Abstract:
:The conversion of the endogenous cellular prion protein to an abnormally folded isoform is a hallmark of transmissible spongiform encephalopathies. It occurs when a misfolded prion protein contacts the cellular PrP. Among the molecular partners suggested to be involved in the misfolding process, the glycosaminoglycans seem to be good candidates. The present study was aimed to examine a possible link between PrP conversion efficiency and transcript level of Chst8 gene that encodes the carbohydrate N-acetylgalactosamine 4-O-sulfotransferase 8. Mov cells expressing ovine PrP were transfected with shRNA directed against Chst8 transcripts. Resulting clones were characterized for their Chst8 and Prnp transcript levels, and for their content in sulfated glycosaminoglycans, more particularly sulfated chondroitins. Unexpectedly, the decreased amount of Chst8 transcript induced an increase of the chondroitin sulfate percentage among total GAGs, with an increased amount of 4-O-sulfation of GalNAc residues. Upon to infection by a sheep prion, a slight amount of PrP(Sc) was observed, which rapidly disappeared upon subpassaging. Together, these findings indicate that the Chst8 transcript level affects the glycosaminoglycan environment of the cellular prion protein, and as a consequence its ability for conversion into PrP(Sc).
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Martin R,Chantepie S,Chapuis J,Le-Duc A,Maftah A,Papy-Garcia D,Laude H,Petit JM,Gallet PFdoi
10.1016/j.bbrc.2011.09.126subject
Has Abstractpub_date
2011-10-28 00:00:00pages
587-91issue
3eissn
0006-291Xissn
1090-2104pii
S0006-291X(11)01741-4journal_volume
414pub_type
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