ArticleACS chemical neuroscience2022
Dysregulation of Neuropeptide and Tau Peptide Signatures in Human Alzheimer's Disease Brain.
Article in ACS chemical neuroscience, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.
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Who cites it
21 citing papers in PubMed, 1 synthesis or guideline pooled it, 37 citations in OpenAlex.
- Biomarkers in Ataxia-Telangiectasia: a Systematic Review.Journal of neurology · 2025Pooled it
- Proteomic maps of synapses and synaptic vesicles across the central and enteric nervous systems.Communications biology · 2026Article
- Degradation graphs reveal hidden proteolytic activity in peptidomes.PLoS computational biology · 2026Article
- Patient-derived induced pluripotent stem cells with a C9orf72 expansion as a model to study frontotemporal dementia pathologies.Molecular biology of the cell · 2025Article
- The Role of Sirt1 in Regulating Inflammatory Cytokines and Oxidative Stress in the Transition Mechanism from Depressive Disorder to Alzheimer's Disease.Molecular neurobiology · 2025Article
- Decoding Neuropeptide Complexity: Advancing Neurobiological Insights from Invertebrates to Vertebrates through Evolutionary Perspectives.ACS chemical neuroscience · 2025Review
- Computational approaches for identifying neuropeptides: A comprehensive review.Molecular therapy. Nucleic acids · 2025Review
- Regulation of granin neuropeptide gene expression in human brain during development.Frontiers in molecular neuroscience · 2025Article
- Long Neuro-COVID-19: Current Mechanistic Views and Therapeutic Perspectives.Biomolecules · 2024Review
- MotifQuest: An Automated Pipeline for Motif Database Creation to Improve Peptidomics Database Searching Programs.Journal of the American Society for Mass Spectrometry · 2024Article
- Single-Cell Patch-Clamp/Proteomics of Human Alzheimer's Disease iPSC-Derived Excitatory Neurons Versus Isogenic Wild-Type Controls Suggests Novel Causation and Therapeutic Targets.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Human iN neuronal model of schizophrenia displays dysregulation of chromogranin B and related neuropeptide transmitter signatures.Molecular psychiatry · 2024Article
- Precision proteoform design for 4R tau isoform selective templated aggregation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Precision Proteoform Design for 4R Tau Isoform Selective Templated Aggregation.bioRxiv : the preprint server for biology · 2023Article
- Identifying and Measuring Endogenous Peptides through Peptidomics.ACS chemical neuroscience · 2023Article
- Brain Hydrophobic Peptides Antagonists of Neurotoxic Amyloid β Peptide Monomers/Oligomers-Protein Interactions.International journal of molecular sciences · 2023Review
- Definitive Screening Designs to Optimize Library-Free DIA-MS Identification and Quantification of Neuropeptides.Journal of proteome research · 2023Article
- Peptidomics.Nature reviews. Methods primers · 2023Article
- Evaluation of bumetanide as a potential therapeutic agent for Alzheimer's disease.Frontiers in pharmacology · 2023Review
- Review
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Synaptic dysfunction and loss occur in Alzheimer's disease (AD) brains, which results in cognitive deficits and brain neurodegeneration. Neuropeptides comprise the major group of synaptic neurotransmitters in the nervous system. This study evaluated neuropeptide signatures that are hypothesized to differ in human AD brain compared to age-matched controls, achieved by global neuropeptidomics analysis of human brain cortex synaptosomes. Neuropeptidomics demonstrated distinct profiles of neuropeptides in AD compared to controls consisting of neuropeptides derived from chromogranin A (CHGA) and granins, VGF (nerve growth factor inducible), cholecystokinin, and others. The differential neuropeptide signatures indicated differences in proteolytic processing of their proneuropeptides. Analysis of cleavage sites showed that dibasic residues at the N-termini and C-termini of neuropeptides were the main sites for proneuropeptide processing, and data also showed that the AD group displayed differences in preferred residues adjacent to the cleavage sites. Notably, tau peptide signatures differed in the AD compared to age-matched control human brain cortex synaptosomes. Unique tau peptides were derived from the tau protein through proteolysis using similar and differential cleavage sites in the AD brain cortex compared to the control. Protease profiles differed in the AD compared to control, indicated by proteomics data. Overall, these results demonstrate that dysregulation of neuropeptides and tau peptides occurs in AD brain cortex synaptosomes compared to age-matched controls, involving differential cleavage site properties for proteolytic processing of precursor proteins. These dynamic changes in neuropeptides and tau peptide signatures may be associated with the severe cognitive deficits of AD.
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Registered trials
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