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Conventional protein kinase C (PKC)‐α and novel PKCε, but not ‐δ, increase the secretion of an N‐terminal fragment of Alzheimer's disease amyloid precursor protein from PKC cDNA transfected 3Y1 fibroblasts
Author(s) -
Abhishek Abhishek,
Hiroyuki Sorimachi,
Kei Maruyama,
Keiko Mizuno,
Shigeo Ohno,
Shoichi Ishiura,
Koichi Suzuki
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00392-m
Subject(s) - protein kinase c , transfection , secretion , amyloid precursor protein , microbiology and biotechnology , chemistry , alzheimer's disease , kinase , biology , biochemistry , medicine , gene , disease
A large soluble N‐terminal fragment of Alzheimer's disease amyloid precursor protein (secreted form of APP: APP s ) is produced by constitutive processing in the middle of the amyloid β‐protein portion of APP. Recent studies indicate that the activation of endogenous protein kinase C (PKC) with phorbol ester raises the rate of secretion of APP s . We constructed rat fibroblast 3Y1 cells that stably overexpress PKC isoenzymes α, δ, or ε, and analyzed the amount of APP s released from these PKC transfectants. The levels of APP s released from 3Y1 cells overexpressing PKCα and ‐ε were higher than those from PKCδ‐transfected and control cells expressing vector only. These results suggest that specific isoforms of PKC regulate the secretion of APP s through a signaling pathway.