23/03/2024
The human prion protein (PrP) is a naturally occurring protein found in the body, primarily in the brain and nervous system. Prions are unique in that they have the ability to fold into abnormal conformations, leading to infectious, self-propagating protein aggregates. These misfolded proteins are associated with several neurodegenerative diseases, including Creutzfeldt-Jakob disease (CJD), variant Creutzfeldt-Jakob disease (vCJD), Gerstmann-Sträussler-Scheinker syndrome (GSS), and kuru.
PrP is encoded by the PRNP gene and is expressed in many tissues, with particularly high levels in the brain. Its exact function is not fully understood, but it is believed to play a role in neuronal protection and cell signaling.
The misfolding of PrP is a central event in prion diseases. The normal, cellular form of PrP (PrPC) undergoes a conformational change to an abnormal, infectious form (PrPSc), which aggregates and forms amyloid fibrils. These aggregated proteins can induce further misfolding of normal PrP molecules, leading to a cascade effect and the progressive accumulation of pathological prions in the brain.
Prion diseases typically manifest as rapidly progressing neurological disorders, characterized by cognitive decline, motor dysfunction, and ultimately, death. Diagnosis of prion diseases often involves clinical evaluation, imaging studies, and laboratory tests such as cerebrospinal fluid analysis and detection of abnormal PrP aggregates. Made with protein imaging app.
