center for ALPD, Keck School of Medicine, Los Angeles, CA 90033, USA
Received: April 1, 2019 Accepted: June 1, 2019 Published: June 9, 2019
https://doi.org/10.18632/aging.102014How to Cite
Copyright: González-Casacuberta et al. This is an open‐access article distributed under the terms of the Creative Commons Attribution License (CC BY 3.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Abstract
PRKN encodes an E3-ubiquitin-ligase involved in multiple cell processes including mitochondrial homeostasis and autophagy. Previous studies reported alterations of mitochondrial function in fibroblasts from patients with PRKN mutation-associated Parkinson’s disease (PRKN-PD) but have been only conducted in glycolytic conditions, potentially masking mitochondrial alterations. Additionally, autophagy flux studies in this cell model are missing.
We analyzed mitochondrial function and autophagy in PRKN-PD skin-fibroblasts (n=7) and controls (n=13) in standard (glucose) and mitochondrial-challenging (galactose) conditions.
In glucose, PRKN-PD fibroblasts showed preserved mitochondrial bioenergetics with trends to abnormally enhanced mitochondrial respiration that, accompanied by decreased CI, may account for the increased oxidative stress. In galactose, PRKN-PD fibroblasts exhibited decreased basal/maximal respiration vs. controls and reduced mitochondrial CIV and oxidative stress compared to glucose, suggesting an inefficient mitochondrial oxidative capacity to meet an extra metabolic requirement. PRKN-PD fibroblasts presented decreased autophagic flux with reduction of autophagy substrate and autophagosome synthesis in both conditions.
The alterations exhibited under neuron-like oxidative environment (galactose), may be relevant to the disease pathogenesis potentially explaining the increased susceptibility of dopaminergic neurons to undergo degeneration. Abnormal PRKN-PD phenotype supports the usefulness of fibroblasts to model disease and the view of PD as a systemic disease where molecular alterations are present in peripheral tissues.