Reconstitution of gamma-secretase activity.
Nat Cell Biol
; 5(5): 486-8, 2003 May.
Article
en En
| MEDLINE
| ID: mdl-12679784
ABSTRACT
gamma-Secretase is a membrane protein complex with an unusual aspartyl protease activity that catalyses the regulated intramembranous cleavage of the beta-amyloid precursor protein (APP) to release the Alzheimer's disease (AD)-associated amyloid beta-peptide (Abeta) and the APP intracellular domain (AICD). Here we show the reconstitution of gamma-secretase activity in the yeast Saccharomyces cerevisiae, which lacks endogenous gamma-secretase activity. Reconstituted gamma-secretase activity depends on the presence of four complex components including presenilin (PS), nicastrin (Nct), APH-1 (refs 3-6) and PEN-2 (refs 4, 7), is associated with endoproteolysis of PS, and produces Abeta and AICD in vitro. Thus, the biological activity of gamma-secretase is reconstituted by the co-expression of human PS, Nct, APH-1 and PEN-2 in yeast.
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Banco de datos:
MEDLINE
Asunto principal:
Endopeptidasas
/
Saccharomyces cerevisiae
/
Membrana Celular
/
Células Eucariotas
Límite:
Humans
Idioma:
En
Año:
2003
Tipo del documento:
Article