TY  - JOUR
A1  - Plum, Sarah
A1  - Steinbach, Simone
A1  - Attems, Johannes
A1  - Keers, Sharon
A1  - Riederer, Peter
A1  - Gerlach, Manfred
A1  - May, Caroline
A1  - Marcus, Katrin
T1  - Proteomic characterization of neuromelanin granules isolated from human substantia nigra by laser-microdissection
JF  - Scientific Reports
N2  - Neuromelanin is a complex polymer pigment found primarily in the dopaminergic neurons of human substantia nigra. Neuromelanin pigment is stored in granules including a protein matrix and lipid droplets. Neuromelanin granules are yet only partially characterised regarding their structure and function. To clarify the exact function of neuromelanin granules in humans, their enrichment and in-depth characterization from human substantia nigra is necessary. Previously published global proteome studies of neuromelanin granules in human substantia nigra required high tissue amounts. Due to the limited availability of human brain tissue we established a new method based on laser microdissection combined with mass spectrometry for the isolation and analysis of neuromelanin granules. With this method it is possible for the first time to isolate a sufficient amount of neuromelanin granules for global proteomics analysis from ten 10 μm tissue sections. In total 1,000 proteins were identified associated with neuromelanin granules. More than 68% of those proteins were also identified in previously performed studies. Our results confirm and further extend previously described findings, supporting the connection of neuromelanin granules to iron homeostasis and lysosomes or endosomes. Hence, this method is suitable for the donor specific enrichment and proteomic analysis of neuromelanin granules.
KW  - neuromelanin
KW  - substantia nigra
KW  - pigment
KW  - granules
Y1  - 2016
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-167507
VL  - 6
IS  - 37139
ER  - 
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  -