Changes in membrane biophysical properties induced by sphingomyelinase depend on the sphingolipid N-acyl chain
Ceramide (Cer) is involved in the regulation of several cellular processes by mechanisms that depend on Cer-induced changes on membrane biophysical properties. Accumulating evidence shows that Cers with different N-acyl chain composition differentially impact cell physiology, which may in part be du...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2014-01-01
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| Series: | Journal of Lipid Research |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S0022227520317417 |
| _version_ | 1818727906904375296 |
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| author | Sandra N. Pinto Elad L. Laviad Johnny Stiban Samuel L. Kelly Alfred H. Merrill, Jr. Manuel Prieto Anthony H. Futerman Liana C. Silva |
| author_facet | Sandra N. Pinto Elad L. Laviad Johnny Stiban Samuel L. Kelly Alfred H. Merrill, Jr. Manuel Prieto Anthony H. Futerman Liana C. Silva |
| author_sort | Sandra N. Pinto |
| collection | DOAJ |
| description | Ceramide (Cer) is involved in the regulation of several cellular processes by mechanisms that depend on Cer-induced changes on membrane biophysical properties. Accumulating evidence shows that Cers with different N-acyl chain composition differentially impact cell physiology, which may in part be due to specific alterations in membrane biophysical properties. We now address how the sphingolipid (SL) N-acyl chain affects membrane properties in cultured human embryonic kidney cells by overexpressing different Cer synthases (CerSs). Our results show an increase in the order of cellular membranes in CerS2-transfected cells caused by the enrichment in very long acyl chain SLs. Formation of Cer upon treatment of cells with bacterial sphingomyelinase promoted sequential changes in the properties of the membranes: after an initial increase in the order of the fluid plasma membrane, reorganization into domains with gel-like properties whose characteristics are dependent on the acyl chain structure of the Cer was observed. Moreover, the extent of alterations of membrane properties correlates with the amount of Cer formed. These data reinforce the significance of Cer-induced changes on membrane biophysical properties as a likely molecular mechanism by which different acyl chain Cers exert their specific biological actions. |
| first_indexed | 2024-12-17T22:21:33Z |
| format | Article |
| id | doaj.art-8cac9f22bb484f81b79a079ebbd60a36 |
| institution | Directory Open Access Journal |
| issn | 0022-2275 |
| language | English |
| last_indexed | 2024-12-17T22:21:33Z |
| publishDate | 2014-01-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Lipid Research |
| spelling | doaj.art-8cac9f22bb484f81b79a079ebbd60a362022-12-21T21:30:27ZengElsevierJournal of Lipid Research0022-22752014-01-015515361Changes in membrane biophysical properties induced by sphingomyelinase depend on the sphingolipid N-acyl chainSandra N. Pinto0Elad L. Laviad1Johnny Stiban2Samuel L. Kelly3Alfred H. Merrill, Jr.4Manuel Prieto5Anthony H. Futerman6Liana C. Silva7Centro de Química-Física Molecular and Institute of Nanoscience and Nanotechnology, Instituto Superior Técnico, Universidade de Lisboa, 1049-001 Lisboa, PortugalDepartment of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, IsraelTo whom correspondence should be addressed.; Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, IsraelSchool of Biology and Petit Institute for Bioengineering and Bioscience, Georgia Institute of Technology, Atlanta, GA 30332-0230; andSchool of Biology and Petit Institute for Bioengineering and Bioscience, Georgia Institute of Technology, Atlanta, GA 30332-0230; andCentro de Química-Física Molecular and Institute of Nanoscience and Nanotechnology, Instituto Superior Técnico, Universidade de Lisboa, 1049-001 Lisboa, PortugalDepartment of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, IsraelTo whom correspondence should be addressed.; iMed.UL, Faculdade de Farmácia Universidade de Lisboa, 1649-003 Lisboa, PortugalCeramide (Cer) is involved in the regulation of several cellular processes by mechanisms that depend on Cer-induced changes on membrane biophysical properties. Accumulating evidence shows that Cers with different N-acyl chain composition differentially impact cell physiology, which may in part be due to specific alterations in membrane biophysical properties. We now address how the sphingolipid (SL) N-acyl chain affects membrane properties in cultured human embryonic kidney cells by overexpressing different Cer synthases (CerSs). Our results show an increase in the order of cellular membranes in CerS2-transfected cells caused by the enrichment in very long acyl chain SLs. Formation of Cer upon treatment of cells with bacterial sphingomyelinase promoted sequential changes in the properties of the membranes: after an initial increase in the order of the fluid plasma membrane, reorganization into domains with gel-like properties whose characteristics are dependent on the acyl chain structure of the Cer was observed. Moreover, the extent of alterations of membrane properties correlates with the amount of Cer formed. These data reinforce the significance of Cer-induced changes on membrane biophysical properties as a likely molecular mechanism by which different acyl chain Cers exert their specific biological actions.http://www.sciencedirect.com/science/article/pii/S0022227520317417sphingolipidsacyl chain structureceramidelipid domainsceramide synthasesmembrane remodeling |
| spellingShingle | Sandra N. Pinto Elad L. Laviad Johnny Stiban Samuel L. Kelly Alfred H. Merrill, Jr. Manuel Prieto Anthony H. Futerman Liana C. Silva Changes in membrane biophysical properties induced by sphingomyelinase depend on the sphingolipid N-acyl chain Journal of Lipid Research sphingolipids acyl chain structure ceramide lipid domains ceramide synthases membrane remodeling |
| title | Changes in membrane biophysical properties induced by sphingomyelinase depend on the sphingolipid N-acyl chain |
| title_full | Changes in membrane biophysical properties induced by sphingomyelinase depend on the sphingolipid N-acyl chain |
| title_fullStr | Changes in membrane biophysical properties induced by sphingomyelinase depend on the sphingolipid N-acyl chain |
| title_full_unstemmed | Changes in membrane biophysical properties induced by sphingomyelinase depend on the sphingolipid N-acyl chain |
| title_short | Changes in membrane biophysical properties induced by sphingomyelinase depend on the sphingolipid N-acyl chain |
| title_sort | changes in membrane biophysical properties induced by sphingomyelinase depend on the sphingolipid n acyl chain |
| topic | sphingolipids acyl chain structure ceramide lipid domains ceramide synthases membrane remodeling |
| url | http://www.sciencedirect.com/science/article/pii/S0022227520317417 |
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