Susceptibility of Plasmodium falciparum cyclic AMP-dependent protein kinase and its mammalian homologue to the inhibitors

Atsushi Sudo, Kentaro Kato, Kyousuke Kobayashi, Yukinobu Tohya, Hiroomi Akashi

Research output: Contribution to journalArticlepeer-review

23 Citations (Scopus)

Abstract

Cyclic AMP-dependent protein kinase (protein kinase A, PKA) is a key element in many cell signaling pathways. An essential role of Plasmodium falciparum PKA (PfPKA) activity was reported in the intraerythrocytic growth of the malaria parasite. However, molecular characterization of PfPKA using purified recombinant proteins has not yet been performed. Here, we report the first successful purification of the enzymatically active PKA catalytic subunit of P. falciparum (PfPKA-C) using a wheat germ cell-free expression system. Interestingly, parasite enzymatic activity was weakly inhibited as compared with the inhibition of mammalian PKA catalytic subunit (PKA-C) by the specific PKA inhibitor, H89. Furthermore, PfPKA-C was only slightly inhibited by protein kinase inhibitor (PKI). These results suggest that substrate sites of PfPKA-C may be different from those of mammalian PKA-Cs. In addition, potential PKI corresponding to malarial PKA-C would also be different from those of mammalian cells.

Original languageEnglish
Pages (from-to)138-142
Number of pages5
JournalMolecular and Biochemical Parasitology
Volume160
Issue number2
DOIs
Publication statusPublished - 2008 Aug 1
Externally publishedYes

Keywords

  • PKA-C
  • PKI
  • Plasmodium falciparum
  • Wheat germ cell-free expression

ASJC Scopus subject areas

  • Parasitology
  • Molecular Biology

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