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Inhibition of protein phosphatases‐1 and ‐2A with acanthifolicin
Author(s) -
Holmes Charles F.B.,
Luu Hue A.,
Carrier France,
Schmitz Francis J.
Publication year - 1990
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(90)81271-o
Subject(s) - okadaic acid , phosphatase , protein phosphatase 2 , in vivo , biochemistry , chemistry , in vitro , acid phosphatase , enzyme , biology , microbiology and biotechnology
Acanthifolicin (9,10‐epithio‐okadaic acid from Pandoras acanthifolium ) inhibited protein phosphatase‐1 (PP1) similarly to okadaic acid (IC 50 = 20 nM and 19 nM, respectively) but was slightly less active against protein phosphatase‐2A (PP2A) (IC 50 1 nM and 0.2 nM, respectively). Methyl esterification of acanthifolicin sharply reduced its activity. PP2A was inhibited with an IC 50 = 5.0 μM, whilst PP1 was inhibited < 10% at 250 μM toxin. Okadaic acid methyl ester was similarly inactive whereas dinophysistoxin‐1 (35‐methyl okadaic acid) inhibited PP1/2A almost as potently as okadaic acid. Pure acanthifolicin/okadaic acid methyl ester may be useful as specific inhibitors of PP2A at 1–10 μM concentrations in vitro and perhaps in vivo. The data also indicate that a region on these toxins important for PP1/2A inhibition comprises the single carboxyl group.