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Neuroprotective secreted amyloid precursor protein acts by disrupting amyloid precursor protein dimers
Gralle M, Botelho MG, Wouters FS.. The Journal of biological chemistry, 2009-03-31
Topic: Brain proteins, microglia and lab models
The amyloid precursor protein (APP) is implied both in cell growth and differentiation and in neurodegenerative processes in Alzheimer disease. Regulated proteolysis of APP generates biologically active fragments such as the neuroprotective secreted ectodomain sAPPalpha and the neurotoxic beta-amyloid peptide. Furthermore, it has been suggested that the intact transmembrane APP plays a signaling role, which might be important for both normal synaptic plasticity and neuronal dysfunction in dementia.
Key findings
- Regulated proteolysis of APP generates biologically active fragments such as the neuroprotective secreted ectodomain sAPPalpha and the neurotoxic beta-amyloid peptide.
- Furthermore, it has been suggested that the intact transmembrane APP plays a signaling role, which might be important for both normal synaptic plasticity and neuronal dysfunction in dementia.
- To understand APP signaling, we tracked single molecules of APP using quantum dots and quantitated APP homodimerization using fluorescence lifetime imaging microscopy for the detection of Förster resonance energy transfer in living neuroblastoma cells.
- Using selective labeling with synthetic fluorophores, we show that the dimerization of APP is considerably higher at the plasma membrane than in intracellular membranes.
Why it matters
This laboratory study found that the neuroprotective secreted amyloid precursor protein acts by disrupting APP dimers. It describes a mechanism of APP signalling and does not test a treatment or prevention in people.
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Study details
- Evidence strengthLow
How this study scored 43/100
Published in a peer-reviewed journal. Scored zero for study design, sample size, effect reported, studied in people and randomised / blinded because the record does not state it.
| Component | Points | Why |
|---|---|---|
| Journal tier | 7 / 10 | Tier 3 — peer-reviewed journal (The Journal of biological chemistry) |
| Journal's citation record | 4 / 4 | Journal of Biological Chemistry: journal h-index 780 (OpenAlex, 2026-10-29) |
| Study design | 0 / 12 | No study design recorded — scores zero, not guessed (not stated in the record — scored 0) |
| Strength of evidence | 1 / 5 | Rated “low” in our summary |
| Peer-review validation | 10 / 10 | Peer-reviewed. Published as an article in a named peer-reviewed journal. |
| How recent | 1 / 5 | 2009 — within 20 year(s) of the newest study here |
| Sample size | 0 / 4 | Participant count not stated — scores zero (not stated in the record — scored 0) |
| Effect reported | 0 / 3 | No effect size reported — scores zero (not stated in the record — scored 0) |
| Studied in people | 0 / 3 | Not stated whether this was studied in people — scores zero (not stated in the record — scored 0) |
| Randomised / blinded | 0 / 2 | No randomisation or blinding stated — scores zero (not stated in the record — scored 0) |
| Times cited | 5 / 7 | Cited 140 times (OpenAlex, 2026-10-10) |
| Citations per year | 2 / 5 | 7.4 citations a year over 19 year(s) since 2009 |
| Impact for its field and year | 4 / 6 | Cited 11.4× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 2 / 6 | Cited by 4 other studies in this library |
| Still being cited | 1 / 4 | Cited 4 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 2 / 4 | Last-listed author Fred Silvester Wouters: h-index 36 (OpenAlex, whole career) |
| Institution's track record | 1 / 3 | University of Göttingen: institution h-index 934 (OpenAlex) |
| Multi-centre collaboration | 1 / 3 | OpenAlex lists 2 institution(s) in 1 country |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 19336403) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Total | 43 / 100 | — |
What each of these 20 components measures, and what this score is not →
Read the original
- DOI: 10.1074/jbc.m808755200
- PubMed: 19336403
- Original source →
- Free full text: Journal of Biological Chemistry →
Full text: free to read — OpenAlex lists this copy as free to read: the link above (checked 6 Feb 1020).
Cite this study APA, Vancouver, BibTeX · download .bib or .ris
Built from the record alzhub holds for this paper, not looked up. Volume, issue and page numbers are not held in the record. Check the citation against the original before you use it.
APA 7th
Gralle, M., Botelho, M. G., & Wouters, F. S. (2009). Neuroprotective secreted amyloid precursor protein acts by disrupting amyloid precursor protein dimers. The Journal of biological chemistry. https://doi.org/10.1074/jbc.m808755200
Vancouver
Gralle M, Botelho MG, Wouters FS. Neuroprotective secreted amyloid precursor protein acts by disrupting amyloid precursor protein dimers. The Journal of biological chemistry. 2009. doi:10.1074/jbc.m808755200. PMID: 19336403.
BibTeX
@article{gralle2009-19336403,
author = {Gralle, M. and Botelho, M. G. and Wouters, F. S.},
title = {{Neuroprotective secreted amyloid precursor protein acts by disrupting amyloid precursor protein dimers}},
journal = {The Journal of biological chemistry},
year = {2009},
doi = {10.1074/jbc.m808755200},
pmid = {19336403},
url = {https://doi.org/10.1074/jbc.m808755200}
}
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Referenced by this study and also in the alzhub library, so you can read them here.
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