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Letter to the editor on: Hornerin deposits in neuronal intranuclear inclusion disease: direct identification of proteins with compositionally biased regions in inclusions by Park et al. (2022).

ABSTRACT:

SUBMITTER: Luo H

PROVIDER: S-EPMC10759526 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature

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Letter to the editor on: Hornerin deposits in neuronal intranuclear inclusion disease: direct identification of proteins with compositionally biased regions in inclusions by Park et al. (2022).

Luo Huihui H Gustavsson Emil K EK Macpherson Hannah H Dominik Natalia N Zhelcheska Kristina K Montgomery Kylie K Anderson Claire C Yau Wai Yan WY Efthymiou Stephanie S Turner Chris C DeTure Michael M Dickson Dennis W DW Josephs Keith A KA Revesz Tamas T Lashley Tammaryn T Halliday Glenda G Rowe Dominic B DB McCann Emily E Blair Ian I Lees Andrew J AJ Tienari Pentti J PJ Suomalainen Anu A Molina-Porcel Laura L Kovacs Gabor G GG Gelpi Ellen E Hardy John J Haltia Matti J MJ Tucci Arianna A Jaunmuktane Zane Z Ryten Mina M Houlden Henry H Chen Zhongbo Z

Acta neuropathologica communications 20240102 1

PMID: 38167323

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Hornerin deposits in neuronal intranuclear inclusion disease: direct identification of proteins with compositionally biased regions in inclusions.

Project description:Neuronal intranuclear inclusion disease (NIID) is a neurodegenerative disorder, characterized by the presence of eosinophilic inclusions (NIIs) within nuclei of central and peripheral nervous system cells. This study aims to identify the components of NIIs, which have been difficult to analyze directly due to their insolubility. In order to establish a method to directly identify the components of NIIs, we first analyzed the huntingtin inclusion-rich fraction obtained from the brains of Huntington disease model mice. Although the sequence with expanded polyglutamine could not be identified by liquid-chromatography mass spectrometry, amino acid analysis revealed that glutamine of the huntingtin inclusion-rich fraction increased significantly. This is compatible with the calculated amino acid content of the transgene product. Therefore, we applied this method to analyze the NIIs of diseased human brains, which may have proteins with compositionally biased regions, and identified a serine-rich protein called hornerin. Since the analyzed NII-rich fraction was also serine-rich, we suggested hornerin as a major component of the NIIs. A specific distribution of hornerin in NIID was also investigated by Matrix-assisted laser desorption/ionization imaging mass spectrometry and immunofluorescence. Finally, we confirmed a variant of hornerin by whole-exome sequencing and DNA sequencing. This study suggests that hornerin may be related to the pathological process of this NIID, and the direct analysis of NIIs, especially by amino acid analysis using the NII-rich fractions, would contribute to a deeper understanding of the disease pathogenesis.

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