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SphK inhibitors block the lipid kinases that turn sphingosine into sphingosine-1-phosphate (S1P). Murine sphingosine kinase 1 (SphK1) was cloned in 1998, and a second isoform, sphingosine kinase 2 (SphK2), followed in 2000. The two enzymes differ in tissue distribution and subcellular location. By phosphorylating sphingosine, they shift the balance away from ceramide and sphingosine toward S1P, which acts on cell surface receptors and inside cells. PF-543, reported in 2012 as a selective SphK1 inhibitor, lowers cellular S1P levels. SK1-IN-1 also targets SphK1, while K145 and opaganib inhibit SphK2 and SKI-II acts on both isoforms. MHP is listed as an activator of SphK1 rather than an inhibitor.
