Most significantly, in contrast to CJD, in which the abnormal PrPSc aggregates mainly consist of full-length protein together with GPI-anchored, N-terminal fragments truncated between residue 82 and residue 104 [129], in GSS or PrP-CAA affected patients the abnormal PrP plaque amyloid that accumulates is composed primarily of truncated internal PrP fragments (e.g., residues 82–153) that lack the GPI anchor and the glycosylated moiety [102, 146, 152]. This evidence concerns the gene PRNP and Creutzfeldt Jacob disease.