Lee, W; Boo, JH; Jung, MW; Park, SD; Kim, YH; Kim, SU; Mook-Jung, I
Molecular and cellular neurosciences, 26(2):222-231, 2004
Molecular and cellular neurosciences
A putative protein kinase C (PKC) pseudosubstrate domain in beta amyloid (Abeta) suggests a potential interaction between Abeta and PKC. In this study, we investigated whether and how Abeta interacts with PKC. Abeta peptides inhibited PKC phosphorylation in a dose-dependent manner in cell-free in vitro condition, suggesting a direct interaction between Abeta and PKC. Experiments involving deletion of the Abeta sequence indicated that the putative PKC pseudosubstrate domain (Abeta 28-30) is critical for Abeta-PKC interaction. Addition of Abeta peptides to cultured B103 cells reduced the activated forms of PKCalpha and PKCepsilon. It also inhibited phorbol-12,13-dibutyrate (PDBu)-induced membrane translocation of PKCalpha and PKCepsilon without altering their expression levels, indicating that activation of intracellular PKC is inhibited by treatment of Abeta peptides. These results suggest that Abeta peptides inhibit PKC activation via direct interactions, which may play a role in pathogenesis of AD.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.
Total Visit :2,783,756
Total Download :1,135,398
Today View :1,226
Ajou University Medical Information & Media Center 164 Worldcup-ro Yeongtong-gu Suwon 16499 Korea / TEL : 031-219-5312 / FAX : 031-219-5314 Copyright (c) Ajou University Medical Information & Media Center All Rights Reserved. AJOU Open Repository는 국립중앙도서관 OAK 보급사업으로 구축되었습니다.