Quantitative proteomics of synaptosome S‐nitrosylation in Alzheimer’s disease
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Abstract Increasing evidence suggests that both synaptic loss and neuroinflammation constitute early pathologic hallmarks of Alzheimer’s disease. A downstream event during inflammatory activation of microglia and astrocytes is the induction of nitric oxide synthase type 2, resulting in an increased release of nitric oxide and the post‐translational S‐nitrosylation of protein cysteine residues. Both early events, inflammation and synaptic dysfunction, could be connected if this excess nitrosylation occurs on synaptic proteins. In the long term, such changes could provide new insight into patho‐mechanisms as well as biomarker candidates from the early stages of disease progression. This study investigated S‐nitrosylation in synaptosomal proteins isolated from APP/PS1 model mice in comparison to wild type and NOS2−/− mice, as well as human control, mild cognitive impairment and Alzheimer’s disease brain tissues. Proteomics data were obtained using an established protocol utilizing an isobaric mass tag method, followed by nanocapillary high performance liquid chromatography tandem mass spectrometry. Statistical analysis identified the S‐nitrosylation sites most likely derived from an increase in nitric oxide (NO) in dependence of presence of AD pathology, age and the key enzyme NOS2. The resulting list of candidate proteins is discussed considering function, previous findings in the context of neurodegeneration, and the potential for further validation studies. image
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Selected studies of the S-nitrosylation proteome in AD identified key proteins with altered functions associated with antioxidant, glycolysis, mitochondrial export, calcium homeostasis, synapses, apoptosis, mitochondrial dynamics, protein folding, and neuroinflammation.
“Selected studies of the S-nitrosylation proteome in AD identified key proteins with altered functions associated with antioxidant, glycolysis, mitochondrial export, calcium homeostasis, synapses, apoptosis, mitochondrial dynamics, protein folding, and neuroinflammation, among other functions [113,114,115,116].”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [115]
The Results (pp. 5, 8) identify altered S-nitrosylation of synaptic proteins in AD models and human samples, and the Discussion (pp. 10–11) links candidates to metabolism, synaptic function, and possible apoptosis. The paper does not establish altered protein functions across the full list: it does not identify glycolysis, mitochondrial export or dynamics, calcium homeostasis, or protein folding as findings of this study, and says the effects of one identified nitrosylation site remain unclear. (LLM, conf=0.87)
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Self-citationS-nitrosylation in Neuropathic pain and Autophagy
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Flagged first, then by citations
Research works printed but not linked: 1
- Mak T. and Saunders M. (2006) The Immune Response - 1st ed.
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Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease
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Systemic inflammation induced the delayed reduction of excitatory synapses in the CA3 during ageing
Manabe, T., Rácz, I., Schwartz, S., Oberle, L., Santarelli, F., Emmrich, J. V., Neher, J. J., & Heneka, M. T. (2021) · Journal of Neurochemistry · doi:10.1111/jnc.15491 · Cited by 44 · see citing works
Self-citation
- Authors
- Wijasa, T. S., Sylvester, M., Brocke‐Ahmadinejad, N., Schwartz, S., Santarelli, F., Gieselmann, V., Klockgether, T., Brosseron, F., & Heneka, M. T.
- Affiliations
- German Center for Neurodegenerative Diseases (DE)
- University of Bonn (DE)
- University Hospital Bonn (DE)
- Corresponding author
- Heneka, Michael T.
- ORCID
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 2019-10-21
- Volume
- 152
- Issue
- 6
- Pages
- 710-726
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- OpenAlex
- W2972561249
- Cited by
- 41
- References
- 108
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 8 · 2023: 7 · 2022: 7 · 2021: 9 · 2020: 4
- FWCI
- 3.42
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neurochemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Open Repository and Bibliography (University of Luxembourg) (submittedVersion, other-oa)
- DZNE Pub (submittedVersion, cc-by)
- Funders
- FP7 Health (HEALTH‐F2‐2011‐278850)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- S-nitrosylation, Alzheimer's disease, synaptosomes, nitric oxide, synaptic proteins, neuroinflammation, microglia, astrocytes, APP/PS1 mice, mild cognitive impairment, biomarkers, post-translational modification
- MeSH terms
- Aged, Aged, 80 and over, Alzheimer Disease, Animals, Brain, Disease Models, Animal, Female, Humans, Male, Mice, Inbred C57BL, Mice, Transgenic, Nerve Tissue Proteins, Nitric Oxide, Synaptosomes, Signal Transduction, Proteomics, Mice, Nitric Oxide Synthase Type II
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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