ISSN:
1573-0778
Keywords:
Alzheimer's disease
;
amyloid precursor protein
;
β-secretase
;
hydroxamate-based metalloprotease inhibitor
;
thimet oligopeptidase
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Medicine
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Abstract Thimet oligopeptidase (TOP) is a thiol- andmetallo-dependent peptidase and has been shown to beone of the β-secretase candidates. TOPexpressed in COS cells cleaved amyloid precursorprotein (APP) at the β-secretase site, and wefound a proteolytic product of APP called secretedform of APP by β-secretase (sAPPβ) in theconditioned media. Here we demonstrate thatsAPPβ was increased in conditioned media whenTOP was coexpressed in COS cells with APP and treatedwith an ADAM inhibitor SI-27. In addition, althoughTOP expressed in COS cell was localized at nuclei orGolgi apparatus, it exclusively colocalized at Golgiapparatus when APP was coexpressed with TOP.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1008119512341
Permalink