Expression of PrPC in the rat brain and characterization of a subset of cortical neurons

Moleres, Francisco J.; Velayos, J. L.

doi:10.1016/j.brainres.2005.06.067

Cited by 25 publications

(19 citation statements)

References 61 publications

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“…Presence of PrP in the glial cells, astrocytes and oligodendrocytes, has been reported in normal mammalian brains in immunohistochemical and in situ hydridization studies (Moser et al, 1995;Lainé et al, 2001;Ford et al, 2002;Moleres and Velayos, 2005). This finding differs from that of the present study.…”

Section: Prp Localization In Birds and Technical Considerationscontrasting

confidence: 85%

“…Ultrastructurally, immunoreactivity in the molecular layer is observed in the axolemma of parallel fibers and basket cells, presynaptic plasmalemma, and plasmalemma of Bergmann glial cells (Lainé et al, 2001;Bailly et al, 2004). In contrast, Moleres and Velayos (2005) reported PrP immunoreactivity in the somata of Purkinje cells, but not in the molecular layer of the rat cerebellum. This variable immunostaining is probably due to the regulation of protein translation (Ford et al, 2002;Bailly et al, 2004).…”

Section: Prp Localization In Birds and Technical Considerationsmentioning

confidence: 72%

“…For example, in the cerebellar cortex, although the cell bodies of Bergmann glial cells did not stain with a monoclonal antibody that recognizes C-terminal residues 158-174 of PrP by light microscopy, immunoelectron microscopy showed immunoreactivity in their plasmalemma located in the molecular layer (Lainé et al, 2001). Other immunohistochemical studies conducted to determine the presence of PrP failed to show staining in Bergmann glial cells (Moser et al, 1995;Liu et al, 2001;Bailly et al, 2004;Moleres and Velayos, 2005). Ford et al (2002) reported that Bergmann glial cells do not express PrP mRNA in mice.…”

Section: Prp Localization In Birds and Technical Considerationsmentioning

confidence: 90%

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Distribution of the cellular prion protein in the central nervous system of the chicken

Atoji

Ishiguro

2009

Journal of Chemical Neuroanatomy

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Section: Prp Localization In Birds and Technical Considerationscontrasting

confidence: 85%

Section: Prp Localization In Birds and Technical Considerationsmentioning

confidence: 72%

Section: Prp Localization In Birds and Technical Considerationsmentioning

confidence: 90%

See 1 more Smart Citation

Distribution of the cellular prion protein in the central nervous system of the chicken

Atoji

Ishiguro

2009

Journal of Chemical Neuroanatomy

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“…In prion diseases, neuroglial cells appear to be potential reservoirs of infectivity. The presence of PrP C in glial cells has been demonstrated both in vivo (Moleres and Velayos 2005) and in vitro (Archer et al 2004). Additional data suggest that astrocytes are among the targets for the scrapie agent in the CNS (Manuelidis et al 1987;Lazarini et al 1994;Titeux et al 2002), with EGCs likely playing a similar role in ENS plexuses from spontaneously and experimentally scrapie-infected sheep (Chiocchetti et al 2005;Marruchella et al 2006).…”

mentioning

confidence: 99%

Nitric Oxide Synthase Immunoreactivity and NADPH-d Histochemistry in the Enteric Nervous System of Sarda Breed Sheep With Different PrP Genotypes in Whole-mount and Cryostat Preparations

Lalatta-Costerbosa

Mazzoni

Clavenzani

et al. 2006

J Histochem Cytochem.

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Until now, significant differences in the neurochemical pattern of enteric neurons have been demonstrated in all species studied; however, some strong similarities also occur across species, such as the occurrence of nitric oxide synthase immunoreactivity (NOS-IR) in inhibitory motor neurons to muscle. In consideration of the insufficient data regarding the enteric nervous system (ENS) of sheep, we investigated the myenteric plexus and submucosal plexus of the ovine ileum. Since the pivotal role of the ENS in the early pathogenesis of sheep scrapie, the “prototype” of prion diseases, has been suggested, we have focused our observations also on the host's PrP genotype. We have studied the morphology and distribution of NOS-IR neurons and their relationships with the enteric glia in whole-mount preparations and in cryostat sections. NOS-IR neurons, always encircled by glial processes, were located in both plexuses. Many NOS-IR fibers were seen in the circular muscle layer, in the submucosa, and in the mucosa. In the submucosa they were close to the lymphoid tissue. No differences in the distribution and percentage of NOS-IR fibers and neurons were observed among sheep carrying different PrP genotype, thus making unlikely their contribution in the determinism of susceptibility/resistance to scrapie infection.

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“…The cellular prion protein (PrP C ) is a glycosylphosphatidylinositol (GPI)-anchored cell surface protein highly expressed by neurons and glial cells in the adult central nervous system (CNS) [1][2][3]. Its physiological functions are poorly understood but a relation between the protein and neuroprotection has been reported [4].…”

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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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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Expression of PrPC in the rat brain and characterization of a subset of cortical neurons

Cited by 25 publications

References 61 publications

Distribution of the cellular prion protein in the central nervous system of the chicken

Distribution of the cellular prion protein in the central nervous system of the chicken

Nitric Oxide Synthase Immunoreactivity and NADPH-d Histochemistry in the Enteric Nervous System of Sarda Breed Sheep With Different PrP Genotypes in Whole-mount and Cryostat Preparations

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

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