Bluhm A, Schrempel S, von Hörsten S, Schulze A, Roßner S (2021)
Publication Type: Journal article, Review article
Publication year: 2021
Book Volume: 22
Article Number: 5450
Journal Issue: 11
DOI: 10.3390/ijms22115450
In Parkinson’s disease, aggregates of α‐synuclein within Lewy bodies and Lewy neurites represent neuropathological hallmarks. However, the cellular and molecular mechanisms triggering oligomeric and fibrillary α‐synuclein aggregation are not fully understood. Recent evidence indicates that oxidative stress induced by metal ions and post‐translational modifications such as phosphorylation, ubiquitination, nitration, glycation, and SUMOylation affect α‐synuclein conformation along with its aggregation propensity and neurotoxic profiles. In addition, proteolytic cleavage of α‐synuclein by specific proteases results in the formation of a broad spectrum of fragments with consecutively altered and not fully understood physiological and/or pathological properties. In the present review, we summarize the current knowledge on proteolytical α‐ synuclein cleavage by neurosin, calpain‐1, cathepsin D, and matrix metalloproteinase‐3 in health and disease. We also shed light on the contribution of the same enzymes to proteolytical processing of pathogenic proteins in Alzheimer’s disease and report potential cross‐disease mechanisms of pathogenic protein aggregation.
APA:
Bluhm, A., Schrempel, S., von Hörsten, S., Schulze, A., & Roßner, S. (2021). Proteolytic α‐synuclein cleavage in health and disease. International Journal of Molecular Sciences, 22(11). https://doi.org/10.3390/ijms22115450
MLA:
Bluhm, Alexandra, et al. "Proteolytic α‐synuclein cleavage in health and disease." International Journal of Molecular Sciences 22.11 (2021).
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