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Amyloid beta peptide directly inhibits PKC activation.

Authors
Lee, W; Boo, JH; Jung, MW; Park, SD; Kim, YH; Kim, SU; Mook-Jung, I
Citation
Molecular and cellular neurosciences, 26(2):222-231, 2004
Journal Title
Molecular and cellular neurosciences
ISSN
1044-74311095-9327
Abstract
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.
MeSH terms
Alzheimer Disease/*enzymology/physiopathologyAmyloid beta-Peptides/*metabolism/pharmacologyAnimalsBrain/*enzymology/physiopathologyCell Line, TumorDose-Response Relationship, DrugFeedback, Physiological/physiologyNeurons/*enzymologyPeptide Fragments/pharmacologyPhorbol 12,13-Dibutyrate/pharmacologyPhosphorylation/drug effectsProtein Kinase C/antagonists & inhibitors/*metabolismProtein Kinase C-alphaProtein Kinase C-epsilonProtein Structure, Tertiary/physiologyRats
DOI
10.1016/j.mcn.2003.10.020
PMID
15207847
Appears in Collections:
Journal Papers > Research Organization > Institute for Medical Sciences
Journal Papers > School of Medicine / Graduate School of Medicine > Neurology
AJOU Authors
정, 민환김, 승업
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