Translocation of cellular prion protein to non-lipid rafts protects human prion-mediated neuronal damage
نویسندگان
چکیده
منابع مشابه
The Molecular Basis of Prion Protein-mediated Neuronal Damage
The most seductive questions in prion biology have always centered around the unusual nature of disease transmissibility1,2. What is the transmissible agent? What are the routes of transmission from one organism to another? How does the transmissible agent spread within an organism? What is the mechanism of replication? What is the nature of the barrier to transmission between species? Although...
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The cellular form of the prion protein (PrP(C)) is a normal constituent of neuronal cell membranes. The protein misfolding causes rare neurodegenerative disorders known as transmissible spongiform encephalopathies or prion diseases. These maladies can be sporadic, genetic or infectious. Sporadic prion diseases are the most common form mainly affecting aging people. In this work, we investigate ...
متن کاملThe role of lipid rafts in prion protein biology.
The conformational conversion of the cellular prion protein, PrP(C), to the misfolded isoform PrP(Sc )is the central pathogenic event in the uniquely transmissible neurodegenerative prion diseases. As both PrP(C) and PrP(Sc) are associated with membranes, the nature of the membrane microenvironment may well play a significant role in both the conformational conversion process as well as the nor...
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The function of the cellular prion protein (PrP) is still poorly understood. We present here an unprecedented role for PrP against Bax-mediated neuronal apoptosis and show that PrP potently inhibits Bax-induced cell death in human primary neurons. Deletion of four octapeptide repeats of PrP (PrPDeltaOR) and familial D178N and T183A PrP mutations completely or partially eliminate the neuroprotec...
متن کاملCellular prion protein in blood platelets associates with both lipid rafts and the cytoskeleton.
The recently shown transmissibility of variant Creutzfeldt-Jakob disease (vCJD) by blood transfusion emphasises the need for better understanding of the cellular prion protein (PrPc) in blood. A substantial amount of cell-associated PrPc in blood resides in platelets. Platelet activation leads to up-regulation of PrPc on the platelet surface and its release on exosomes and microparticles. The s...
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ژورنال
عنوان ژورنال: International Journal of Molecular Medicine
سال: 2011
ISSN: 1107-3756,1791-244X
DOI: 10.3892/ijmm.2011.864