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Kinetics of expression of prion protein in uninfected and scrapie‐infected N 2 a mouse neuroblastoma cells
Author(s) -
Pfeifer Karin,
Bachmann Michael,
Schröder Heinz C.,
Forrest Jock,
Müller Werner E. G.
Publication year - 1993
Publication title -
cell biochemistry and function
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.933
H-Index - 61
eISSN - 1099-0844
pISSN - 0263-6484
DOI - 10.1002/cbf.290110102
Subject(s) - scrapie , nucleolus , microbiology and biotechnology , messenger rna , gene isoform , biology , prion protein , complementary dna , gene expression , rna , blot , immunocytochemistry , transcription (linguistics) , gene , cell , nucleus , cell culture , biochemistry , genetics , medicine , linguistics , philosophy , disease , pathology , endocrinology
The scrapie prion protein, PrP Sc , is formed from its isoform, the cellular PrP c . There is evidence available indicating that PrP Sc is necessary component of the infectious prion particle to cause a series of transmissible spongiform encephalopathies. We have used immunocytochemistry and RNA blotting techniques to investigate if infection with prions results in an increased PrP gene expression. For the experiments we used N 2 a cells which had been infected with prions (ScN 2 a cells). We demonstrated by confocal laser scanning microscopy that PrP‐protein was present in the nucleus (predominantly in the nucleoli) of ScN 2 a cells. Analysis of the PrP‐mRNA levels both in N 2 a‐ and in ScN 2 a cells using cDNA encoding PrP c revealed no marked alteration of the mRNA steady state level between the two cell strains. Likewise, in run‐off experiments no changes in either PrP‐specific transcription or in general transcriptional activity were found. The half‐life of PrP‐mRNA was found to be identical in both cell strains (7 h). Taken together, these results show that PrP Sc and /or PrP c is present in the nucleus (nucleoli) of ScN 2 a cells but does not display and effect on the expression of the PrP gene.