ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience1997
Late compartments of amyloid precursor protein transport in SY5Y cells are involved in beta-amyloid secretion.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 70 citations in OpenAlex.
- lncRNAs: key player in Aβ deposition.RNA biology · 2026Review
- Amyloid-β with isomerized Asp7 cytotoxicity is coupled to protein phosphorylation.Scientific reports · 2018Article
- Collapsin Response Mediator Protein-2 (CRMP2) is a Plausible Etiological Factor and Potential Therapeutic Target in Alzheimer's Disease: Comparison and Contrast with Microtubule-Associated Protein Tau.Journal of Alzheimer's disease : JAD · 2016Review
- Sequential proteolytic processing of the triggering receptor expressed on myeloid cells-2 (TREM2) protein by ectodomain shedding and γ-secretase-dependent intramembranous cleavage.The Journal of biological chemistry · 2013Article
- An intronic ncRNA-dependent regulation of SORL1 expression affecting Aβ formation is upregulated in post-mortem Alzheimer's disease brain samples.Disease models & mechanisms · 2013Article
- Cell surface binding and internalization of aβ modulated by degree of aggregation.International journal of Alzheimer's disease · 2011Article
- Article
- Eicosapentaenoic acid (EPA) increases cell viability and expression of neurotrophin receptors in retinoic acid and brain-derived neurotrophic factor differentiated SH-SY5Y cells.European journal of nutrition · 2008Article
- Requirement of aggregation propensity of Alzheimer amyloid peptides for neuronal cell surface binding.BMC neuroscience · 2007Article
- Neuronal sorting protein-related receptor sorLA/LR11 regulates processing of the amyloid precursor protein.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Processing of Notch and amyloid precursor protein by gamma-secretase is spatially distinct.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- The discrepancy between presenilin subcellular localization and gamma-secretase processing of amyloid precursor protein.The Journal of cell biology · 2001Article
- The endosomal-lysosomal system of neurons in Alzheimer's disease pathogenesis: a review.Neurochemical research · 2000Review
- Endocytic pathway abnormalities precede amyloid beta deposition in sporadic Alzheimer's disease and Down syndrome: differential effects of APOE genotype and presenilin mutations.The American journal of pathology · 2000Article
- Copper inhibits beta-amyloid production and stimulates the non-amyloidogenic pathway of amyloid-precursor-protein secretion.The Biochemical journal · 1999Article
- Presenilin 1 controls gamma-secretase processing of amyloid precursor protein in pre-golgi compartments of hippocampal neurons.The Journal of cell biology · 1999Article
- Pulse-chase experiments revealed beta-secretase cleavage from immature full-length amyloid precursor protein harboring the Swedish mutation. Implications for distinct pathways.Journal of molecular neuroscience : MN · 1998Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloid plaques, composed mainly of the 39-43 amino acid betaA4 peptide, are a characteristic feature of Alzheimer's disease. Generation of betaA4 by proteolytic processing of the amyloid precursor protein (APP) is thought to occur in a pathway that includes the activity of two as yet unknown proteases, with beta-secretase cleaving at the N terminus and gamma-secretase releasing the C terminus of betaA4. Inhibition studies and the finding that cell surface APP can serve as a direct precursor of betaA4 suggest that the endosomal/lysosomal compartment is involved in the proteolysis of APP into betaA4. In this study we targeted APP695 chimeric proteins directly into the endosomal/lysosomal compartment. This decreased the amount of released betaA4, while the generation of the betaA4 N terminus continued. APP695 proteins were constructed also, which carried sorting signals responsible for recycling between the trans-Golgi network (TGN) and the cell surface. These proteins were processed into secreted betaA4 at even higher levels than wild-type APP695. Moreover, retention of APP695 proteins in the endoplasmic reticulum led to neither betaA4 secretion nor to processing by beta-secretase in human SH-SY5Y neuroblastoma cells. These data suggest that a beta-cleavage activity resides in a late endosomal compartment and that a gamma-cleavage occurs in early endosomes, resulting in the generation of betaA4 peptides with the majority ending at residue 40.
Indexed as
Identifiers
9315893PMC6793894W1902701859What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.