NR AWJJ
AU Maddison,B.C.; Whitelam,G.C.; Gough,K.C.
TI Cellular prion protein in milk
QU International Conference - Prion 2006: Strategies, advances and trends towards protection of society - 3.10.-6.10.2006, Torino, Italy, Lingotto Conference Centre - Poster sessions CE-27
PT Konferenz-Poster
AB Cellular prion protein, PrPc, is essential for the development of prion diseases where PrPc is considered the substrate for the formation of a disease associated conformer, PrPsc. In sheep, the natural host of the prion disease scrapie, PrPc is abundant in CNS tissue and is also found at lower concentrations in a range of non-neuronal tissues including skeletal muscle and mammary gland. Here, we demonstrate the presence of cellular prion protein in milk from both ovine and bovine sources. Milk PrPc has increased electrophoretic mobility compared with brain PrPc yet is recognised by antibodies directed to epitopes at the C- and N-terminal regions of the protein. Furthermore, milk PrPc is apparently not membrane-associated; together these observations suggest absence of the C-terminal GPI-anchor. Milk PrPc is present predominantly as three species that differ only in the extent of their N-linked glycosylation, with glycoform profiles varying among animals. These apparently full-length PrPc species are also present in commercial homogenised/pasteurised bovine milk, although at reduced levels compared with unprocessed milk. Additional N-terminal fragments of PrPc are also detectable in ruminant milk and commercial milk products. These findings represent the first evidence of the presence of PrPc in milk and raise the question of whether disease-associated PrP species and prion infectivity can also be secreted into milk.
AD B.C. Maddison, K.C. Gough: ADAS UK, Department of Biology, University of Leicester, University Road, Leicester, LE1 7RH. UK; G.C. Whitelam: Department of Biology, University of Leicester, University Road, Leicester, LE1 7RH. UK. E-mail: Ben.Maddison@adas.co.uk
SP englisch
PO Italien