scholarly journals Human FDC express PrPcinvivoandinvitro

2001 ◽  
Vol 8 (3-4) ◽  
pp. 259-266 ◽  
Author(s):  
Caroline Thielen ◽  
Nadine Antoine ◽  
France Mélot ◽  
Jean-Yves Cesbron ◽  
Ernst Heinen ◽  
...  
Keyword(s):  
Dendritic Cells ◽  
Prion Protein ◽  
Neurodegenerative Disorders ◽  
Prion Diseases ◽  
Cellular Prion Protein ◽  
Follicular Dendritic Cells ◽  
Germinal Centres ◽  
Peripheral Infection ◽  
Follicular Dendritic ◽  
Enzymatic Procedure

Prion diseases are fatal neurodegenerative disorders caused by accumulation of abnormal prion protein (protease-resistant prion, PrPres). PrPres accumulation is also detected in lymphoid organs after peripheral infection. Several studies suggest that follicular dendritic cells (FDC) could be the site of PrPres retention and amplification.Here we show that human follicular dendritic cells can express normal cellular prion protein (PrPc) bothinsituandinvitro. When tonsillar cryosections were treated with anti-PrP antibody, the label was found on some very delicate cell extensions inside the lymphoid follicles, especially in the germinal centres. These extensions react with DRC1 antibody, used frequently to label FDC. Other structures labelled with anti-PrP antibody were the keratinocytes.To confirm the ability of FDC to synthesise PrPc, we isolated FDC by a non-enzymatic procedure and cultured them. By cytochemistry and flow cytometry it was clearly shown that FDC do produce PrPc.

Isolation of bovine follicular dendritic cells allows the demonstration of a particular cellular prion protein

2001 ◽  
Vol 306 (1) ◽  
pp. 49-55 ◽  
Author(s):  
Thielen C. ◽  
Mélot F. ◽  
Jolois O. ◽  
Leclercq F. ◽  
Tsunoda R. ◽  
...  
Keyword(s):  
Dendritic Cells ◽  
Prion Protein ◽  
Cellular Prion Protein ◽  
Follicular Dendritic Cells ◽  
Follicular Dendritic

scholarly journals Prion protein and prion disease at a glance

2021 ◽  
Vol 134 (17) ◽  
Author(s):  
Caihong Zhu ◽  
Adriano Aguzzi
Keyword(s):  
Prion Protein ◽  
Prion Disease ◽  
Neurodegenerative Disorders ◽  
Prion Diseases ◽  
Amyloid Β ◽  
Cellular Prion Protein ◽  
Future Studies ◽  
Associated Proteins ◽  
Main Component ◽  
Conformational Conversion

ABSTRACT Prion diseases are neurodegenerative disorders caused by conformational conversion of the cellular prion protein (PrPC) into scrapie prion protein (PrPSc). As the main component of prion, PrPSc acts as an infectious template that recruits and converts normal cellular PrPC into its pathogenic, misfolded isoform. Intriguingly, the phenomenon of prionoid, or prion-like, spread has also been observed in many other disease-associated proteins, such as amyloid β (Aβ), tau and α-synuclein. This Cell Science at a Glance and the accompanying poster highlight recently described physiological roles of prion protein and the advanced understanding of pathogenesis of prion disease they have afforded. Importantly, prion protein may also be involved in the pathogenesis of other neurodegenerative disorders such as Alzheimer's and Parkinson's disease. Therapeutic studies of prion disease have also exploited novel strategies to combat these devastating diseases. Future studies on prion protein and prion disease will deepen our understanding of the pathogenesis of a broad spectrum of neurodegenerative conditions.

Scrapie replication in lymphoid tissues depends on prion protein-expressing follicular dendritic cells

10.1038/15264 ◽  
1999 ◽  
Vol 5 (11) ◽  
pp. 1308-1312 ◽  
Author(s):  
K.L. Brown ◽  
K. Stewart ◽  
D.L. Ritchie ◽  
N.A. Mabbott ◽  
A. Williams ◽  
...  
Keyword(s):  
Dendritic Cells ◽  
Prion Protein ◽  
Lymphoid Tissues ◽  
Follicular Dendritic Cells ◽  
Follicular Dendritic

scholarly journals Prion protein and its role in signal transduction

2013 ◽  
Vol 18 (2) ◽  
Author(s):  
Alessandro Didonna
Keyword(s):  
Signal Transduction ◽  
Prion Protein ◽  
Neurodegenerative Disorders ◽  
Physiological Function ◽  
Prion Diseases ◽  
Etiologic Agent ◽  
Cellular Prion Protein ◽  
Considerable Effort ◽  
Unique Nature ◽  
First Time

AbstractPrion diseases are a class of fatal neurodegenerative disorders that can be sporadic, genetic or iatrogenic. They are characterized by the unique nature of their etiologic agent: prions (PrPSc). A prion is an infectious protein with the ability to convert the host-encoded cellular prion protein (PrPC) into new prion molecules by acting as a template. Since Stanley B. Prusiner proposed the “protein-only” hypothesis for the first time, considerable effort has been put into defining the role played by PrPC in neurons. However, its physiological function remains unclear. This review summarizes the major findings that support the involvement of PrPC in signal transduction.

scholarly journals Protease-sensitive prion species in neoplastic spleens of prion-infected mice with uncoupling of PrPSc and prion infectivity

2013 ◽  
Vol 94 (2) ◽  
pp. 453-463 ◽  
Author(s):  
Susanne Krasemann ◽  
Melanie Neumann ◽  
Beata Szalay ◽  
Carol Stocking ◽  
Markus Glatzel
Keyword(s):  
Neurodegenerative Disorders ◽  
Prion Diseases ◽  
Biochemical Properties ◽  
Cellular Prion Protein ◽  
Follicular Dendritic Cells ◽  
Tissue Architecture ◽  
Common Component ◽  
Prion Infectivity ◽  
The Impact ◽  
Diagnostic Criterion

Prion diseases are fatal neurodegenerative disorders. An important step in disease pathophysiology is the conversion of cellular prion protein (PrPC) to disease-associated misfolded conformers (PrPSc). These misfolded PrP variants are a common component of prion infectivity and are detectable in diseased brain and lymphoreticular organs such as spleen. In the latter, PrPSc is thought to replicate mainly in follicular dendritic cells within spleen follicles. Although the presence of PrPSc is a hallmark for prion disease and serves as a main diagnostic criterion, in certain instances the amount of PrPSc does not correlate well with neurotoxicity or prion infectivity. Therefore, it has been proposed that prions might be a mixture of different conformers and aggregates with differing properties. This study investigated the impact of disruption of spleen architecture by neoplasia on the abundance of different PrP species in spleens of prion-infected mice. Although follicular integrity was completely disturbed, titres of prion infectivity in neoplastic spleens were not significantly altered, yet no protease-resistant PrPSc was detectable. Instead, unique protease-sensitive prion species could be detected in neoplastic spleens. These results indicate the dissociation of PrPSc and prion infectivity and showed the presence of non-PrPSc PrP species in spleen with divergent biochemical properties that become apparent after tissue architecture disruption.

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