Norwegian describes scrapie gene
Intestinal lymphatic tissue is important for the absorption and spread of the scrapie prion, suggests a Norwegian researcher.
Protein molecules may show different properties when their structures become altered, for example, proteins in egg white are hardened by heat treatment. The assumed cause of prion diseases is that the structure of the normal prion protein, called PrPC, becomes altered. The abnormal, disease-associated form of the prion protein, called PrPSc, is assumed to be the infectious agent.
Lars Austbø used advanced gene technology and molecular biology to study both prion gene activity and the presence of the protein PrPC in the Payer's patches of the small intestine and in the spleen - two organs where lymphoreticular tissue is assumed to be important for the absorption of the infective substance, PrPSc, and its spread the the brain.
He has compiled new knowledge of the tissues that the PrPC protein and its mRNA is expressed in and the degree to which the gene is active. In addition, the study has shown that accumulation of the disease-related prion protein, PrPSc, is not necessarily associated with high levels of the normal prion protein. This conflicts with earlier assumptions and may force a re-evaluation of earlier theories on the absorption and distribution of the disease-related prion protein.
