Filling_The_Holes_Of_Spongiform_Encephalopathies

Filling The Holes Of Spongiform Encephalopathies Filling the Holes of Spongiform Encephalopathies Introduction Until a few years ago it was believed that a disease could only be transmitted from one organism to another through a virus or microorganism (1). Evidence now exists that transmission of a protein may be the cause of a class of diseases known as Transmissible Spongiform Encephalopathies (TSEs). The most well known of these diseases is bovine spongiform encephalopathy or mad cow disease. Other forms include scrapie in sheep, and Creutzfeldt-Jakob Disease (CJD) in humans (2). The protein responsible for these diseases has been termed prion-related-protein or PrP. The normal, cellular protein (PrPc) is found in many animals including humans. Prions are transmissible particles that are composed exclusively of a modified protein (PrPsc) (2). Under certain conditions, not yet fully understood, a conformational shift occurs of PrPc to a disease causing prion termed prion-related protein scapies (PrPsc). This shift causes the amino-terminus of PrPc to partially fold into a ƒÒ-sheet that results in the disruption of electrical stimulation of the nervous system. The disruptions are caused by the formation of plaque bundles in the brain that give the brain a spongy look upon postmortem examination, hence the prpsc, protein, polyamines, cells, prpc, binding, antibody, disease, brain, prp, prions, prion, plasminogen, 15b3, spongiform, normal, mouse, indicated, further, branched, blood, western, treatment, proteinase, mice, encephalopathies, bovine, blot, using, transmissible, through, three, tested, scrapie, scn2a