Abstract:
:The synchronization of intraerythrocytic maturation of Plasmodium parasites is an important factor in the malaria infection process. Synchronization is mediated by inositol phosphate (InsP(x))-induced Ca(2+)-release from internal stores. To further investigate the InsP(x) metabolism in these parasites a Plasmodium protein possessing inositol phosphate kinase (IPK) activity was recombinantly expressed, purified and enzymatically characterized for the first time. Its main activity is the conversion of the Ca(2+)-releasing second messenger Ins(1,4,5)P(3) to Ins(1,3,4,5)P(4), an important factor in chromatin remodeling and also in Ca(2+)-release. This protein possesses several additional IPK activities pointing to a potential role as inositol phosphate multikinase. Interestingly, we have also identified three putative subdomains of histone deacetylase in this protein possibly linking InsP(x)- and acetylation-mediated transcription regulation. Furthermore, we examined the inhibitory potential of >40 polyphenolic substances against its kinase activity. Because of the important role of InsP(x)-induced Ca(2+)-release in the development of Plasmodium parasites, IPKs are interesting targets for novel antimalarial approaches.
journal_name
Mol Biochem Parasitoljournal_title
Molecular and biochemical parasitologyauthors
Stritzke C,Nalaskowski MM,Fanick W,Lin H,Mayr GWdoi
10.1016/j.molbiopara.2012.10.005subject
Has Abstractpub_date
2012-12-01 00:00:00pages
134-8issue
2eissn
0166-6851issn
1872-9428pii
S0166-6851(12)00249-6journal_volume
186pub_type
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