ArticleMolecular neurodegeneration2018
Alzheimer-associated cerebrospinal fluid fragments of neurogranin are generated by Calpain-1 and prolyl endopeptidase.
Article in Molecular neurodegeneration, 2018. 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, 32 citations in OpenAlex.
- Calpain Inhibitors as Potential Therapeutic Modulators in Neurodegenerative Diseases.Neurochemical research · 2022Pooled it
- Altered synaptic and astrocytic proteins in Lewy body disorders associated withBrain communications · 2026Article
- The Cooperation of Neurogranin with Calmodulin Promotes the Treatment of Aging-Related Diseases via Regular Exercise.Molecular neurobiology · 2025Review
- Early- and Late-Onset Alzheimer's Disease: Two Sides of the Same Coin?Diseases (Basel, Switzerland) · 2024Review
- Novel ultrasensitive immunoassay for the selective quantification of tau oligomers and related soluble aggregates.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2024Article
- Alzheimer's Disease Biomarker Analysis Using Targeted Mass Spectrometry.Molecular & cellular proteomics : MCP · 2024Review
- Advanced Overview of Biomarkers and Techniques for Early Diagnosis of Alzheimer's Disease.Cellular and molecular neurobiology · 2023Review
- Subtle Differences in Cognition in 70-Year-Olds with Elevated Cerebrospinal Fluid Neurofilament Light and Neurogranin: A H70 Cross-Sectional Study.Journal of Alzheimer's disease : JAD · 2023Article
- Pathological (Dis)Similarities in Neuronal Exosome-Derived Synaptic and Organellar Marker Levels Between Alzheimer's Disease and Frontotemporal Dementia.Journal of Alzheimer's disease : JAD · 2023Article
- Increased Expression of Prolyl Endopeptidase Induced by Oxidative Stress in Nucleus Pulposus Cells Aggravates Intervertebral Disc Degeneration.Oxidative medicine and cellular longevity · 2022Article
- Profiling Basal Forebrain Cholinergic Neurons Reveals a Molecular Basis for Vulnerability Within the Ts65Dn Model of Down Syndrome and Alzheimer's Disease.Molecular neurobiology · 2021Article
- Molecular forms of neurogranin in cerebrospinal fluid.Journal of neurochemistry · 2021Article
- Full-length and C-terminal neurogranin in Alzheimer's disease cerebrospinal fluid analyzed by novel ultrasensitive immunoassays.Alzheimer's research & therapy · 2020Article
- Body Fluid Biomarkers for Alzheimer's Disease-An Up-To-Date Overview.Biomedicines · 2020Review
- Article
- Cerebrospinal fluid neurogranin as a new player in prion disease diagnosis and prognosis.Neural regeneration research · 2020Article
- Neurogranin: A Potential Biomarker of Neurological and Mental Diseases.Frontiers in aging neuroscience · 2020Review
- Fluid Biomarkers for Synaptic Dysfunction and Loss.Biomarker insights · 2020Review
- CSF synaptic protein concentrations are raised in those with atypical Alzheimer's disease but not frontotemporal dementia.Alzheimer's research & therapy · 2019Article
- Neurogranin Expression Is Regulated by Synaptic Activity and Promotes Synaptogenesis in Cultured Hippocampal Neurons.Molecular neurobiology · 2019Article
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Authors and funding
12 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundNeurogranin (Ng) is a small 7.6 kDa postsynaptic protein that has been detected at elevated concentrations in cerebrospinal fluid (CSF) of patients with Alzheimer's disease (AD), both as a full-length molecule and as fragments from its C-terminal half. Ng is involved in postsynaptic calcium (Ca) signal transduction and memory formation via binding to calmodulin in a Ca-dependent manner. The mechanism of Ng secretion from neurons to CSF is currently unknown, but enzymatic cleavage of Ng may be of relevance. Therefore, the aim of the study was to identify the enzymes responsible for the cleavage of Ng, yielding the Ng fragment pattern of C-terminal fragments detectable and increased in CSF of AD patients.
methodsFluorigenic quenched FRET probes containing sequences of Ng were utilized to identify Ng cleaving activities among enzymes known to have increased activity in AD and in chromatographically fractionated mouse brain extracts.
resultsHuman Calpain-1 and prolyl endopeptidase were identified as the candidate enzymes involved in the formation of endogenous Ng peptides present in CSF, cleaving mainly in the central region of Ng, and between amino acids 75_76 in the Ng sequence, respectively. The cleavage by Calpain-1 affects the IQ domain of Ng, which may deactivate or change the function of Ng in Ca
conclusionsCalpain-1 and prolyl endopeptidase cleave Ng in the IQ domain and near the C-terminus, respectively, yielding specific fragments of Ng in CSF. These fragments may give clues to the roles of increased activities of these enzymes in the pathophysiology of AD, and provide possible targets for pharmacologic intervention.
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