Abnormal prion proteins

Tracing conformational transition of abnormal prion proteins during interspecies transmission by using novel antibodies.

Conformational differences in abnormal prion proteins (PrP(Sc)) have been postulated to produce different prion phenotypes. During the interspecies transmission of prions, the conformation of PrP(Sc) may change with passage; however, little is known about the mechanism of PrP(Sc) transition. In this study, novel PrP(Sc)-specific monoclonal antibodies (mAbs) were developed that could detect the ...

Prions and prion-like proteins.

Prions are self-replicating protein aggregates and are the primary causative factor in a number of neurological diseases in mammals. The prion protein (PrP) undergoes a conformational transformation leading to aggregation into an infectious cellular pathogen. Prion-like protein spreading and transmission of aggregates between cells have also been demonstrated for other proteins associated with ...

Prion Proteins and Sleep Disturbances

Prions normally exist as cellular membrane proteins. In humans, 209 amino acids with one disulfide bond form a primarily alpha-helical prion protein structure with a molecular mass of 35 to 36 kDa. The specific role and function of the prion protein elude research efforts and remains a controversial topic. Misfolding of the native prion protein leads to a protein structure with increased propor...

Neuronal Autophagy and Prion Proteins

Prion proteins leading to neurodegeneration.

Prion diseases are fatal neurodegenerative disorders related to the conformational alteration of the prion protein (PrP C) into a pathogenic and protease-resistant isoform PrP(Sc). PrP(C) is a cell surface glycoprotein expressed mainly in the central nervous system and despite numerous efforts to elucidate its physiological role, the exact biological function remains unknown. Many lines of evid...