Prion protein PrP is a membrane glycosylphosphatidylinositol(GPI) anchored glycoprotein highly expressed in neurons and glial cells, as well as immune and reproductive cells. Mutations, mostly in the octapeptide repeat regions, have been associated with neurodegenerative diseases such as Creutzfeldt Jakob disease, fatal familial insomnia, Gerstmann Straussler disease, Huntington disease like 1, and kuru. The infectious isoform of PrPC, known as PrPSc, is able to induce a conformational change in normal PrPC proteins to convert them into the infectious isoform. Both forms of PrP are initially expressed as a ~250 amino acid protein which is truncated to produce the mature protein of 209 amino acids. Several topological forms exist: one cell surface form which is anchored via a glycolipid modification, and two transmembrane forms. Thus, more than one band is visible on an SDS-PAGE.
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