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    FEBS Lett. 2004 Jan 16;557(1-3):288-92.

    Hydrolysis of sphingosylphosphocholine by neutral sphingomyelinases.

    Miura Y, Gotoh E, Nara F, Nishijima M, Hanada K.

    Source

    Department of Biochemistry and Cell Biology, National Institute of Infectious Diseases, 1-23-1, Toyama, Shinjuku-ku, Tokyo 162-8640, Japan.

    Erratum in

    • FEBS Lett. 2004 May 7;565(1-3):207.

    Abstract

    Sphingosylphosphocholine (SPC), the N-deacylated form of sphingomyelin (SM), is a naturally occurring lipid mediator. However, little is known about the metabolism of SPC. We here report an in vitro assay system for SPC-phospholipase C (PLC). Using this assay system, we demonstrated that nSMase1 and nSMase2, human neutral sphingomyelinases (SMases), are capable of hydrolyzing SPC efficiently under detergent-free conditions. Bacterial and plasmodial neutral SMases also showed SPC-PLC activity. The substrate specificity of neutral SMases that hydrolyze SM, SPC, and monoradyl glycerophosphocholine, but not diradyl glycerophosphocholine, suggested that a hydrogen-bond donor at the C-2 or sn-2 position in the substrate is required for recognition by the enzymes.

    PMID:
    14741383
    [PubMed - indexed for MEDLINE]

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