The Branched-Chain Aminotransferase Proteins: Novel Redox Chaperones for Protein Disulfide Isomerase–Implications in Alzheimer's Disease
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Aims: The human branched-chain aminotransferase proteins (hBCATm and hBCATc) are regulated through oxidation and S-nitrosation. However, it remains unknown whether they share common redox characteristics to enzymes such as protein disulfide isomerase (PDI) in terms of regulating cellular repair and protein misfolding. Results: Here, similar to PDI, the hBCAT proteins showed dithiol-disulfide isomerase activity that was mediated through an S-glutathionylated mechanism. Site-directed mutagenesis of the active thiols of the CXXC motif demonstrates that they are fundamental to optimal protein folding. Far Western analysis indicated that both hBCAT proteins can associate with PDI. Co-immunoprecipitation studies demonstrated that hBCATm directly binds to PDI in IMR-32 cells and the human brain. Electron and confocal microscopy validated the expression of PDI in mitochondria (using Mia40 as a mitochondrial control), where both PDI and Mia40 were found to be co-localized with hBCATm. Under conditions of oxidative stress, this interaction is decreased, suggesting that the proposed chaperone role for hBCATm may be perturbed. Moreover, immunohistochemistry studies show that PDI and hBCAT are expressed in the same neuronal and endothelial cells of the vasculature of the human brain, supporting a physiological role for this binding. Innovation: This study identifies a novel redox role for hBCAT and confirms that hBCATm differentially binds to PDI under cellular stress. Conclusion: These studies indicate that hBCAT may play a role in the stress response of the cell as a novel redox chaperone, which, if compromised, may result in protein misfolding, creating aggregates as a key feature in neurodegenerative conditions such as Alzheimer's disease. Antioxid. Redox Signal. 20, 2497–2513.
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BCAT was identified as a novel chaperone in protein folding through its thiol oxidoreductase activity.
“These include proteins important in cell signalling and protein folding (e.g. BCAT was identified as a novel chaperone in protein folding through its thiol oxidoreductase activity, El Hindy et al. 2014).”
From Alzheimer’s disease: Targeting the glutamatergic system (2020) · cites this paper as El Hindy et al. 2014
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Nanotherapy for Early Dementia: Targeting Senile DementiaPreprint
D'Arrigo, J. S. (2017) · doi:10.31219/osf.io/3vysu_v1
Dare, E. S., Schultz, M. B., Hughes, J. J., Conway, M. E., & Dong, M. (2026) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2026.2711110
Self-citation
- Authors
- El Hindy, M., Hezwani, M., Corry, D., Hull, J., El Amraoui, F., Harris, M., Lee, C., Forshaw, T., Wilson, A., Mansbridge, A., Hassler, M., Patel, V. B., Kehoe, P. G., Love, S., & Conway, M. E.
- Affiliations
- University of the West of England
- University of the West of England (GB)
- University of Westminster (GB)
- Frenchay Hospital (GB)
- ORCID
- Venue
- Antioxidants & Redox Signaling
- Publisher
- SAGE Publications
- Published
- 2014-06
- Volume
- 20
- Issue
- 16
- Pages
- 2497-2513
- ISSN
- 1523-0864 (ISSN-L)
- 1557-7716
- PMC
- PMC4026213
- OpenAlex
- W2023847913
- Cited by
- 31
- References
- 74
- Citations by year
- 2026: 1 · 2025: 1 · 2022: 6 · 2021: 1 · 2020: 5 · 2019: 1 · 2018: 2 · 2017: 4 · 2016: 4 · 2015: 5 · 2014: 1
- FWCI
- 1.93
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Antioxidants and Redox Signaling (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- UWE Research Repository (UWE Bristol) (submittedVersion, cc-by)
- Explore Bristol Research (submittedVersion)
- Funders
- Wake Forest University
- University of Bristol
- University of the West of England
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- branched-chain amino acid aminotransferase, protein disulfide isomerase, S-glutathionylation, CXXC motif, protein misfolding, protein folding, oxidative stress, S-nitrosylation, protein-protein interaction, Alzheimer's disease, neurodegeneration, cerebral vasculature
- MeSH terms
- Alzheimer Disease, Transaminases, Cell Line, Humans, Oxidation-Reduction, Oxidative Stress, Protein Disulfide-Isomerases
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