ArticleMolecular neurodegeneration2015
Heteromers of amyloid precursor protein in cerebrospinal fluid.
Article in Molecular neurodegeneration, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 27 citations in OpenAlex.
- Selective reduction of ADAM10 in brain and cerebrospinal fluid of Alzheimer's disease patients.Alzheimer's research & therapy · 2026Article
- Alterations of NMDAR Subunits in the Cerebrospinal Fluid Across Neurodegenerative and Immunological Disorders.Journal of neurochemistry · 2025Article
- Soluble APP-α and APP-β in cerebrospinal fluid as potential biomarkers for differential diagnosis of mild cognitive impairment.Aging clinical and experimental research · 2022Article
- α-Secretase nonsense mutation (ADAM10 Tyr167*) in familial Alzheimer's disease.Alzheimer's research & therapy · 2020Article
- Amyloid precursor protein glycosylation is altered in the brain of patients with Alzheimer's disease.Alzheimer's research & therapy · 2020Article
- CSF sAPPα and sAPPβ levels in Alzheimer's Disease and Multiple Other Neurodegenerative Diseases: A Network Meta-Analysis.Neuromolecular medicine · 2020Article
- Plasma biomarkers of the amyloid pathway are associated with geographic atrophy secondary to age-related macular degeneration.PloS one · 2020Article
- Characterization of Cerebrospinal Fluid BACE1 Species.Molecular neurobiology · 2019Article
- Human cerebrospinal fluid 6E10-immunoreactive protein species contain amyloid precursor protein fragments.PloS one · 2019Article
- Levels of ADAM10 are reduced in Alzheimer's disease CSF.Journal of neuroinflammation · 2018Article
- APLP1 is endoproteolytically cleaved by γ-secretase without previous ectodomain shedding.Scientific reports · 2018Article
- C-terminal fragments of the amyloid precursor protein in cerebrospinal fluid as potential biomarkers for Alzheimer disease.Scientific reports · 2017Article
- Restoring Soluble Amyloid Precursor Protein α Functions as a Potential Treatment for Alzheimer's Disease.Journal of neuroscience research · 2017Review
- Reduced neurotrophic factor level is the early event before the functional neuronal deficiency in high-fat diet induced obese mice.Metabolic brain disease · 2017Article
- The role of exosomes in the pathogenesis of Alzheimer' disease.Translational neurodegeneration · 2017Review
- Transmembrane Amyloid-Related Proteins in CSF as Potential Biomarkers for Alzheimer's Disease.Frontiers in neurology · 2015Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundSoluble fragments of the amyloid precursor protein (APP) generated by α- and β-secretases, sAPPα and sAPPβ, have been postulated as promising new cerebrospinal fluid (CSF) biomarkers for the clinical diagnosis of Alzheimer's disease (AD). However, the capacity of these soluble proteins to assemble has not been explored and could be relevant. Our aim is to characterize possible sAPP oligomers that could contribute to the quantification of sAPPα and sAPPβ in CSF by ELISA, as well as to characterize the possible presence of soluble full-length APP (sAPPf).
resultsWe employed co-immunoprecipitation, native polyacrylamide gel electrophoresis and ultracentrifugation in sucrose density gradients to characterize sAPP oligomers in CSF. We have characterized the presence of sAPPf in CSF from NDC and AD subjects and demonstrated that all forms, including sAPPα and sAPPβ, are capable of assembling into heteromers, which differ from brain APP membrane-dimers. We measured sAPPf, sAPPα and sAPPβ by ELISA in CSF samples from AD (n = 13) and non-disease subjects (NDC, n = 13) before and after immunoprecipitation with antibodies against the C-terminal APP or against sAPPβ. We demonstrated that these sAPP heteromers participate in the quantification of sAPPα and sAPPβ by ELISA. Immunoprecipitation with a C-terminal antibody to remove sAPPf reduced by ~30% the determinations of sAPPα and sAPPβ by ELISA, whereas immunoprecipitation with an APPβ antibody reduced by ~80% the determination of sAPPf and sAPPα.
conclusionsThe presence of sAPPf and sAPP heteromers should be taken into consideration when exploring the levels of sAPPα and sAPPβ as potential CSF biomarkers.
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