ArticleBiochemistry2013
A loss in cellular protein partners promotes α-synuclein aggregation in cells resulting from oxidative stress.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 17 citations in OpenAlex.
- Small molecules to perform big roles: The search for Parkinson's and Huntington's disease therapeutics.Frontiers in neuroscience · 2022Review
- The role of phospholipase Cβ on the plasma membrane and in the cytosol: How modular domains enable novel functions.Advances in biological regulation · 2019Article
- Diagnostic and prognostic value of mRNA expression of phospholipase C β family genes in hepatitis B virus‑associated hepatocellular carcinoma.Oncology reports · 2019Article
- Nuclear Lipids in the Nervous System: What they do in Health and Disease.Neurochemical research · 2017Review
- Sleep apnea leading to Parkinson's disease - an important association.Neuropsychiatric disease and treatment · 2017Article
- Up-regulated expression of phospholipase C, β1 is associated with tumor cell proliferation and poor prognosis in hepatocellular carcinoma.OncoTargets and therapy · 2016Article
- Article
- Linking alpha-synuclein properties with oxidation: a hypothesis on a mechanism underling cellular aggregation.Journal of bioenergetics and biomembranes · 2014Review
- Defining the oligomerization state of γ-synuclein in solution and in cells.Biochemistry · 2014Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
There is a consensus that oxidative stress promotes neurodegeneration and may be linked to plaque formation. α-Synuclein is the main component of neurodegenerative plaques. We have found that α-synuclein binds strongly to the enzyme phospholipase Cβ1 (PLCβ1) in vitro and in cells affecting both its G protein activation and its degradation. Because PLCβ1 binds to α-synuclein in cells, we tested whether decreasing its level would promote α-synuclein aggregation and whether overproducing PLCβ1 would inhibit aggregation. By imaging fluorescent α-synuclein in living HEK293, PC12, and SK-H-SH cells, we find that α-synuclein aggregation is directly related to the level of PLCβ1. Importantly, we found that oxidative stress does not affect the cellular levels of α-synuclein but results in the down-regulation of PLCβ1 thereby promoting α-synuclein aggregation. A peptide that mimics part of the α-synuclein binding site to PLCβ prevents aggregation. Our studies indicate that PLCβ1 can reduce cell damage under oxidative stress and offers a potential site that might be exploited to prevent α-synuclein aggregation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.