Add time:09/30/2019         Source:infona.pl

Proteins comprising the first nucleotide-binding- and R-domains of wild-type and ΔF508 cystic fibrosis transmembrane conductance regulator (CFTR) have been synthesised by in vitro transcription/translation. The kinetics and extent of degradation of wild-type and ΔF508 cytoplasmic domain proteins in rabbit reticulocyte lysates, in which proteasome activity was inhibited, were similar, with a half-life of approximately 4h. The results show for the first time, that the benzo(c)quinolizinium compounds, MPB-07 and MPB-91, selectively inhibit degradation of the ΔF508 cytoplasmic domain protein. Studies using protease inhibitors demonstrated that both ΔF508 and wild-type proteins are substrates for cysteine proteases. The studies provide evidence that benzo(c)quinolizinium compounds protect a proteolytic cleavage site by direct binding to the first cytoplasmic domain of ΔF508-CFTR and this is a likely mechanism for increasing ΔF508-CFTR trafficking in intact cells.

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