| Literature DB >> 19002828 |
H Koike1, Z Kouchi, T Kinouchi, T Maeda, H Sorimachi, T C Saido, K Maruyama, A Okuyama, K Suzuki, S Ishiura.
Abstract
Thimet oligopeptidase (TOP) is a thiol- andmetallo-dependent peptidase and has been shown to beone of the beta-secretase candidates. TOPexpressed in COS cells cleaved amyloid precursorprotein (APP) at the beta-secretase site, and wefound a proteolytic product of APP called secretedform of APP by beta-secretase (sAPPbeta) in theconditioned media. Here we demonstrate thatsAPPbeta 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.Entities:
Year: 2000 PMID: 19002828 PMCID: PMC3466702 DOI: 10.1023/A:1008119512341
Source DB: PubMed Journal: Cytotechnology ISSN: 0920-9069 Impact factor: 2.058