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Proteomics analysis of amyloid and nonamyloid prion disease phenotypes reveals both common and divergent mechanisms of neuropathogenesis. | LitMetric

Proteomics analysis of amyloid and nonamyloid prion disease phenotypes reveals both common and divergent mechanisms of neuropathogenesis.

J Proteome Res

Laboratory of Persistent Viral Diseases and ‡Research Technologies Branch, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, Hamilton, Montana 59840, United States.

Published: November 2014

AI Article Synopsis

  • Prion diseases are neurodegenerative disorders caused by the misfolding of a normal protein (PrP(C)) into a harmful form (PrP(Sc)), affecting various mammals, including humans.
  • In wild-type mice, PrP(Sc) forms diffuse deposits, while mice lacking the protein's membrane anchor develop denser amyloid plaques with different biochemical implications.
  • A proteomics approach revealed that both models show neuroinflammation and cell death-related proteins, but mitochondrial pathways are specifically affected in diffuse deposits, while metal binding and synaptic transport are disrupted in amyloid plaques.

Article Abstract

Prion diseases are a heterogeneous group of neurodegenerative disorders affecting various mammals including humans. Prion diseases are characterized by a misfolding of the host-encoded prion protein (PrP(C)) into a pathological isoform termed PrP(Sc). In wild-type mice, PrP(C) is attached to the plasma membrane by a glycosylphosphatidylinositol (GPI) anchor and PrP(Sc) typically accumulates in diffuse nonamyloid deposits with gray matter spongiosis. By contrast, when mice lacking the GPI anchor are infected with the same prion inoculum, PrP(Sc) accumulates in dense perivascular amyloid plaques with little or no gray matter spongiosis. In order to evaluate whether different host biochemical pathways were implicated in these two phenotypically distinct prion disease models, we utilized a proteomics approach. In both models, infected mice displayed evidence of a neuroinflammatory response and complement activation. Proteins involved in cell death and calcium homeostasis were also identified in both phenotypes. However, mitochondrial pathways of apoptosis were implicated only in the nonamyloid form, whereas metal binding and synaptic vesicle transport were more disrupted in the amyloid phenotype. Thus, following infection with a single prion strain, PrP(C) anchoring to the plasma membrane correlated not only with the type of PrP(Sc) deposition but also with unique biochemical pathways associated with pathogenesis.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4227561PMC
http://dx.doi.org/10.1021/pr500329wDOI Listing

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