Prion proteins interaction with

Ermonval M, Baudry A, Baychelier F et al (2009) The cellular prion protein interacts with the tissue non-specific alkaline phosphatase in membrane microdomains of bioami-nergic neuronal cells. PLoS One 4 e6497... 

Granic 1, Dolga AM, Nijholt IM, van Dijk G, Eisel UL (2009) Inflammation and NF-kappaB in Alzheimer s disease and diabetes. J Alzheimers Dis 16 809-821 Grossman A, Zeiler B, Sapirstein V (2003) Prion protein interactions with nucleic acid possible models for prion disease and prion fimction. Neurochem Res 28 955-963 Guan Z, Sdderberg M, Sindelar P, Pmsiner SB, Kristensson K, Dallner G (1996) Lipid composition in scrapie-infected mouse brain prion infection increases the levels of dolichyl phosphate and ubiquinone. J Neurochem 66 277-285... 

Other phenomena. Prion proteins, the mutated forms of which cause Creutzfeldt-Jacob disease, also appear to interact with metal ions. Spectra of Cu(H) bound to various mutant proteins have indicated anomalous binding behaviour.331 Hydroxyl radical generation during the interaction of mutant forms of a prion protein fragment with Fe(II) has also been reported.332... 

The role of copper in other disease states is being investigated. For Alzheimer s disease studies, it has been found that the amyloid precursor protein interacts with copper to produce increased oxidant damage, and trace amounts of copper promote the precipitation of the amyloid p protein. In familial myotrophic lateral sclerosis about a quarter of the cases are caused by inherited dominant mutations in the Cu/Zn superoxide dismutase that probably result in abnormal Cu binding and the generation of reactive oxygen species. Copper has also been proposed to be involved in prion metabolism and fimction however, whether or not this imphcates copper in the prion diseases is unclear at this time. ... 

Prions—protein particles that lack nucleic acid— cause fatal transmissible spongiform encephalopathies such as Creutzfeldt-Jakob disease, scrapie, and bovine spongiform encephalopathy. Prion diseases involve an altered secondary-tertiary strucmre of a namrally occurring protein, PrPc. When PrPc interacts with its pathologic isoform PrPSc, its conformation is transformed from a predominantly a-helical strucmre to the P-sheet strucmre characteristic of PrPSc. 

Edskes, H. K., and Wickner, R. B. (2002). Conservation of a portion of the S. cerevisiae Ure2p prion domain that interacts with the full-length protein. Proc. Natl. Acad. Sci. USA 99(Suppl. 4), 16384-16391. 

When the abnormal prion interacts with the normal version of the protein on the membranes of nerve cells, the abnormal protein somehow induces the normal molecules to change their shape. This is the part of the process we know the least about. 

Nieznanski K (2010) Interactions of prion protein with intracellular proteins so many partners and no consequences Cell Mol Neurobiol 30 653-666... 

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