The prion-like phenomenon in Alzheimer’s disease: Evidence of pathology transmission in humans
Ruben Gomez‐Gutierrez, Rodrigo Morales
Abstract
Most neurodegenerative diseases, such as Alzheimer's disease (AD), Parkinson's disease (PD), Huntington's disease (HD), and prion diseases, share common pathogenic features. These include the presence of misfolded protein deposits and progressive neuronal loss in specific areas of the brain. Notably, the misfolded proteins involved in these diseases (prions, amyloid (A), tau, and -synuclein) share common structural, biological, and biochemical features, as well as similar mechanisms of aggregation and self-propagation. The infectious prion protein (PrP Sc ) was the first disease-causing "proteinaceous infectious agent" ever described PrP Sc has the ability to "transmit" its disease-associated conformation to normally folded prion proteins (PrP C ). In turn, PrP Sc can transfer its disease-causing information at different biological levels, including cell to cell, tissue to tissue, or between individuals. PrP Sc particles associated with Creutzfeldt-Jakob disease (CJD) are able to transmit disease by different means, including corneal and dura transplants, implantation of electrodes, administration of cadaveric-derived human growth hormone (c-hGH), and blood transfusions