Recruitment of a phospholipase C/sphingomyelinase into non-lamellar lipid droplets during hydrolysis of lipid bilayers
| Autor: | Adriana I. Vasil, Jesús Sot, Maitane Ibarguren, L.-Ruth Montes, Michael L. Vasil, Alicia Alonso, Félix M. Goñi |
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| Rok vydání: | 2013 |
| Předmět: |
Phosphatidylethanolamine
Ceramide Phospholipase C Chemistry Hydrolysis Vesicle Lipid Bilayers Organic Chemistry Cell Biology Ceramides Biochemistry Article Diglycerides chemistry.chemical_compound Type C Phospholipases Phosphatidylcholine Lipid droplet Pseudomonas aeruginosa Humans Pseudomonas Infections Lipid bilayer Sphingomyelin Molecular Biology Unilamellar Liposomes |
| Zdroj: | Chemistry and Physics of Lipids. 166:12-17 |
| ISSN: | 0009-3084 |
| Popis: | When giant unilamellar vesicles (GUVs) composed of sphingomyelin, phosphatidylcholine, phosphatidylethanolamine, and cholesterol are treated with PlcHR(2), a phospholipase C/sphingomyelinase from Pseudomonas aeruginosa, the initial stages of lipid hydrolysis do not cause large changes in vesicle morphology (Ibarguren et al., 2011). However, when hydrolysis progresses confocal fluorescence microscopy reveals the formation of lipid aggregates, whose morphology is not compatible with that of bilayers. Smaller vesicles or droplets can also be seen inside the GUV. Our studies indicate that these aggregates or droplets are enriched in the non-lamellar lipid ceramide, an end-product of PlcHR(2) reaction. Moreover, the aggregates/droplets appear enriched in the hydrolytic enzyme PlcHR(2). At a final stage GUVs containing the enzyme-enriched droplets disintegrate and vanish from the microscope field. The observed non-lamellar enzyme-rich structures may be related to intermediates in the process of aggregation and fusion although the experimental design prevents vesicle free diffusion in the aqueous medium, thus actual aggregation or fusion cannot be observed. |
| Databáze: | OpenAIRE |
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