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The phorbol derivatives thymeleatoxin and 12‐deoxyphorbol‐13‐ O ‐phenylacetate‐10‐acetate cause translocation and down‐regulation of multiple protein kinase C isozymes
Author(s) -
Roivainen Reina,
Messing Robert O.
Publication year - 1993
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(93)80031-o
Subject(s) - isozyme , protein kinase c , phenylacetate , phorbol , chemistry , chromosomal translocation , biochemistry , enzyme , gene
Phorbol esters such as phorbol 12‐myristate,13‐acetate (PMA) are potent activators of protein kinase C (PKC), and activate all PKC isozymes except ζ, and λ. Recently, 12‐deoxyphorbol‐13‐ O ‐phenylacetate‐20‐acetate (dPPA) and thymeleatoxin (Tx) were reported to selectively activate PKCβ 1 (dPPA) and PKCα, ‐β, and ‐γ (Tx), but not PKCδ or PKCϵ in vitro. We examined the ability of these phorbol derivatives to translocate and down‐regulate PKC isozymes in intact cells. Our findings demonstrate that dPPA and Tx cause translocation and down‐regulation of multiple PKC isozymes, including δ and ϵ.