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  • Title: Identification and evaluation of neutral sphingomyelinase 2 inhibitors.
    Author: Lee DH, Kim SH, Ahn KH, Kim SK, Choi JM, Ji JE, Won JH, Park YH, Lim C, Kim S, Kim DK.
    Journal: Arch Pharm Res; 2011 Feb; 34(2):229-36. PubMed ID: 21380806.
    Abstract:
    Sphingomyelinase catalyzes the hydrolysis of sphingomyelin to generate ceramide, an important molecule involved in the regulation of various cellular responses. In this study, we partially purified the neutral sphingomyelinase2 (nSMase2) and identified the inhibitors, D-lyxophytosphingosine and D-arabino-phytosphingosine, which have an inhibitory effect on nSMase2 in a concentration-dependent manner. A Dixon plot of each phytosphingosines revealed their probable inhibitory pattern, i.e., apparent competitive inhibition. These compounds did not inhibit the Mg(2+)-independent neutral SMase activity, although the known nSMase2 inhibitor, GW4869, showed inhibitory effects on Mg(2+)-independent neutral SMase activity. Further, the two phytosphingosines specifically inhibited the ceramide generation regulated by nSMase2.
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