scholarly journals Quantitative Measurement of Intact Alpha-Synuclein Proteoforms from Post-Mortem Control and Parkinson's Disease Brain Tissue by Intact Protein Mass Spectrometry

2014 ◽  
Vol 4 (1) ◽  
Author(s):  
John F. Kellie ◽  
Richard E. Higgs ◽  
John W. Ryder ◽  
Anthony Major ◽  
Thomas G. Beach ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Parkinson’S Disease ◽  
Parkinson's Disease ◽  
Brain Tissue ◽  
Quantitative Measurement ◽  
Alpha Synuclein ◽  
Intact Protein ◽  
Post Mortem ◽  
Protein Mass ◽  
Protein Mass Spectrometry

Organochlorine compounds in human brain

1996 ◽  
Vol 15 (3) ◽  
pp. 262-264 ◽  
Author(s):  
FM Corrigan ◽  
M. French ◽  
L. Murray
Keyword(s):  
Parkinson’S Disease ◽  
Parkinson's Disease ◽  
Basal Ganglia ◽  
Polychlorinated Biphenyls ◽  
Human Brain ◽  
Frontal Cortex ◽  
Brain Tissue ◽  
Organochlorine Compounds ◽  
Post Mortem ◽  
Lipid Weight

Having observed polychlorinated biphenyls (PCBs) in brain tissue obtained post mortem from two men we have carried out a study of organochlorine compounds in frontal cortex from patients with Parkinson's disease (PD) and from controls. No PCBs were found in any of those samples. There was no difference in the concentra tion of the DDT metabolite pp'-DDE in the PD brain samples. Dieldrin (HEOD) was significantly decreased in PD brain when analysed by lipid weight. While these findings would not support the hypothesis that PCBs may contribute to the development of Parkinson's disease in humans it remains possible that they may cause damage to the basal ganglia before being displaced from brain tissue.

scholarly journals Intact protein mass spectrometry reveals intraspecies variations in venom composition of a local population of Vipera kaznakovi in Northeastern Turkey

2019 ◽  
Vol 199 ◽  
pp. 31-50 ◽  
Author(s):  
Daniel Petras ◽  
Benjamin-Florian Hempel ◽  
Bayram Göçmen ◽  
Mert Karis ◽  
Gareth Whiteley ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Local Population ◽  
Intact Protein ◽  
Protein Mass ◽  
Protein Mass Spectrometry ◽  
Venom Composition

scholarly journals The subcellular arrangement of alpha-synuclein proteoforms in the Parkinson’s disease brain as revealed by multicolor STED microscopy

2021 ◽  
Author(s):  
Tim E. Moors ◽  
Christina A. Maat ◽  
Daniel Niedieker ◽  
Daniel Mona ◽  
Dennis Petersen ◽  
...  
Keyword(s):  
Parkinson’S Disease ◽  
Parkinson's Disease ◽  
High Resolution ◽  
Physiological Role ◽  
Alpha Synuclein ◽  
Stimulated Emission ◽  
Disease Stage ◽  
Post Mortem ◽  
Label Free ◽  
Sted Microscopy

AbstractVarious post-translationally modified (PTM) proteoforms of alpha-synuclein (aSyn)—including C-terminally truncated (CTT) and Serine 129 phosphorylated (Ser129-p) aSyn—accumulate in Lewy bodies (LBs) in different regions of the Parkinson’s disease (PD) brain. Insight into the distribution of these proteoforms within LBs and subcellular compartments may aid in understanding the orchestration of Lewy pathology in PD. We applied epitope-specific antibodies against CTT and Ser129-p aSyn proteoforms and different aSyn domains in immunohistochemical multiple labelings on post-mortem brain tissue from PD patients and non-neurological, aged controls, which were scanned using high-resolution 3D multicolor confocal and stimulated emission depletion (STED) microscopy. Our multiple labeling setup highlighted a consistent onion skin-type 3D architecture in mature nigral LBs in which an intricate and structured-appearing framework of Ser129-p aSyn and cytoskeletal elements encapsulates a core enriched in CTT aSyn species. By label-free CARS microscopy we found that enrichments of proteins and lipids were mainly localized to the central portion of nigral aSyn-immunopositive (aSyn+) inclusions. Outside LBs, we observed that 122CTT aSyn+ punctae localized at mitochondrial membranes in the cytoplasm of neurons in PD and control brains, suggesting a physiological role for 122CTT aSyn outside of LBs. In contrast, very limited to no Ser129-p aSyn immunoreactivity was observed in brains of non-neurological controls, while the alignment of Ser129-p aSyn in a neuronal cytoplasmic network was characteristic for brains with (incidental) LB disease. Interestingly, Ser129-p aSyn+ network profiles were not only observed in neurons containing LBs but also in neurons without LBs particularly in donors at early disease stage, pointing towards a possible subcellular pathological phenotype preceding LB formation. Together, our high-resolution and 3D multicolor microscopy observations in the post-mortem human brain provide insights into potential mechanisms underlying a regulated LB morphogenesis.

Intact Protein Mass Spectrometry of Cell Culture Harvest Guides Cell Line Development for Trispecific Antibodies

2020 ◽  
Vol 92 (3) ◽  
pp. 2764-2769
Author(s):  
Fateme Tousi ◽  
Yan Jiang ◽  
Sharmila Sivendran ◽  
Yvonne Song ◽  
Susan Elliott ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Cell Culture ◽  
Cell Line ◽  
Intact Protein ◽  
Cell Line Development ◽  
Protein Mass ◽  
Protein Mass Spectrometry
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