T. O. Veklich1, A. A. Shkrabak1, S. O. Cherenok2, V. I. Kalchenko2, S. O. Kosterin1
The aim of our investigation was to determine structural features of calixarene C-99 which are important for its inhibition properties relative to Nа+,K+-ATPase of uterus myocite plasma membrane. Therefore we studied the effect of calix-arenes С-296, С-297, С-424, С-425, С-426, С-427, which are structurally similar to this inhibitor, on the mentioned enzyme activity. We have shown that calixarenes С-296 and С-297 which have two additional propoxy groups on the lower rim of macrocycle are less effective inhibitors of Nа+,K+-ATPase relative to calixarene C-99. Calixarenes С-425 and С-427 which have on the upper rim of macrocycle three and four phosponic residues, respectively, also inhibit Nа+,K+-ATPase activity less effectively as compared to calixarene C-99. Both calixarenes: С-424, which has only two carbonate residues on the upper rim, and С-426, which has on the upper rim ketomethilphosphonate residues instead of hydroxymethilphosphonate residues of calixarene C-99, do not affect Nа+,K+-ATPase activity. We have made respective conclusions concerning the role of certain chemical groups of calixarene C-99 during its interaction with Nа+,K+-ATPase.
Key words: Na+,K+-ATPase, Mg2+-ATPase, plasma membrane, smooth muscle cells, myometrium, kinetic properties of ATPase, calixarenes, aminophosphonic acids.
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