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Neurosci Lett. 2012 Jul 11;521(1):82-7. doi: 10.1016/j.neulet.2012.05.064. Epub 2012 Jun 1.

Immunoreactivity of the amino-terminal portion of the amyloid-beta precursor protein in the nucleolus.

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  • 1Research and Development Administration Department, Toagosei Co., Ltd., 1-14-1, Nishisinbashi, Minato-ku, Tokyo 105-8419, Japan.


The functioning and metabolic pathway of the amyloid β-precursor protein (APP) have not been fully elucidated. To fill this research gap, this study immunocytochemically investigated the intracellular localization of APP in the neuroblastoma cell line SK-N-SH and in normal primary cells. Using antibodies against the amino-terminal portion of the APP molecule, immunoreactivity was detected not only in the cytoplasm but also in the nucleus and nucleolus. Further analysis revealed the co-localization of amino acids 44-63 of the APP molecule with fibrillarin, a nucleolus marker. These findings indicate that a fraction of APP, including its amino-terminal portion, may be localized in the nucleus as well as in the nucleolus, suggesting an important role of APP in RNA metabolism and other intra-nucleolus functions.

Copyright © 2012 Elsevier Ireland Ltd. All rights reserved.

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