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Redox proteomics identification of specifically carbonylated proteins in the hippocampi of triple transgenic Alzheimer's disease mice at its earliest pathological stage
Shen L, Chen C, Yang A, Chen Y, Liu Q, Ni J.. Journal of proteomics, 2015-04-15
Topic: Brain proteins, microglia and lab models
Alzheimer's disease (AD) is the most common cause of dementia in the elderly population. Attempts to develop therapies for the treatment of the late stage AD have been unsuccessful. Increasing evidences indicate that oxidative stress is an early event of neurodegeneration, however the pathogenic mechanism of AD remains unclarified. In the present study, slot-blot analysis was used to determine the levels of protein carbonyls in the hippocampi of 3-month-old triple transgenic AD mice (3 × Tg-AD). The increased levels of protein carbonyls were observed in the hippocampi of 3 × Tg-AD mice as compared to the non-transgenic controls (non-Tg). Using a redox-proteomic approach, twelve proteins were found to be significantly altered in the levels of protein carbonyls in the hippocampus. These proteins are crucial in energy metabolism, protein folding, cell structure, signal transduction and excitotoxicity. Immunoprecipitation and Western blot were used to validate two proteins identified by the redox proteomics. In addition, increased expression level of carbonyl reductase 1 (CBR1) was observed in the hippocampi of 3 × Tg-AD mice. These results demonstrate that significant protein carbonylation occurs early in the 3-month-old 3 × Tg-AD mice, which support the viewpoint that oxidative stress is an early event in AD progression. Biological significance In this study, we have observed increased levels of protein carbonyls in the hippocampi of 3 × Tg-AD mice before the appearance of Aβ plaques and neurofibrillary tangles (NFTs). By redox proteomics, twelve specifically carbonylated proteins were identified. Among them, alpha-enolase (ENO1) and glutamine synthetase (GS) were identified as the common targets of oxidation in the brains of 3 × Tg-AD mice, mild cognitive impairment (MCI) sufferers and AD patients. For the first time, the oxidation of t-complex protein 1 subunit epsilon (CCT5) and protein disulfide-isomerase A3 (PDIA3) were reported to be associated with AD. These results indicated that the combination of monoclonal anti-DNP antibody with digital imaging system could enhance the specificity and accuracy of redox proteomics analysis. Those data support the viewpoint that oxidative stress occurs at the early pathological stage of AD. In addition, this paper provides new information for understanding the pathological process of AD and for developing more appropriate therapies to intervene AD progression.
Cite this study APA, Vancouver, BibTeX · download .bib or .ris
APA 7th
Shen, L., Chen, C., Yang, A., Chen, Y., Liu, Q., & Ni, J. (2015). Redox proteomics identification of specifically carbonylated proteins in the hippocampi of triple transgenic Alzheimer's disease mice at its earliest pathological stage. Journal of proteomics. https://doi.org/10.1016/j.jprot.2015.04.005
Vancouver
Shen L, Chen C, Yang A, Chen Y, Liu Q, Ni J. Redox proteomics identification of specifically carbonylated proteins in the hippocampi of triple transgenic Alzheimer's disease mice at its earliest pathological stage. Journal of proteomics. 2015. doi:10.1016/j.jprot.2015.04.005. PMID: 25890254.
BibTeX
@article{shen2015-25890254,
author = {Shen, L. and Chen, C. and Yang, A. and Chen, Y. and Liu, Q. and Ni, J.},
title = {{Redox proteomics identification of specifically carbonylated proteins in the hippocampi of triple transgenic Alzheimer's disease mice at its earliest pathological stage}},
journal = {Journal of proteomics},
year = {2015},
doi = {10.1016/j.jprot.2015.04.005},
pmid = {25890254},
url = {https://doi.org/10.1016/j.jprot.2015.04.005}
}
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Key findings
- Increasing evidences indicate that oxidative stress is an early event of neurodegeneration, however the pathogenic mechanism of AD remains unclarified.
- The increased levels of protein carbonyls were observed in the hippocampi of 3 × Tg-AD mice as compared to the non-transgenic controls (non-Tg).
- Using a redox-proteomic approach, twelve proteins were found to be significantly altered in the levels of protein carbonyls in the hippocampus.
- These results demonstrate that significant protein carbonylation occurs early in the 3-month-old 3 × Tg-AD mice, which support the viewpoint that oxidative stress is an early event in AD progression.
- For the first time, the oxidation of t-complex protein 1 subunit epsilon (CCT5) and protein disulfide-isomerase A3 (PDIA3) were reported to be associated with AD.
Why it matters
In 3-month-old triple transgenic Alzheimer's disease mice, increased protein carbonylation was found in the hippocampus, supporting the view that oxidative stress is an early event in Alzheimer's disease progression. This is early animal research and does not establish any treatment, cure, or prevention for people.
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Study details
- Evidence strengthLow
How this study scored 35/100
Published in a peer-reviewed journal. Scored zero for study design, sample size, effect reported and randomised / blinded because the record does not state it.
| Component | Points | Why |
|---|---|---|
| Journal tier | 7 / 10 | Tier 3 — peer-reviewed journal (Journal of proteomics) |
| Journal's citation record | 1 / 4 | Journal of Proteomics: journal h-index 141 (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 | 2015 — 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 | Laboratory or animal study (title names “transgenic”) — scores zero |
| Randomised / blinded | 0 / 2 | No randomisation or blinding stated — scores zero (not stated in the record — scored 0) |
| Times cited | 4 / 7 | Cited 72 times (OpenAlex, 2026-10-10) |
| Citations per year | 2 / 5 | 5.5 citations a year over 13 year(s) since 2015 |
| Impact for its field and year | 3 / 6 | Cited 5.4× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 1 / 6 | Cited by 2 other studies in this library |
| Still being cited | 1 / 4 | Cited 13 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 2 / 4 | Last-listed author Jiazuan Ni: h-index 35 (OpenAlex, whole career) |
| Institution's track record | 0 / 3 | Shenzhen University: institution h-index 530 (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 25890254) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Total | 35 / 100 | — |
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