TY  - JOUR
A1  - Plum, Sarah
A1  - Eggers, Britta
A1  - Helling, Stefan
A1  - Stepath, Markus
A1  - Theiss, Carsten
A1  - Leite, Renata E. P.
A1  - Molina, Mariana
A1  - Grinberg, Lea T.
A1  - Riederer, Peter
A1  - Gerlach, Manfred
A1  - May, Caroline
A1  - Marcus, Katrin
T1  - Proteomic characterization of synaptosomes from human substantia nigra indicates altered mitochondrial translation in Parkinson's disease
JF  - Cells
N2  - The pathological hallmark of Parkinson's disease (PD) is the loss of neuromelanin-containing dopaminergic neurons within the substantia nigra pars compacta (SNpc). Additionally, numerous studies indicate an altered synaptic function during disease progression. To gain new insights into the molecular processes underlying the alteration of synaptic function in PD, a proteomic study was performed. Therefore, synaptosomes were isolated by density gradient centrifugation from SNpc tissue of individuals at advanced PD stages (N = 5) as well as control subjects free of pathology (N = 5) followed by mass spectrometry-based analysis. In total, 362 proteins were identified and assigned to the synaptosomal core proteome. This core proteome comprised all proteins expressed within the synapses without regard to data analysis software, gender, age, or disease. The differential analysis between control subjects and PD cases revealed that CD9 antigen was overrepresented and fourteen proteins, among them Thymidine kinase 2 (TK2), mitochondrial, 39S ribosomal protein L37, neurolysin, and Methionine-tRNA ligase (MARS2) were underrepresented in PD suggesting an alteration in mitochondrial translation within synaptosomes.
KW  - synaptosomes
KW  - proteomics
KW  - Parkinson's disease
KW  - substantia nigra pars compacta
KW  - mitochondrial pathology
KW  - mitochondrial translation
Y1  - 2020
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-219978
SN  - 2073-4409
VL  - 9
IS  - 12
ER  -