Prion proteins interaction

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... 

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. 

Horiuchi, M., Baron, G. S., Xiong, L. W., and Caughey, B. (2001). Inhibition of interactions and interconversions of prion protein isoforms by peptide fragments from the C-terminal folded domain./. Biol. Chem. 276, 15489-15497. 

ACE has been used to characterize protein-sugar interactions,45 DNA binding to an anti-DNA monoclonal antibody,46 antibody-antigen47 antisteroidal inflammatory drugs,48 and prion protein in sheep brain preparations.49... 

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... 

In inherited forms of prion diseases, a mutation in the gene encoding PrP produces a change in one amino acid residue that is believed to make the conversion of PrPG to PrPSc more likely. A complete understanding of prion diseases awaits new information about how prion protein affects brain function. Structural information about PrP is beginning to provide insights into the molecular process that allows the prion proteins to interact so as to alter their conformation (Fig. 2). 

ESiverstahl, H., A. Andersson, A. Graslund and L. Maler (2004) NMR solution structure and membrane interaction of the N-terminal sequence (1-30) of the bovine prion protein. Biochemistry 43, 14940-14947. 

Thus, exposure to UV light causes perturbation of the N-terminal region of prion protein (which has seven out of eight tryptophans) and leads to amorphous aggregation. Noncovalent interactions play a predominant role in the photo-aggregation of prion protein [3],... 

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. ... 

Freir DB, Nicoll AJ, Klyubin I, Panico S, Me Donald JM, Risse E et al (2011) Interaction between prion protein and toxic amyloid p assemblies can be therapeutically targeted at multiple sites. Nat Commun 2 336... 

The pathogenesis of another well-known neurodegenerative disease (Jacob Creutzfeld disease) seems to be strongly linked to the presence of prion proteins in the brain. These macromolecules contain multiple Met residues, some of them in close vicinity. Such structure should favour stabilization of MetS as intramolecular (S.-.S) complexes. Since weak intramolecular non-bonded S O and S N interactions have been recently suggested in proteins [14], stabilization of MetS +through formation of S.-.N- and/or S.-.O-complexes might potentially accelerate oxidation processes in proteins.The first experimental evidence... 

M. Horiuchi, S. A. Priola, J. Chabry, et al. Interactions between heterologous fortms of prion protein binding, inhibition of conversion, and species barriers. Proceedings of the Society of National Academy of Sciences (USA) 97,5836 (2000). 

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

Telling GC, Haga T, Torchia M, Tremblay P, DeArmond SJ, Prusiner SB (1996) Interactions between wild-type and mutant prion proteins modulate neurodegeneration in transgenic mice. Genes Dev 10 1736-1750... 

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