Involvement of Macrophages in the Pathogenesis of Transmissible Spongiform Encephalopathies

Béringue, Vincent; Couvreur, Patrick; Dormont, Dominique

doi:10.1080/10446670290030981

Cited by 12 publications

(8 citation statements)

References 56 publications

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“…Two independent studies have shown that macrophages reduced prion infectivity during early infection (71,72), probably by degrading infectious prions. In a more recent study, it was found that mice deprived of TLR-4 developed accelerated scrapie, irrespective of which prion strain was injected and whether prions had been inoculated i.c.…”

Section: Discussionmentioning

confidence: 99%

Adoptive Transfer of T Lymphocytes Sensitized against the Prion Protein Attenuates Prion Invasion in Scrapie-Infected Mice

Gourdain

Grégoire

Iken

et al. 2009

The Journal of Immunology

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There is to date no effective way of preventing or curing neurodegenerative diseases such as Alzheimer disease or transmissible spongiform encephalopathies. The idea of treating those conditions by immunological approaches has progressively emerged over the last ten years. Encouraging results have been reported in Alzheimer disease and in peripheral forms of mouse prion diseases following passive injection of Abs or active immunization against the peptides or proteins presumably at the origin of those disorders. Still, major difficulties persist due to some characteristics of those conditions such as slow evolution, brain location, uncertainties regarding precise pathogenic pathways, and, above all, the fact that the target Ag is self, meaning that it is poorly immunogenic and potentially harmful if tolerance was transgressed. To analyze some of those difficulties, we are developing adoptive cell transfer approaches. In this study, lymphocytes sensitized against the prion protein in nontolerant Prnp−/− mice were transferred into histocompatible wild-type recipients which were partly or totally devoid of their own lymphocytes. Under such conditions, we found that the engrafted T lymphocytes resisted peripheral tolerance, remained reactive for several months against epitopes of the prion protein, and significantly attenuated the progression of prions in secondary lymphoid organs with subsequent delay in the evolution of the neurological disease. Interestingly, those protective T lymphocytes secreted lymphokines and migrated more readily into the host CNS but did not appear to be engaged in cooperation with host B cells for Ab production.

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Section: Discussionmentioning

confidence: 99%

Adoptive Transfer of T Lymphocytes Sensitized against the Prion Protein Attenuates Prion Invasion in Scrapie-Infected Mice

Gourdain

Grégoire

Iken

et al. 2009

The Journal of Immunology

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“…1992; Jeffrey et al . 2000; Klein and Aguzzi 2000; Aucouturier and Carnaud 2002; Beringue et al . 2002; Perry et al .…”

Section: Signaling In the Immune Systemmentioning

confidence: 99%

PrP^c on the road: trafficking of the cellular prion protein

Prado¹,

Silva²,

Magalhães³

et al. 2004

Journal of Neurochemistry

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“…Prion diseases or transmissible spongiform encephalopathies (TSEs) are neurodegenerative disorders that are characterized by loss of motor control, dementia, central nervous system (CNS) spongiosis, and microglial activation (1,2).…”

Section: Introductionmentioning

confidence: 99%

Lactoferrin protects against prion protein-induced cell death in neuronal cells by preventing mitochondrial dysfunction

Park

Jeong

Lee

et al. 2012

International Journal of Molecular Medicine

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Prion disorder-related neurodegenerative diseases are characterized by the accumulation of prion protein (PrP) scrapie isoform (PrPsc) within the central nervous system. PrPsc induces neuronal cell death by increasing intracellular generation of reactive oxygen species (ROS). Lactoferrin (LF) is an 80 kDa protein, which has antioxidant abilities due to the scavenging of ROS. The effects of LF treatment on PrP (106-126)-mediated neurotoxicity and ROS generation were the focus of this study. LF treatment protected against PrP (106-126)-induced neuronal cell death and decreased ROS generation. The reduced ROS generation prevented PrP (106-126)-induced mitochondrial dysfunction. Moreover, PrP (106-126)-induced protein activation including c-Jun N-terminal kinase and caspase-3 were blocked by LF treatment. These results demonstrated that LF protects neuronal cells against PrP (106-126)-mediated neurotoxicity through the scavenging of ROS and provide evidence that LF treatment prevents neuronal cell death caused by PrP (106-126).

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Involvement of Macrophages in the Pathogenesis of Transmissible Spongiform Encephalopathies

Cited by 12 publications

References 56 publications

Adoptive Transfer of T Lymphocytes Sensitized against the Prion Protein Attenuates Prion Invasion in Scrapie-Infected Mice

Adoptive Transfer of T Lymphocytes Sensitized against the Prion Protein Attenuates Prion Invasion in Scrapie-Infected Mice

PrP^c on the road: trafficking of the cellular prion protein

Lactoferrin protects against prion protein-induced cell death in neuronal cells by preventing mitochondrial dysfunction

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Involvement of Macrophages in the Pathogenesis of Transmissible Spongiform Encephalopathies

Cited by 12 publications

References 56 publications

Adoptive Transfer of T Lymphocytes Sensitized against the Prion Protein Attenuates Prion Invasion in Scrapie-Infected Mice

Adoptive Transfer of T Lymphocytes Sensitized against the Prion Protein Attenuates Prion Invasion in Scrapie-Infected Mice

PrPc on the road: trafficking of the cellular prion protein

Lactoferrin protects against prion protein-induced cell death in neuronal cells by preventing mitochondrial dysfunction

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Product

Resources

About

PrP^c on the road: trafficking of the cellular prion protein