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Identification of the Alzheimer beta/A4 amyloid precursor protein in clathrin-coated vesicles purified from PC12 cells
Nordstedt C, Caporaso GL, Thyberg J, Gandy SE, Greengard P.. The Journal of biological chemistry, 1993-01-01
Topic: Amyloid, tau and blood-test diagnosis
The Alzheimer beta/A4 amyloid precursor protein (APP) can be proteolytically processed by at least two separate pathways in PC12 cells: chloroquine-insensitive secretory cleavage and chloroquine-sensitive intracellular degradation, presumably in the endosomal/lysosomal system. To further investigate the possibility of APP processing in the endosomal/lysosomal system, we have examined whether APP is present in clathrin-coated vesicles (CCVs), which mediate the transport of many proteins to the endosomal compartment. Using a procedure derived from established protocols for the purification of CCVs from mammalian organs, we obtained from PC12 cells highly purified CCVs that displayed the same morphological features as described for CCVs purified from other sources.
Cite this study APA, Vancouver, BibTeX · download .bib or .ris
APA 7th
Nordstedt, C., Caporaso, G. L., Thyberg, J., Gandy, S. E., & Greengard, P. (1993). Identification of the Alzheimer beta/A4 amyloid precursor protein in clathrin-coated vesicles purified from PC12 cells. The Journal of biological chemistry. https://doi.org/10.1016/s0021-9258(18)54194-6
Vancouver
Nordstedt C, Caporaso GL, Thyberg J, Gandy SE, Greengard P. Identification of the Alzheimer beta/A4 amyloid precursor protein in clathrin-coated vesicles purified from PC12 cells. The Journal of biological chemistry. 1993. doi:10.1016/s0021-9258(18)54194-6. PMID: 8416966.
BibTeX
@article{nordstedt1993-8416966,
author = {Nordstedt, C. and Caporaso, G. L. and Thyberg, J. and Gandy, S. E. and Greengard, P.},
title = {{Identification of the Alzheimer beta/A4 amyloid precursor protein in clathrin-coated vesicles purified from PC12 cells}},
journal = {The Journal of biological chemistry},
year = {1993},
doi = {10.1016/s0021-9258(18)54194-6},
pmid = {8416966},
url = {https://doi.org/10.1016/s0021-9258(18)54194-6}
}
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.
Key findings
- To further investigate the possibility of APP processing in the endosomal/lysosomal system, we have examined whether APP is present in clathrin-coated vesicles (CCVs), which mediate the transport of many proteins to the endosomal compartment.
- Using a procedure derived from established protocols for the purification of CCVs from mammalian organs, we obtained from PC12 cells highly purified CCVs that displayed the same morphological features as described for CCVs purified from other sources.
- The CCVs were enriched in full-length mature (fully post-translationally modified) forms of APP, as well as in the carboxyl-terminal APP fragment produced by the secretory cleavage pathway.
- As CCVs are known to be involved in only two intracellular pathways (trafficking from the plasma membrane to early endosomes, and from the trans-Golgi network to late endosomes/prelysosomes), these findings provide direct evidence that APP is transported to the endosomal/lysosomal system.
Why it matters
This laboratory work in PC12 cells found the amyloid precursor protein inside clathrin-coated vesicles, which carry proteins to the endosomal compartment. It is early cell-based research about how amyloid precursor protein is processed and does not show any treatment, cure or prevention for Alzheimer's disease.
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Study details
- Evidence strengthLow
How this study scored 44/100
Published in a peer-reviewed journal. Scored zero for study design, sample size, effect reported, studied in people and randomized / 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 | 1993 — older than 20 years, still counted |
| 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) |
| Randomized / blinded | 0 / 2 | No randomization or blinding stated — scores zero (not stated in the record — scored 0) |
| Times cited | 5 / 7 | Cited 209 times (OpenAlex, 2026-10-10) |
| Citations per year | 2 / 5 | 6.0 citations a year over 35 year(s) since 1993 |
| Impact for its field and year | 4 / 6 | Cited 10.0× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 2 / 6 | Cited by 5 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 | 4 / 4 | Last-listed author Paul Greengard: h-index 206 (OpenAlex, whole career) |
| Institution's track record | 1 / 3 | Rockefeller University: institution h-index 1,200 (OpenAlex) |
| Multicenter collaboration | 0 / 3 | OpenAlex lists 1 institution(s) in 1 country — scores zero (affiliation lists can be incomplete) |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 8416966) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Total | 44 / 100 | — |
What each of these 20 components measures, and what this score is not →
Read the original
- DOI: 10.1016/s0021-9258(18)54194-6
- PubMed: 8416966
- 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).
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