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Immunochemical and biochemical characterization of tau proteins in normal and Alzheimer's disease brains with Alz 50 and Tau-1
Ksiezak-Reding H, Binder LI, Yen SH.. The Journal of biological chemistry, 1988-06-01
Topic: Disease mechanisms in lab and animal studies
Microtubule-associated protein tau was characterized in 5 Alzheimer and 5 control brains using two monoclonal antibodies, Alz 50 and Tau-1. Quantitative analysis of immunoblots with the antibodies showed that both homogenate and supernatant fractions (12,000 x g) from Alzheimer brains contained 38-65% less tau immunoreactivity compared to normal brains. The reduction was found in all brain regions studied (frontal and temporal lobes and thalamus) and in both gray and white matter. In partially purified tau preparations, the yield of protein was lower in Alzheimer (by 35%) than in control brain. Incubation of brain proteins, transferred onto nitrocellulose paper, with alkaline phosphatase had either no effect or slightly increased the antibody binding to tau proteins from both brain tissues. Immunoblots of tau-enriched preparations subjected to two-dimensional gel electrophoresis showed no major changes in the staining pattern of tau isoforms in Alzheimer samples except for a weaker reactivity of the basic isovariants as compared to non-Alzheimer samples. The elution volume of tau from Alzheimer brain supernatant on a Sepharose CL-6B column was similar to that from non-Alzheimer brain and equal to that of aldolase (Mr = 158,000). Our data suggest that most of tau proteins from both types of brain have similar biochemical properties. The reduction in tau reactivity in Alzheimer tissue may be due to a reduction in neuronal cell population or incorporation of soluble tau into stable structures such as neurofibrillary tangles, since the tangles have been shown to react with anti-tau antibodies.
Key findings
- Quantitative analysis of immunoblots with the antibodies showed that both homogenate and supernatant fractions (12,000 x g) from Alzheimer brains contained 38-65% less tau immunoreactivity compared to normal brains.
- Immunoblots of tau-enriched preparations subjected to two-dimensional gel electrophoresis showed no major changes in the staining pattern of tau isoforms in Alzheimer samples except for a weaker reactivity of the basic isovariants as compared to non-Alzheimer samples.
- Our data suggest that most of tau proteins from both types of brain have similar biochemical properties.
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Study details
- Evidence strengthLow
How this study scored 36/100
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. We have no data on journal's citation record, times cited, citations per year, impact for its field and year, cited by studies here, still being cited, senior author's track record, institution's track record and multi-centre collaboration, so those were left out: it earned 21 of the 58 points we could judge it on, which is 36 out of 100.
| Component | Points | Why |
|---|---|---|
| Journal tier | 7 / 10 | Tier 3 — peer-reviewed journal (The Journal of biological chemistry) |
| Journal's citation record | — / 4 | No journal record from OpenAlex — left out of this score |
| 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 | 1988 — 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 | — / 7 | No citation count (not found in OpenAlex) — left out of this score |
| Citations per year | — / 5 | No citation count or no year — left out of this score |
| Impact for its field and year | — / 6 | No field-weighted citation impact (OpenAlex has none yet) — left out of this score |
| Cited by studies here | — / 6 | Not yet checked against this library's citation graph — left out of this score |
| Still being cited | — / 4 | No yearly citation counts — left out of this score |
| Senior author's track record | — / 4 | Senior author's record not available — left out of this score |
| Institution's track record | — / 3 | No institution listed in OpenAlex — left out of this score |
| Multi-centre collaboration | — / 3 | Institutions not listed — left out of this score |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 3131334) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Points | 21 / 58 | Scored on 11 of 20 parts. We have no data for the rest, so they are left out: 21 of the 58 points we could judge it on is 36 out of 100. |
| Total | 36 / 100 | — |
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Cite this study APA, Vancouver, BibTeX · download .bib or .ris
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APA 7th
Ksiezak-Reding, H., Binder, L. I., & Yen, S. H. (1988). Immunochemical and biochemical characterization of tau proteins in normal and Alzheimer's disease brains with Alz 50 and Tau-1. The Journal of biological chemistry. https://doi.org/10.1016/s0021-9258(18)68426-1
Vancouver
Ksiezak-Reding H, Binder LI, Yen SH. Immunochemical and biochemical characterization of tau proteins in normal and Alzheimer's disease brains with Alz 50 and Tau-1. The Journal of biological chemistry. 1988. doi:10.1016/s0021-9258(18)68426-1. PMID: 3131334.
BibTeX
@article{ksiezakreding1988-3131334,
author = {Ksiezak-Reding, H. and Binder, L. I. and Yen, S. H.},
title = {{Immunochemical and biochemical characterization of tau proteins in normal and Alzheimer's disease brains with Alz 50 and Tau-1}},
journal = {The Journal of biological chemistry},
year = {1988},
doi = {10.1016/s0021-9258(18)68426-1},
pmid = {3131334},
url = {https://doi.org/10.1016/s0021-9258(18)68426-1}
}
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