ArticleNeurotoxicology2010
Lead-induced accumulation of beta-amyloid in the choroid plexus: role of low density lipoprotein receptor protein-1 and protein kinase C.
Article in Neurotoxicology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 39 citations in OpenAlex.
- Metabolite transport across central nervous system barriers.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2024Review
- Microglial Activation in Metal Neurotoxicity: Impact in Neurodegenerative Diseases.BioMed research international · 2023Review
- Role of environmental pollutants in Alzheimer's disease: a review.Environmental science and pollution research international · 2020Review
- Emerging risk of environmental factors: insight mechanisms of Alzheimer's diseases.Environmental science and pollution research international · 2020Review
- The Role of Neurovascular System in Neurodegenerative Diseases.Molecular neurobiology · 2020Review
- An efficient autometallography approach to localize lead at ultra-structural levels of cultured cells.Biophysics reports · 2020Article
- Heavy Metal-Induced Cerebral Small Vessel Disease: Insights into Molecular Mechanisms and Possible Reversal Strategies.International journal of molecular sciences · 2020Review
- Childhood Lead Exposure and Adult Neurodegenerative Disease.Journal of Alzheimer's disease : JAD · 2018Review
- Dissecting the Contribution of Vascular Alterations and Aging to Alzheimer's Disease.Molecular neurobiology · 2016Review
- Immunohistochemical analysis of transporters related to clearance of amyloid-β peptides through blood-cerebrospinal fluid barrier in human brain.Histochemistry and cell biology · 2015Article
- Environmental pollutants as risk factors for neurodegenerative disorders: Alzheimer and Parkinson diseases.Frontiers in cellular neuroscience · 2015Review
- Choroid plexus dysfunction impairs beta-amyloid clearance in a triple transgenic mouse model of Alzheimer's disease.Frontiers in cellular neuroscience · 2015Article
- Stress-induced stimulation of choline transport in cultured choroid plexus epithelium exposed to low concentrations of cadmium.American journal of physiology. Regulatory, integrative and comparative physiology · 2014Article
- Upregulation of zinc transporter 2 in the blood-CSF barrier following lead exposure.Experimental biology and medicine (Maywood, N.J.) · 2014Article
- Neurovascular defects and faulty amyloid-β vascular clearance in Alzheimer's disease.Journal of Alzheimer's disease : JAD · 2013Review
- Neurovascular dysfunction and faulty amyloid β-peptide clearance in Alzheimer disease.Cold Spring Harbor perspectives in medicine · 2012Review
- Increased β-amyloid deposition in Tg-SWDI transgenic mouse brain following in vivo lead exposure.Toxicology letters · 2012Article
- The role of environmental exposures in neurodegeneration and neurodegenerative diseases.Toxicological sciences : an official journal of the Society of Toxicology · 2011Review
- Neurovascular pathways to neurodegeneration in Alzheimer's disease and other disorders.Nature reviews. Neuroscience · 2011Review
- Molecular biology of the blood-brain and the blood-cerebrospinal fluid barriers: similarities and differences.Fluids and barriers of the CNS · 2011Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The choroid plexus (CP), constituting the blood-cerebrospinal fluid barrier, has the capacity to remove beta-amyloid (Abeta) from the cerebrospinal fluid. Our previous work indicates that exposure to lead (Pb) results in Abeta accumulation in the CP by decreasing the expression of low density lipoprotein receptor protein-1 (LRP1), a protein involved in the transport and clearance of Abeta. The current study was designed to explore the relationship between Abeta accumulation, protein kinase C (PKC) activity, and LRP1 status in the CP following Pb exposure. Confocal microscopy revealed that LRP1 was primarily localized in the cytosol of the CP in control rats and migrated distinctly towards the apical surface and the microvilli following acute Pb exposure (27 mg Pb/kg, i.p., 24h). Co-immunostaining revealed a co-localization of both PKC-delta and LRP1 in the cytosol of control rats, with a distinct relocalization of both towards the apical membrane following Pb exposure. Preincubation of the tissues with PKC-delta inhibitor rottlerin (2 microM) prior to Pb exposure in vitro, resulted in abolishing the Pb-induced relocalization of LRP1 to the apical surface. Importantly, a significant elevation in intracellular Abeta levels (p<0.01) was observed in the cytosol of the CP following Pb exposure, which was abolished following preincubation with rottlerin. In addition, rottlerin caused a relocalization of Abeta from the cytosol to the nucleus in both Pb-treated and control CP tissues. Finally, co-immunoprecipitation studies revealed a strong protein-protein interaction between LRP1 and PKC-delta in the CP. These studies suggest that Pb exposure disrupts Abeta homeostasis at the CP, owing partly to a Pb-induced relocalization of LRP1 via PKC-delta.
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Registered trials
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