The prion protein in human neuromuscular diseases

Gábor G. Kovács, Ognian Kalev, Ellen Gelpi, Christine Haberler, Julia Wanschitz, Michaela Strohschneider, Mária J. Molnár, L. László, Herbert Budka

Research output: Contribution to journalArticle

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Abstract

The basis of human prion diseases affecting the nervous system is accumulation of a disease-associated conformer (PrPSc) of the normal cellular prion protein (PrPC). Earlier studies demonstrated increased expression of PrPC in inclusion body myositis (IBM), dermato-, and polymyositis, as well as neurogenic muscle atrophy. To define the spectrum and reliability of PrPC immunoreactivity, its expression was examined systematically in a series of pathologically characterized muscular disorders by means of immunohistochemistry, confocal laser microscopy, and immunogold electron microscopy. Anti-PrPC immunolabelling of rimmed vacuoles was observed in IBM, inclusions of myofibrillary myopathy, targets, regenerating, and atrophic fibres, mononuclear cells, in addition to ragged red fibres in mitochondrial myopathies, and focal sarcolemmal immunostaining in non-diseased controls. Quantitative analysis demonstrated that, in neurogenic muscle lesions, anti-PrPC staining detects a significantly broader spectrum of fibres than anti-vimentin or anti-NCAM. In dystrophic muscle, PrPC expression was mainly restricted to regenerating fibres. In IBM, PrPC expression was not confined to rimmed vacuoles or vacuolated fibres and only a small percentage (7.1%) of rimmed vacuoles were PrPC positive. Ultrastructurally, PrPC was observed in the cytoplasm of lymphocytes, in the myofibrillar network of targets, and in rimmed vacuoles. Knowledge of disease circumstances with altered expression of PrPC is important in the setting of a potentially increased chance for extraneural PrPC-PrPSc conversion. In addition, our observations suggest that PrPC may have a general stress-response effect in various neuromuscular disorders.

Original languageEnglish
Pages (from-to)241-247
Number of pages7
JournalJournal of Pathology
Volume204
Issue number3
DOIs
Publication statusPublished - Nov 2004

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Neuromuscular Diseases
Inclusion Body Myositis
Vacuoles
Confocal Microscopy
Mitochondrial Myopathies
Neural Cell Adhesion Molecules
Muscles
Prion Diseases
Dermatomyositis
Muscular Atrophy
Vimentin
Muscular Diseases
Nervous System
Electron Microscopy
Cytoplasm
Immunohistochemistry
Lymphocytes
Staining and Labeling
Prion Proteins

Keywords

  • Inclusion body myositis
  • Inflammation
  • Muscle
  • Prion protein
  • Rimmed vacuole
  • Target

ASJC Scopus subject areas

  • Pathology and Forensic Medicine

Cite this

Kovács, G. G., Kalev, O., Gelpi, E., Haberler, C., Wanschitz, J., Strohschneider, M., ... Budka, H. (2004). The prion protein in human neuromuscular diseases. Journal of Pathology, 204(3), 241-247. https://doi.org/10.1002/path.1633

The prion protein in human neuromuscular diseases. / Kovács, Gábor G.; Kalev, Ognian; Gelpi, Ellen; Haberler, Christine; Wanschitz, Julia; Strohschneider, Michaela; Molnár, Mária J.; László, L.; Budka, Herbert.

In: Journal of Pathology, Vol. 204, No. 3, 11.2004, p. 241-247.

Research output: Contribution to journalArticle

Kovács, GG, Kalev, O, Gelpi, E, Haberler, C, Wanschitz, J, Strohschneider, M, Molnár, MJ, László, L & Budka, H 2004, 'The prion protein in human neuromuscular diseases', Journal of Pathology, vol. 204, no. 3, pp. 241-247. https://doi.org/10.1002/path.1633
Kovács GG, Kalev O, Gelpi E, Haberler C, Wanschitz J, Strohschneider M et al. The prion protein in human neuromuscular diseases. Journal of Pathology. 2004 Nov;204(3):241-247. https://doi.org/10.1002/path.1633
Kovács, Gábor G. ; Kalev, Ognian ; Gelpi, Ellen ; Haberler, Christine ; Wanschitz, Julia ; Strohschneider, Michaela ; Molnár, Mária J. ; László, L. ; Budka, Herbert. / The prion protein in human neuromuscular diseases. In: Journal of Pathology. 2004 ; Vol. 204, No. 3. pp. 241-247.
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