Proteomic and functional data sets on synaptic mitochondria from rats with genetic ablation of Parkin

Abstract

In this paper, we provide proteomic and functional data for synaptic mitochondria from the striatum of rats with Parkin ablation. The quantitative proteomic data was obtained using SWATH-MS methodology and mitochondrial function was assessed through measurement of oxygen consumption rate using the Seahorse XF Analyzer. This data facilitates comparisons with previous proteomic and functional data obtained using the exact same methods. A complete set of proteomic data is contained in Supplementary Table 1.

Mitochondrial DNA Instability Supersedes Parkin Mutations in Driving Mitochondrial Proteomic Alterations and Functional Deficits in Polg Mutator Mice

“…Though ventricular mitochondria were not significantly impaired by loss of mtDNA fidelity, loss of Parkin improved electron flow efficiency beyond WT levels. Traditionally, loss of Parkin is thought to promote increased mitochondrial dysfunction [39,41,68]; however, numerous recent reports, including our study, contest this [36,42,[69][70][71]. Previously, our lab reported rats lacking Parkin do not exhibit functional deficits in striatal synaptic mitochondria [72].…”

“…Previously, our lab reported rats lacking Parkin do not exhibit functional deficits in striatal synaptic mitochondria [ 72 ]. Additionally, in a recent preprint, Filograna et al report that genetic ablation of Parkin did not impair activity of oxidative phosphorylation enzymes in mitochondria isolated from brain, heart, or skeletal muscle [ 71 ]. Interestingly, though not reaching significance, Complex I and Complex I/Complex III activity was modestly elevated in heart mitochondria of Parkin-null mice compared to WT.…”

“…Interestingly, though not reaching significance, Complex I and Complex I/Complex III activity was modestly elevated in heart mitochondria of Parkin-null mice compared to WT. Moreover, ATP production of Parkin-null PD patient-derived skeletal muscle mitochondria was modestly increased when stimulated with substrates specific to Complex I + II (glucose and succinate) or Complex IV (ascorbate/TMPD) [ 71 ]. Scott et al similarly reported no significant differences in the activity of Complex I or Complex IV of Parkin-null mice [ 42 ].…”

“…Scott et al similarly reported no significant differences in the activity of Complex I or Complex IV of Parkin-null mice [ 42 ]. Notably, both studies also investigated the effects of Parkin insufficiency in the Polg mutator mouse, concluding that loss of Parkin did not exacerbate the Polg phenotype [ 42 , 71 ]. Despite this evidence, the possibility does exist that the bioenergetic rescue effect we observed may be the result of Parkin-independent effects.…”