ArticleHistochemistry and cell biology2009
Distribution of the epilepsy-related Lgi1 protein in rat cortical neurons.
Article in Histochemistry and cell biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 8 citations in OpenAlex.
- A novel LGI1 mutation causing autosomal dominant lateral temporal lobe epilepsy confirmed by a precise knock-in mouse model.CNS neuroscience & therapeutics · 2022Article
- Secretion-Positive LGI1 Mutations Linked to Lateral Temporal Epilepsy Impair Binding to ADAM22 and ADAM23 Receptors.PLoS genetics · 2016Article
- The temporal and spatial expression pattern of the LGI1 epilepsy predisposition gene during mouse embryonic cranial development.BMC neuroscience · 2011Article
- Extending the knowledge in histochemistry and cell biology.Histochemistry and cell biology · 2010Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Lgi1 protein is involved in the pathogenesis of autosomal dominant lateral temporal epilepsy because mutations in the leucine-rich, glioma-inactivated 1 (LGI1) gene have been found in affected subjects and families; however, the function of Lgi1 is still unclear. Definition of the fine intracellular distribution of Lgi1 in normal cortical tissue would add in understanding its role and envisage pathogenetic mechanisms. Therefore, we analyzed normal rat cortex for Lgi1 by combining biochemistry, immunohistochemistry and immunoelectron microscopy. Our results demonstrate that Lgi1 is a cytoplasmic protein distributed both in the soma and in the processes of neurons: it occurs on the rough endoplasmic reticulum, the site of synthesis, in the Golgi complex, where it undergoes glycosylation, and in close proximity to neurotubules and neurofilaments, especially in the axons, but it is scarce at synapses and the neurilemma. Lgi1 association with axonal cytoskeletal structures would imply Lgi1 is either transported along axons by motor proteins, or playing some role as a carrier in the axonal Xux, or it could be involved in the regulation of cytoskeletal organization.
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Registered trials
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