Reference : Do Bovine Lymphocytes Express a Peculiar Prion Protein?
Scientific journals : Article
Life sciences : Veterinary medicine & animal health
Life sciences : Anatomy (cytology, histology, embryology...) & physiology
http://hdl.handle.net/2268/7135
Do Bovine Lymphocytes Express a Peculiar Prion Protein?
English
Mélot, France mailto [Université de Liège - ULg > Services généraux (Faculté de médecine) > Service administratif de la Faculté (Médecine) >]
Thielen, Caroline mailto [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Anatomie et cytologie pathologiques >]
Labiet, T. [> > > >]
Eisher, S. [> > > >]
Jolois, Olivier mailto [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Histologie humaine >]
Heinen, Ernst mailto [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Histologie humaine >]
Antoine, Nadine mailto [Université de Liège - ULg > Département de morphologie et pathologie > Histologie >]
Dec-2002
Developmental Immunology
9
4
245-52
Yes (verified by ORBi)
International
1044-6672
[en] Blotting, Western ; Blotting, Western ; Cattle/immunology ; Cells, Cultured ; Encephalopathy, Bovine Spongiform/immunology ; Flow Cytometry ; Glycosylation ; Lymphocyte Activation ; Lymphocyte Subsets/metabolism ; Lymphoid Tissue/metabolism ; PrPC Proteins/metabolism ; Protein Isoforms/metabolism
[en] The cellular prion protein (PrPc) is a glycolipid-anchored cell surface protein that usually exhibits three glycosylation states. Its post-translationally modified isoform, PrPsc, is involved in the pathogenesis of various transmissible spongiform encephalopathies (TSEs). In bovine species, BSE infectivity appears to be restricted to the central nervous system; few or no detectable infectivity is found in lymphoid tissues in contrast to scrapie or variant CJD. Since expression of PrPc is a prerequisite for prion replication, we have investigated PrPc expression by bovine immune cells. Lymphocytes from blood and five different lymph organs were isolated from the same animal to assess intra- and interindividual variability of PrPc expression, considering six individuals. As shown by flow cytometry, this expression is absent or weak on granulocytes but is measurable on monocytes, B and T cells from blood and lymph organs. The activation of the bovine cells produces an upregulation of PrPc. The results of our in vitro study of PrPc biosynthesis are consistent with previous studies in other species. Interestingly, western blotting experiments showed only one form of the protein, the diglycosylated band. We propose that the glycosylation state could explain the lack of infectivity of the bovine immune cells.
http://hdl.handle.net/2268/7135

File(s) associated to this reference

Fulltext file(s):

FileCommentaryVersionSizeAccess
Restricted access
Mélot.pdfAuthor preprint300.35 kBRequest copy

Bookmark and Share SFX Query

All documents in ORBi are protected by a user license.