ArticleToxicological sciences : an official journal of the Society of Toxicology2009
Potential role of alpha-synuclein and metallothionein in lead-induced inclusion body formation.
Article in Toxicological sciences : an official journal of the Society of Toxicology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 30 citations in OpenAlex.
- Disease-specific tau polymorphs are associated with unique protein networks across proteinopathies.The EMBO journal · 2026Article
- Emerging Roles of Metallothioneins in Beta Cell Pathophysiology: Beyond and Above Metal Homeostasis and Antioxidant Response.Biology · 2021Review
- An efficient autometallography approach to localize lead at ultra-structural levels of cultured cells.Biophysics reports · 2020Article
- α-Synuclein Enhances Cadmium Uptake and Neurotoxicity via Oxidative Stress and Caspase Activated Cell Death Mechanisms in a Dopaminergic Cell Model of Parkinson's Disease.Neurotoxicity research · 2017Article
- Mammalian Metallothionein-3: New Functional and Structural Insights.International journal of molecular sciences · 2017Review
- On the nature of the Cu-rich aggregates in brain astrocytes.Redox biology · 2017Article
- Metallothionein blocks oxidative DNA damage induced by acute inorganic arsenic exposure.Toxicology and applied pharmacology · 2015Article
- Distribution of selected essential (Co, Cu, Fe, Mn, Mo, Se, and Zn) and nonessential (Cd, Pb) trace elements among protein fractions from hepatic cytosol of European chub (Squalius cephalus L.).Environmental science and pollution research international · 2013Article
- Metallothionein blocks oxidative DNA damage in vitro.Archives of toxicology · 2013Article
- Phosphorylation of α-Synuclein at Y125 and S129 alters its metal binding properties: implications for understanding the role of α-Synuclein in the pathogenesis of Parkinson's Disease and related disorders.ACS chemical neuroscience · 2011Article
- Mammalian metallothionein in toxicology, cancer, and cancer chemotherapy.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2011Review
- Lead-binding proteins: a review.Journal of toxicology · 2011Article
- Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Lead (Pb) produces aggresome-like inclusion bodies (IBs) in target cells as a toxic response. Our prior work shows metallothionein (MT) is required for this process. We used MT-I/II double knockout (MT-null) and parental wild-type (WT) cell lines to further explore the formation process of Pb-induced IBs. Unlike WT cells, MT-null cells did not form IBs after Pb exposure. Western blot of cytosol showed soluble MT protein in WT cells was lost during Pb exposure as IBs formed. Transfection of MT-I into MT-null cells allowed IBs formation after Pb exposure. Considering Pb-induced IBs may be like disease-related aggresomes, which often contain alpha-synuclein (Scna), we investigated Scna expression in cells capable (WT) and incapable (MT-null) of producing IBs after Pb exposure. Scna protein showed poor basal expression in MT-null cells. Pb exposure increased Scna expression only in WT cells. MT transfection increased Scna transcript to WT levels. In WT or MT-transfected MT-null cells, Pb-induced Scna expression rapidly increased and then decreased over 48 h as Pb-induced IBs were formed. A direct interaction between Scna and MT was confirmed ex vivo by antibody pulldown assay where the proteins coprecipitated with an antibody to MT. Pb exposure caused increased colocalization of MT and Scna proteins with time only in WT cells. In WT mice after chronic Pb exposure Scna was localized in renal cells containing forming IBs, whereas MT-null mice did not form IBs. Thus, Scna could be component of Pb-induced IBs and, with MT, may play a role in IBs formation.
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