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p62/SQSTM1 is overexpressed and prominently accumulated in inclusions of sporadic inclusion-body myositis muscle fibers, and can help differentiating it from polymyositis and dermatomyositis

Nogalska, Anna, Terracciano, Chiara, D’Agostino, Carla, King Engel, W., Askanas, Valerie·2009·Acta Neuropathologica
DOI 10.1007/s00401-009-0564-6
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Abstract

p62, also known as sequestosome1, is a shuttle protein transporting polyubiquitinated proteins for both the proteasomal and lysosomal degradation. p62 is an integral component of inclusions in brains of various neurodegenerative disorders, including Alzheimer disease (AD) neurofibrillary tangles (NFTs) and Lewy bodies in Parkinson disease. In AD brain, the p62 localized in NFTs is associated with phosphorylated tau (p-tau). Sporadic inclusion-body myositis (s-IBM) is the most common progressive muscle disease associated with aging, and its muscle tissue has several phenotypic similarities to AD brain. Abnormal accumulation of intracellular multiprotein inclusions, containing p-tau in the form of paired helical filaments, amyloid-beta, and several other "Alzheimer-characteristic proteins", is a characteristic feature of the s-IBM muscle fiber phenotype. Diminished proteasomal and lysosomal protein degradation appear to play an important role in the formation of intra-muscle-fiber inclusions. We now report that: (1) in s-IBM muscle fibers, p62 protein is increased on both the protein and the mRNA levels, and it is strongly accumulated within, and as a dense peripheral shell surrounding, p-tau containing inclusions, by both the light- and electron-microscopy. Accordingly, our studies provide a new, reliable, and simple molecular marker of p-tau inclusions in s-IBM muscle fibers. The prominent p62 immunohistochemical positivity and pattern diagnostically distinguish s-IBM from po…

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  • An increase in LC3-II levels in combination with the lysosomal (or ideally autophagy-specific) removal of an autophagic substrate that is not a good proteasomal substrate provides an independent assessment of autophagic flux.

    “For example, an increase in LC3-II levels in combination with the lysosomal (or ideally autophagy-specific) removal of an autophagic substrate (such as an organelle [340,341]) that is not a good proteasomal substrate provides an independent assessment of autophagic flux.”

    From Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1 (2021) · cites this paper as [340]

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Research works printed but not linked: 35

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Metadata

Authors
Nogalska, A., Terracciano, C., D’Agostino, C., King Engel, W., & Askanas, V.
Venue
Acta Neuropathologica
Publisher
Springer Science and Business Media LLC
Published
2009-06-26
Volume
118
Issue
3
Pages
407-413
ISSN
  • 0001-6322
  • 1432-0533
DOI
10.1007/s00401-009-0564-6
Cited by
134
References
4
Language
en
Licence
www.springer.com/tdm (tdm)

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