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Identification and evaluation of neutral sphingomyelinase 2 inhibitors

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 - lyxo phytosphingosine and d...

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Bibliographic Details
Published in:Archives of pharmacal research 2011, 34(2), , pp.229-236
Main Authors: Lee, Dong Hun, Kim, Sung Hyun, Ahn, Kyong Hoon, Kim, Seok Kyun, Choi, Jong Min, Ji, Jung Eun, Won, Jong Hoon, Park, Yang Hui, Lim, Chaemin, Kim, Sanghee, Kim, Dae Kyong
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Language:English
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Summary: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 - lyxo phytosphingosine 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.
ISSN:0253-6269
1976-3786
DOI:10.1007/s12272-011-0208-y