Unaltered prion protein cleavage in plasminogen-deficient mice.
In normal brains and cultured cells, cellular prion protein (PrP) is partially found as N-terminally truncated fragments, designated C1 and C2. The cleavage of recombinant PrP to a fragment corresponding to C1 can be mediated by the protease plasmin (Pln) in vitro, suggesting that plasmin might be responsible for the generation of the C1 fragment in vivo as well. The cleavage pattern of PrP found in both brain lysates and other tissues of plasminogen knock-out mice, however, is unaltered. The presence of C1 fragment in homogenates from plasminogen-deficient mice in a comparable ratio with full-length PrP as can be found in wild-type animals indicates that other proteases in addition to plasmin are responsible for PrP cleavage in vivo.
Center for Neuropathology and Prion Research, Ludwig Maximilians University, Munich, Germany.
Kathrin
K
Barnewitz
Marko
M
Maringer
Gerda
G
Mitteregger
Armin
A
Giese
Uwe
U
Bertsch
Hans A
HA
Kretzschmar
D000818:Animals; D015153:Blotting, Western; D005341:Fibrinolysin / Q000378:metabolism; D005838:Genotype; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase / Q000378:metabolism; D051379:Mice; D008810:Mice, Inbred C57BL; D018345:Mice, Knockout; D010958:Plasminogen / Q000172:deficiency / Q000235:genetics / Q000502:physiology*; D011328:Prions / Q000378:metabolism*; D020133:Reverse Transcriptase Polymerase Chain Reaction
D011328:Prions; D010958:Plasminogen; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; D005341:Fibrinolysin