Abstract:
:We reported previously that N-linked glycoproteins were accumulated in the cytosol of the normal aging rat brain, and that one protein had been identified as cathepsin D (Mech. Ageing Dev., 127, 771-778 (2006)). In this study, to elucidate the mechanism of cathepsin D accumulation in the cytosol, we examined the effects of oxidative stress and proteasome inhibition on the apoptosis and subcellular localization of cathepsin D in primary cultured neurons and astrocytes. Using 4'-6-diamidino-2-phenylindole (DAPI)- or Hoechst 33342-staining and annexin V detection, we found that oxidative stress caused by tert-butyl hydroperoxide and proteasome inhibition by lactacystin induced apoptosis in neurons and astrocytes. Furthermore, after cell fractionation, it was demonstrated that cathepsin D was translocated from lysosomes to cytosol under apoptosis-inducing conditions in both cells. These results suggested that oxidative stress and the suppression of proteasome activity triggered the translocation of cathepsin D from lysosomes to cytosol. The possible mechanism of age-related accumulation of cathepsin D in the cytosol of the normal rat brain will be discussed.
journal_name
Biol Pharm Bulljournal_title
Biological & pharmaceutical bulletinauthors
Miura Y,Sakurai Y,Hayakawa M,Shimada Y,Zempel H,Sato Y,Hisanaga S,Endo Tdoi
10.1248/bpb.33.22subject
Has Abstractpub_date
2010-01-01 00:00:00pages
22-8issue
1eissn
0918-6158issn
1347-5215pii
JST.JSTAGE/bpb/33.22journal_volume
33pub_type
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