Prionproteinet

Prionproteinet, often abbreviated as PrP, is a protein that in its normal form is found on the surface of cells in the body. It is particularly abundant in the nervous system. The normal function of PrP is not fully understood, but it is thought to be involved in cell signaling, cell adhesion, and copper metabolism.

The critical aspect of PrP is its ability to misfold. Prions are infectious agents composed solely of protein, and the prion protein is the sole known component of these agents. When PrP misfolds, it can induce other normal PrP molecules to misfold as well, creating a chain reaction. This abnormal, misfolded form of PrP is known as PrPSc.

This misfolding process leads to the accumulation of PrPSc in the brain, forming aggregates that can damage and kill nerve cells. This neuronal death is responsible for the development of a group of fatal neurodegenerative diseases called prion diseases, also known as transmissible spongiform encephalopathies (TSEs). Examples of prion diseases in humans include Creutzfeldt-Jakob disease (CJD), kuru, Gerstmann-Sträussler-Scheinker syndrome (GSS), and fatal familial insomnia (FFI). In animals, common prion diseases include scrapie in sheep, bovine spongiform encephalopathy (BSE) in cattle, and chronic wasting disease (CWD) in deer and elk.

The mechanism by which PrPSc causes disease is not fully elucidated, but it is believed to involve disruption of normal cellular processes and the triggering of inflammatory responses in the brain. Prion diseases are currently untreatable and invariably fatal.