scholarly journals Ablation of the cellular prion protein, PrPC, specifically on follicular dendritic cells has no effect on their maturation or function

Immunology ◽  
2013 ◽  
Vol 138 (3) ◽  
pp. 246-257 ◽  
Author(s):  
Laura McCulloch ◽  
Karen L. Brown ◽  
Neil A. Mabbott
2001 ◽  
Vol 306 (1) ◽  
pp. 49-55 ◽  
Author(s):  
Thielen C. ◽  
Mélot F. ◽  
Jolois O. ◽  
Leclercq F. ◽  
Tsunoda R. ◽  
...  

2001 ◽  
Vol 8 (3-4) ◽  
pp. 259-266 ◽  
Author(s):  
Caroline Thielen ◽  
Nadine Antoine ◽  
France Mélot ◽  
Jean-Yves Cesbron ◽  
Ernst Heinen ◽  
...  

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.


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 ◽  
...  

2006 ◽  
Vol 209 (4) ◽  
pp. 484-491 ◽  
Author(s):  
K Sasaki ◽  
K Doh-ura ◽  
JW Ironside ◽  
N Mabbott ◽  
T Iwaki

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