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Qualitative and quantitative comparison of brain proteins in Alzheimer's disease
Buee L, Laine A, Delacourte A, Flament S, Han KK.. Biological chemistry Hoppe-Seyler, 1989-11-01
Topic: Amyloid, tau and blood-test diagnosis
In human brain extracts, most proteins of pathological interest in Alzheimer's disease are insoluble and their analysis is often performed on denatured and reduced samples by immunoblotting after electrophoresis on polyacrylamide gel in presence of sodium dodecyl sulfate. Because we needed to accurately compare the concentration of several proteins in brain extracts to investigate the etiology of the disease, the quantitative aspect of immunoblotting was assessed and the results compared for a soluble component with those obtained by electroimmunoassay. Glial fibrillary acidic protein (GFAP) and Tau proteins were analysed by immunoblotting in brain homogenates treated with the Laemmli sample buffer from 10 control and 25 Alzheimer's disease brains. The linearity of densitometric measures of dilutions for one given sample was demonstrated. A 8 to 16-fold GFAP increase in Alzheimer brain was established. With regard to Tau proteins it was possible to show the presence of two pathological Tau variants (Tau 64 and 69) in all the Alzheimer brain homogenates, furthermore, the amount of Tau 64 and 69 was proportional to the presence of neurofibrillary degeneration. As far as alpha 1-antichymotrypsin is concerned, we showed, in a second set of brain samples (14 control and 12 Alzheimer brains), discrepancies between the results obtained by immunoblotting and by electroimmunoassay while for a given sample linearity of immunoblotting measures of dilutions of this sample was demonstrated. Quantitation by immunoblotting of such components which can be quantified using other procedures is uncertain whereas the interest of immunoblotting is undoubted for the insoluble proteins in the brain extracts.
Key findings
- Because we needed to accurately compare the concentration of several proteins in brain extracts to investigate the etiology of the disease, the quantitative aspect of immunoblotting was assessed and the results compared for a soluble component with those obtained by electroimmunoassay.
- The linearity of densitometric measures of dilutions for one given sample was demonstrated.
- As far as alpha 1-antichymotrypsin is concerned, we showed, in a second set of brain samples (14 control and 12 Alzheimer brains), discrepancies between the results obtained by immunoblotting and by electroimmunoassay while for a given sample linearity of immunoblotting measures of dilutions of this sample was demonstrated.
Why it matters
This 1989 laboratory study compared protein measurement methods in brain extracts and found an 8- to 16-fold GFAP increase and two pathological Tau variants in Alzheimer brains. It is a methods and tissue analysis study and does not provide any treatment, cure, or prevention for Alzheimer's disease.
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Study details
- Evidence strengthLow
How this study scored 28/100
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 (Biological chemistry Hoppe-Seyler) |
| Journal's citation record | 0 / 4 | Biological Chemistry Hoppe-Seyler: journal h-index 73 (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 | 1989 — 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) |
| Randomised / blinded | 0 / 2 | No randomisation or blinding stated — scores zero (not stated in the record — scored 0) |
| Times cited | 2 / 7 | Cited 14 times (OpenAlex, 2026-10-10) |
| Citations per year | 0 / 5 | 0.4 citations a year over 39 year(s) since 1989 |
| Impact for its field and year | 2 / 6 | Cited 1.2× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 0 / 6 | No other study in this library cites it |
| Still being cited | 0 / 4 | Cited 0 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 1 / 4 | Last-listed author Kia‐Ki Han: h-index 18 (OpenAlex, whole career) |
| Institution's track record | 2 / 3 | Inserm: institution h-index 1,988 (OpenAlex) |
| Multi-centre 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 2514723) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Total | 28 / 100 | — |
What each of these 20 components measures, and what this score is not →
Read the original
May need a subscription Unpaywall, Europe PMC and OpenAlex found no free copy of the full text (checked 10 Oct 2026), so the publisher may charge for it. The PubMed abstract is free.
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
Buee, L., Laine, A., Delacourte, A., Flament, S., & Han, K. K. (1989). Qualitative and quantitative comparison of brain proteins in Alzheimer's disease. Biological chemistry Hoppe-Seyler. https://doi.org/10.1515/bchm3.1989.370.2.1229
Vancouver
Buee L, Laine A, Delacourte A, Flament S, Han KK. Qualitative and quantitative comparison of brain proteins in Alzheimer's disease. Biological chemistry Hoppe-Seyler. 1989. doi:10.1515/bchm3.1989.370.2.1229. PMID: 2514723.
BibTeX
@article{buee1989-2514723,
author = {Buee, L. and Laine, A. and Delacourte, A. and Flament, S. and Han, K. K.},
title = {{Qualitative and quantitative comparison of brain proteins in Alzheimer's disease}},
journal = {Biological chemistry Hoppe-Seyler},
year = {1989},
doi = {10.1515/bchm3.1989.370.2.1229},
pmid = {2514723},
url = {https://doi.org/10.1515/bchm3.1989.370.2.1229}
}
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