Metabolism of amyloid precursor protein in COS cells transfected with a beta-secretase candidate.
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.
Koike
H
H
Department of Life Sciences, Graduate School of Arts and Sciences, The University of Tokyo, 3-8-1 Komaba, Meguro-ku, Tokyo, 153-8902, Japan.
Kouchi
Z
Z
Kinouchi
T
T
Maeda
T
T
Sorimachi
H
H
Saido
T C
TC
Maruyama
K
K
Okuyama
A
A
Suzuki
K
K
Ishiura
S
S