New insights into cellular prion protein (PrPc) functions: The “ying and yang” of a relevant protein

Nicolas, Oriol; Gavı́n, Rosalina; Rı́o, José Antonio del

doi:10.1016/j.brainresrev.2009.06.002

Cited by 51 publications

(44 citation statements)

References 204 publications

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“…It is relevant to note that increased expression of PrP C increased its association with lipid rafts which may in turn trigger increased intracellular oxidative stress [76,22], thereby affecting tau expression and phosphorylation [74,77]. In contrast to the expected result, decreased PrP C expression in our experiments correlated with increased tau phosphorylation (ptau/total tau as well as ptau/actin ratios) after in vitro treatment with ADDLs.…”

Section: Discussioncontrasting

confidence: 63%

“…In addition, other studies have associated GSK3 and Cdk5 activity with neurotoxic processes induced by the PrP peptide, a synthetic peptide widely used as a model of neurotoxicity in prion research (e.g., [20,21]). In parallel, PrP C may bind with several intracellular proteins including tubulin [22,23]. And more relevantly, Wang et al described physical interaction between tau and PrP C hypothesizing that the presence of phosphorylated tau in some TSEs is the result of a differential affinity between tau and the N-terminal octarepeat (OR)…”

Section: Introductionmentioning

confidence: 99%

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Role of PrPC Expression in Tau Protein Levels and Phosphorylation in Alzheimer’s Disease Evolution

et al. 2014

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Alzheimer's disease (AD) is characterized by the presence of amyloid plaques mainly consisting of hydrophobic -amyloid peptide (A) aggregates and neurofibrillary tangles (NFTs) composed principally of hyperphosphorylated tau. A oligomers have been described as the earliest effectors to negatively affect synaptic structure and plasticity in the affected brains, and cellular prion protein (PrP C ) has been proposed as receptor for these oligomers.The most widely accepted theory holds that the toxic effects of A are upstream of change in tau, a neuronal microtubule-associated protein that promotes the polymerization and stabilization of microtubules. However, tau is considered decisive for the progression of neurodegeneration, and indeed tau pathology correlates well with clinical symptoms such as dementia. Different pathways can lead to abnormal phosphorylation, and, as a consequence, tau aggregates into Paired Helical Filaments (PHF) and later on into NFTs.Reported data suggest a regulatory tendency of PrP C expression in the development of AD, and a putative relationship between PrP C and tau processing is emerging. However the role of tau/PrP C interaction in AD is poorly understood.In this study we show increased susceptibility to A derived diffusible ligands (ADDLs) in neuronal primary cultures from PrP C knock-out mice, compared to wild-type, which correlates with increased tau expression. Moreover, we found increased PrP C expression that paralleled with tau at early ages in an AD murine model, and in early Braak stages of AD in affected individuals. Taken together, these results suggest a protective role for PrP C in AD by down-regulating tau expression, and they point to this protein as being crucial in the molecular events that lead to neurodegeneration in AD.

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Section: Discussioncontrasting

confidence: 63%

Section: Introductionmentioning

confidence: 99%

Role of PrPC Expression in Tau Protein Levels and Phosphorylation in Alzheimer’s Disease Evolution

et al. 2014

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“…To date, the molecular mechanisms underlying prion pathology remain to be fully clarified (e.g., see (Aguzzi et al, 2008;Nicolas et al, 2009;Weissmann, 2004) for reviews). Most intracellular mechanisms in proteinopathies with amyloid deposits are expected to be similar (e.g., (Gaggelli et al, 2006)).…”

Section: Discussionmentioning

confidence: 99%

Involvement of Dab1 in APP processing and β-amyloid deposition in sporadic Creutzfeldt–Jakob patients

Gavı́n¹,

Ferrer²,

Rı́o³

2010

Neurobiology of Disease

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Alzheimer's disease and prion pathologies (e.g., Creutzfeldt-Jakob disease (CJD)) display profound neural lesions associated with aberrant protein processing and extracellular amyloid deposits. Dab1 has been implicated in the regulation of Amyloid Precursor Protein (APP), but a direct link between human prion diseases and Dab1/APP interactions has not been published. Here we examined this putative relationship in seventeen cases of sporadic CJD (sCJD) post mortem. Biochemical analyses of brain tissue revealed two groups, which also correlated with PrP sc types 1 and 2. One group, with PrP sc type 1 showed increased Dab1 phosphorylation, and lower CTF production with an absence of A deposition. The second sCJD group, which carried PrP sc type 2, showed lower levels of Dab1 phosphorylation and CTF production, and A deposition. Thus, the present observations suggest a correlation between Dab1-phosphorylation, A deposition and PrP sc type in sCJD.

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“…The success of the measures is evident from the dramatic decline in the incidence of BSE and, in recent years, the substantial reduction of ruminant TSE and human new vCJD cases. glycoprotein in the plasma membrane of cells, although its exact function is still unknown (Nicolas et al, 2009). Prion disease diagnosis can be accomplished by testing brain or lymphoid tissues for the presence of PrP Sc , which unlike PrP C is partially resistant to protease digestion.…”

Section: Introductionmentioning

confidence: 99%

Differentiation of ruminant transmissible spongiform encephalopathy isolate types, including bovine spongiform encephalopathy and CH1641 scrapie

Jacobs

Sauer

Keulen

et al. 2010

Journal of General Virology

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New insights into cellular prion protein (PrPc) functions: The “ying and yang” of a relevant protein

Abstract: The conversion of cellular prion protein (PrP c )

Cited by 51 publications

References 204 publications

Role of PrPC Expression in Tau Protein Levels and Phosphorylation in Alzheimer’s Disease Evolution

Role of PrPC Expression in Tau Protein Levels and Phosphorylation in Alzheimer’s Disease Evolution

Involvement of Dab1 in APP processing and β-amyloid deposition in sporadic Creutzfeldt–Jakob patients

Differentiation of ruminant transmissible spongiform encephalopathy isolate types, including bovine spongiform encephalopathy and CH1641 scrapie

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