By Stanley B. Prusiner (auth.), Mathias Jucker, Yves Christen (eds.)
The misfolding and aggregation of particular proteins is an early and compulsory occasion in lots of of the age-related neurodegenerative illnesses of people. The preliminary explanation for this pathogenic cascade and the capacity wherein disorder spreads throughout the frightened method, stay doubtful. a contemporary surge of study, first instigated by means of pathologic similarities among prion ailment and Alzheimer’s sickness, more and more implicates the conversion of disease-specific proteins into an aggregate-prone b-sheet-rich country because the top mover of the neurodegenerative technique. This prion-like corruptive protein templating or seeding now characterizes such clinically and etiologically different neurological problems as Alzheimer´s disorder, Parkinson’s illness, Huntington’s affliction, amyotrophic lateral sclerosis, and frontotemporal lobar degeneration. realizing the misfolding, aggregation, trafficking and pathogenicity of the affected proteins might accordingly demonstrate common pathomechanistic ideas for essentially the most devastating and intractable human mind problems. it's time to settle for that the prion inspiration isn't any longer limited to prionoses yet is a promising idea for the knowledge and remedy of a striking number of illnesses that afflict basically our getting older society.
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Additional resources for Proteopathic Seeds and Neurodegenerative Diseases
Pmel17 amyloids serve as a template for ligand binding (Fowler et al. 2006), whereas other amyloids induce a specific toxic response, as shown for the HET-s prion system (Maddelein et al. 2002). The structural repetitiveness of the amyloid fiber provides an ideal template for making it into a transmissible or infectious fold. In fact, most prions (infectious proteins) have been found in their infectious form to be amyloids whereas the amyloid structure itself appears to be responsible for prion strain diversity (Toyama et al.
2008). Fibrils formed by the fungal prion protein HET-s have been shown to have a “pseudo-in-register” structure, in which homologous segments align with one another in parallel β-sheets (Van Melckebeke et al. 2010). Thus, the in-register, parallel β-sheet organization predominates in biologically relevant fibrils. In addition to Aβ34–42, several other short Aβ fragments have been shown by solid state NMR to form fibrils containing antiparallel β-sheets (Balbach et al. 2000; Bu et al. 2007; Kammerer et al.
The complexity of its structure reflects its evolutionarily optimized role as an amyloid. The β-solenoid structure is not a chance misfolding of the PFD but rather a very stable conformation that can spontaneously occur at moderate protein concentration. The presence of a pseudo-repeat in the sequence allows a single PFD to adopt two turns of the β-solenoid, forming the nucleus of the amyloid fold. As well, it gives rise to alternating charges along the fibril axis that support the correct in-register alignment of the β-sheets (Fig.