The fungal teratogen secalonic acid D is an inhibitor of protein kinase C and of cyclic AMP-dependent protein kinase

Bing Hui Wang, Gideon M. Polya

Research output: Contribution to journalArticleResearchpeer-review

31 Citations (Scopus)

Abstract

The teratogenic metabolite secalonic acid D deriving from the ergot-producing, rye-infecting ascomycete fungus Claviceps purpurea and from Penicillium oxalicum is an inhibitor of Ca2+- and phospholipid-dependent protein kinase C (PKC) and of the catalytic subunit of cyclic AMP-dependent protein kinase (cAK) (IC50 values 15 μM and 12 μM, respectively). Secalonic acid D also inhibits Ca2+-calmodulin-dependent myosin light chain kinase (MLCK) and plant Ca2+-dependent protein kinase (CDPK). The inhibition of cAK by secalonic acid D is competitive with respect to both peptide substrate and ATP. However, secalonic acid D does not inhibit a high-affinity nucleotide-binding phosphatase from potato. A variety of other naturally-occurring teratogenic agents are not inhibitors of the protein kinases examined.

Original languageEnglish
Pages (from-to)111-114
Number of pages4
JournalPlanta Medica
Volume62
Issue number2
DOIs
Publication statusPublished - 13 May 1996
Externally publishedYes

Keywords

  • Ascomycotina
  • Claviceps purpurea
  • Penicillium oxalicum
  • Poaceae
  • protein kinase inhibitors
  • Secale cereale
  • secalonic acid D
  • teratogens

Cite this