Unaltered prion protein cleavage in plasminogen-deficient mice.
Neuroreport
; 17(5): 527-30, 2006 Apr 03.
Article
em En
| MEDLINE
| ID: mdl-16543819
ABSTRACT
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.
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Base de dados:
MEDLINE
Assunto principal:
Plasminogênio
/
Príons
Limite:
Animals
Idioma:
En
Ano de publicação:
2006
Tipo de documento:
Article