Inhibition of eukaryote serine/threonine-specific protein kinases by piceatannol

Bing Hui Wang, Zhe Xiong Lu, Gideon M. Polya

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41 Citations (Scopus)

Abstract

The protein tyrosine kinase (PTK) inhibitor piceatannol is also an inhibitor of the rat liver cyclic AMP-dependent protein kinase (PKA) catalytic subunit (cAK), rat brain Ca2+- and phospholipid-dependent protein kinase C (PKC), avian gizzard Ca2+-calmodulin-dependent myosin light chain kinase (MLCK), and of wheat embryo Ca2+-dependent protein kinase (CDPK) (IC50 values 3, 8, 12, and 19 μM, respectively). However, a number of piceatannol-related compounds with fewer or no phenolic hydroxy substituents are inactive or very poor inhibitors of these serine/threonine protein kinases. Similarly, the PTK inhibitor ellagic acid is a potent inhibitor of cAK and of PKC (IC50 values 2 and 8 μM, respectively), whereas the non- phenolic perylene is ineffective as a protein kinase inhibitor. Ellagic acid is a competitive inhibitor of both cAK and of PKC but piceatannol inhibits these enzymes in a fashion that is competitive and noncompetitive, respectively. Interaction with calmodulin may contribute to the inhibition of MLCK and CDPK by piceatannol.

Original languageEnglish
Pages (from-to)195-199
Number of pages5
JournalPlanta Medica
Volume64
Issue number3
DOIs
Publication statusPublished - 1 Jan 1998
Externally publishedYes

Keywords

  • Ellagic acid
  • Piceatannol
  • Protein kinase
  • Stilbenes

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