YES!!!! Thank You Beijing China!!! Super Day...super day.... Using Protein Misfolding Cyclic Amplification Generates a Highly Neurotoxic PrP Dimer Causing Neurodegeneration. ncbi.nlm.nih.gov/pubmed/23771785 J Mol Neurosci. 2013 Jun 16. [Epub ahead of print] Yang X, Yang L, Zhou X, Khan SH, Wang H, Yin X, Yuan Z, Song Z, Wu W, Zhao D. Source State Key Laboratories for Agrobiotechnology, Key Lab of Animal Epidemiology and Zoonosis, Ministry of Agriculture, National Animal Transmissible Spongiform Encephalopathy Laboratory, College of Veterinary Medicine, China Agricultural University, Beijing, 100193, China. Abstract Under the "protein-only" hypothesis, prion-based diseases are proposed to result from an infectious agent that is an abnormal isoform of the prion protein in the scrapie form, PrPSc. However, since PrPSc is highly insoluble and easily aggregates in vivo, this view appears to be overly simplistic, implying that the presence of PrPSc may indirectly cause neurodegeneration through its intermediate soluble form. We generated a neurotoxic PrP dimer with partial pathogenic characteristics of PrPSc by protein misfolding cyclic amplification in the presence of 1-palmitoyl-2-oleoylphosphatidylglycerol consisting of recombinant hamster PrP (23-231). After intracerebral injection of the PrP dimer, wild-type hamsters developed signs of neurodegeneration. Clinical symptoms, necropsy findings, and histopathological changes were very similar to those of transmissible spongiform encephalopathies. Additional investigation showed that the toxicity is primarily related to cellular apoptosis. All results suggested that we generated a new neurotoxic form of PrP, PrP dimer, which can cause neurodegeneration. Thus, our study introduces a useful model for investigating PrP-linked neurodegenerative mechanisms.
Posted on: Wed, 19 Jun 2013 17:27:21 +0000
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