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Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-1909

Parizek, P; Roeckl, C; Weber, J; Flechsig, E; Aguzzi, A; Raeber, A J (2001). Similar turnover and shedding of the cellular prion protein in primary lymphoid and neuronal cells. Journal of Biological Chemistry, 276(48):44627-44632.

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Abstract

The cellular prion protein (PrP(C)) is essential for pathogenesis and transmission of prion diseases. Although prion replication in the brain is accompanied by neurodegeneration, prions multiply efficiently in the lymphoreticular system without any detectable pathology. We have used pulse-chase metabolic radiolabeling experiments to investigate the turnover and processing of PrP(C) in primary cell cultures derived from lymphoid and nervous tissues. Similar kinetics of PrP(C) degradation were observed in these tissues. This indicates that the differences between these two organs with respect to their capacity to replicate prions is not due to differences in the turnover of PrP(C). Substantial amounts of a soluble form of PrP that lacks the glycolipid anchor appeared in the medium of splenocytes and cerebellar granule cells. Soluble PrP was detected in murine and human serum, suggesting that it might be of physiological relevance.

Item Type:Journal Article, refereed
Communities & Collections:04 Faculty of Medicine > University Hospital Zurich > Institute of Neuropathology
DDC:570 Life sciences; biology
610 Medicine & health
Language:English
Date:30 November 2001
Deposited On:11 Feb 2008 12:26
Last Modified:27 Nov 2013 21:38
Publisher:American Society for Biochemistry and Molecular Biology
ISSN:0021-9258
Publisher DOI:10.1074/jbc.M107458200
PubMed ID:11571302
Citations:Web of Science®. Times Cited: 51
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