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 language | English |
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Pages (from-to) | 111-114 |
Number of pages | 4 |
Journal | Planta Medica |
Volume | 62 |
Issue number | 2 |
DOIs | |
Publication status | Published - 13 May 1996 |
Externally published | Yes |
Keywords
- Ascomycotina
- Claviceps purpurea
- Penicillium oxalicum
- Poaceae
- protein kinase inhibitors
- Secale cereale
- secalonic acid D
- teratogens