Leucine-rich glioma inactivated 3 is involved in amyloid β peptide uptake by astrocytes and endocytosis itself

We earlier showed that leucine-rich glioma inactivated 3 (LGI3) colocalizes with amyloid β peptide (Aβ) taken up by astrocytes both in vitro and in vivo, and that LGI3 accumulated with endocytosis-associated proteins in aged monkey brains. In this study, we confirmed that LGI3 localizes to the endoc...

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Veröffentlicht in:Neuroreport 2008-08, Vol.19 (12), p.1175-1179
Hauptverfasser: Okabayashi, Sachi, Kimura, Nobuyuki
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Kimura, Nobuyuki
description We earlier showed that leucine-rich glioma inactivated 3 (LGI3) colocalizes with amyloid β peptide (Aβ) taken up by astrocytes both in vitro and in vivo, and that LGI3 accumulated with endocytosis-associated proteins in aged monkey brains. In this study, we confirmed that LGI3 localizes to the endocytic pathway and found that its accumulation is caused by endocytic perturbation. Most notably, RNA interference experiments demonstrated that the downregulation of LGI3 clearly inhibited Aβ uptake by cultured rat astrocytes, moreover, transferrin uptake by both astrocytes and neuronal cells. Together with our earlier findings, our results suggest that LGI3 is involved in Aβ uptake by astrocytes and even endocytosis itself.
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subjects Amyloid beta-Peptides - metabolism
Animals
Astrocytes - cytology
Astrocytes - metabolism
Blotting, Western
Cell Line, Tumor
Cells, Cultured
Endocytosis
Female
Immunohistochemistry
Nerve Tissue Proteins - genetics
Nerve Tissue Proteins - metabolism
Neurons - cytology
Neurons - metabolism
Pregnancy
Rats
Rats, Sprague-Dawley
RNA Interference
Transferrin - metabolism
title Leucine-rich glioma inactivated 3 is involved in amyloid β peptide uptake by astrocytes and endocytosis itself
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