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A more recent version of this article appeared on May 1, 2008

Papers In Press, published online ahead of print February 8, 2008
J. Lipid Res., doi:10.1194/jlr.M700587-JLR200
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Submitted on December 19, 2007
Revised on February 4, 2008
Accepted on February 7, 2008

The relationship between the metabolism of sphingomyelin species and hemolysis of sheep erythrocytes induced by Clostridium perfringens alpha-toxin

Masataka Oda, Takayuki Matsuno, Ryouta Shiihara, Sadayuki Ochi, Rieko Yamauchi, Hiroshi Imagawa, Masahiro Nagahama, Mugio Nishizawa, and Jun Sakurai

Department of Microbiology, Tokushima Bunri University, Tokushima, Tokushima 770-8514

Corresponding Author: masa{at}ph.bunri-u.ac.jp

Clostridium perfringens alpha-toxin induces the hemolysis of sheep erythrocytes by activating the metabolism of sphingomyelin (SM) via a GTP-binding protein in membranes. Alpha-toxin stimulated the formation of N-nervonoyl sphingosine (C24:1-ceramide), which was identified by positive ion FAB-MS and 1H-NMR spectroscopy. C24:1-ceramide stimulated the toxin-induced hemolysis of saponin-pretreated sheep erythrocytes and increased the production of sphingosine 1-phosphate (S1P) in the cells, but N-lignoceroyl sphingosine (C24:0-ceramide) did not. These events elicited by the toxin in the presence of C24:1-ceramide were significantly attenuated by treatment with dihydrosphingosine (DHS), a sphingosine kinase inhibitor. TLC showed that the level of C24:1-ceramide was highest among the ceramides with an unsaturated bond in the fatty acyl chain in the detergent-resistant membranes (DRM). The toxin specifically bound to DRM rich in cholesterol, resulting in the hydrolysis of N-nervonic sphingomyelin (C24:1-SM) in DRM. Treatment of the cells with pertussis toxin (PT) inhibited the alpha-toxin-induced formation of C24:1-ceramide from C24:1-SM in DRM and hemolysis, indicating that endogenous sphingomyelinase which hydrolyzes C24:1-SM to C24:1-ceramide is controlled by PT-sensitive GTP-binding protein in membranes. The results show that the toxin-induced metabolism of C24:1-SM to S1P in DRM plays an important role in the toxin-induced hemolysis of sheep erythrocytes.


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