Source:http://linkedlifedata.com/resource/pubmed/id/20214877
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2010-5-3
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pubmed:abstractText |
Bacillus cereus sphingomyelinase (Bc-SMase) induces hemolysis of sheep erythrocytes which contain large amounts of sphingomyelin. We investigated the mechanism of this hemolysis in comparison to that induced by Clostridium perfringens alpha-toxin. Pertussis toxin, a Gi-specific inhibitor, N-oleoylethernolamine, a ceramidase inhibitor, and dihydrosphingosine, a sphingosine kinase inhibitor, did not inhibit the hemolysis by Bc-SMase, but did inhibit that by alpha-toxin. Bc-SMase broadly bound to whole membranes, and alpha-toxin specifically bound to the detergent-resistant membrane fractions, lipid rafts. The level of ceramide production induced by Bc-SMase in sheep erythrocytes was 6- to 15-fold that induced by alpha-toxin, when the extent of the hemolysis by Bc-SMase was the same as that by the toxin. However, the level of ceramide production induced by Bc-SMase in SM-liposomes was equal to that triggered by the toxin, when the carboxyl fluorescein-release from liposomes induced by Bc-SMase was the same as that induced by alpha-toxin. Confocal laser microscopy showed that treatment of the cells with Bc-SMase resulted in the formation of ceramide-rich domains. A photobleaching analysis suggested that treatment of the cells with Bc-SMase leads to a reduction in membrane fluidity. These results show that Bc-SMase-induced hemolysis of sheep erythrocytes is related to the formation of interface between ceramide-rich domains and ceramide-poor domains through production of ceramide from SM.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Toxins,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ceramides,
http://linkedlifedata.com/resource/pubmed/chemical/Pertussis Toxin,
http://linkedlifedata.com/resource/pubmed/chemical/Sphingomyelin Phosphodiesterase,
http://linkedlifedata.com/resource/pubmed/chemical/Sphingosine,
http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases,
http://linkedlifedata.com/resource/pubmed/chemical/alpha toxin, Clostridium perfringens,
http://linkedlifedata.com/resource/pubmed/chemical/safingol
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
1798
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1073-80
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pubmed:meshHeading |
pubmed-meshheading:20214877-Animals,
pubmed-meshheading:20214877-Bacillus cereus,
pubmed-meshheading:20214877-Bacterial Toxins,
pubmed-meshheading:20214877-Calcium-Binding Proteins,
pubmed-meshheading:20214877-Ceramides,
pubmed-meshheading:20214877-Erythrocyte Membrane,
pubmed-meshheading:20214877-Hemolysis,
pubmed-meshheading:20214877-Membrane Fluidity,
pubmed-meshheading:20214877-Membrane Microdomains,
pubmed-meshheading:20214877-Pertussis Toxin,
pubmed-meshheading:20214877-Sheep,
pubmed-meshheading:20214877-Sphingomyelin Phosphodiesterase,
pubmed-meshheading:20214877-Sphingosine,
pubmed-meshheading:20214877-Type C Phospholipases
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pubmed:year |
2010
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pubmed:articleTitle |
Hemolysis induced by Bacillus cereus sphingomyelinase.
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pubmed:affiliation |
Department of Microbiology, Faculty of Pharmaceutical Sciences, Tokushima Bunri University, Yamashiro-cho, Tokushima, Japan 770-8514.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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