A secondary assay for ceramide kinase inhibitors based on cell growth inhibition by short-chain ceramides

  • Anal Biochem. 2009 Jan 1;384(1):166-9. doi: 10.1016/j.ab.2008.09.008.
Christine Graf  1 Philipp Rovina Frédéric Bornancin
Affiliations
  • 1. Novartis Institutes for BioMedical Research, A-1235 Vienna, Austria.
Abstract

We recently reported that ectopic expression of ceramide kinase (CerK) in various cell lines increases their sensitivity to cell death induced by the exogenous addition of short-chain (e.g., C2) ceramides (Cer). Here we show that this higher sensitivity results from CerK catalytic activity and production of C2-ceramide 1-phosphate (C2-C1P). If CerK activity is inhibited by the potent inhibitor NVP-231, C2-C1P is not produced and viability returns to control levels. The EC(50) of NVP-231 in this assay is in the low nanomolar range, consistent with the IC(50) determined in activity assays in vitro using purified CerK. NVP-995, a structurally related but inactive compound, does not protect against C2-Cer-induced cell death. This assay is robust and easy to implement and scale up, thereby providing a valuable secondary screen assay for CerK inhibitors.

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