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• W2075212824 abstract "Conventional (α, βI, βII, γ) and novel (δ, ε, η, θ) protein kinase C (PKC) isozymes are main targets of tumor promoters, such as phorbol esters and indolactam-V (ILV). We have recently found that 1-hexyl derivatives of indolinelactam-V (2, 3), in which the indole ring of ILV was replaced with the indoline ring, showed a binding preference for novel PKCs over conventional PKCs. To develop a new ILV analogue displaying increased synthetic accessibility and improved binding selectivity for novel PKCs, we have designed 8-octyl-benzolactam-V9 (4), a simple analogue without the pyrrolidine moiety of 2 and 3. Compound 4 showed significant binding selectivity for isolated C1B domains of novel PKCs. Moreover, 4 translocated PKCε and η from the cytoplasm to the plasma membrane of HeLa cells at 1 μM, whereas other PKC isozymes did not respond even at 10 μM. These results indicate that 4 could be a selective activator for PKCε and η." @default.
• W2075212824 created "2016-06-24" @default.
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• W2075212824 date "2006-04-01" @default.
• W2075212824 modified "2023-10-17" @default.
• W2075212824 title "Design and Synthesis of 8-Octyl-benzolactam-V9, a Selective Activator for Protein Kinase Cε and η" @default.
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• W2075212824 doi "https://doi.org/10.1021/jm050857c" @default.
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