Quantitative profiling of the endonuclear glycerophospholipidome of murine embryonic fibroblasts[S]
A reliable method for purifying envelope-stripped nuclei from immortalized murine embryonic fibroblasts (iMEFs) was established. Quantitative profiling of the glycerophospholipids (GPLs) in envelope-free iMEF nuclei yields several conclusions. First, we find the endonuclear glycerophospholipidome di...
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| Published in | Journal of lipid research Vol. 57; no. 8; pp. 1492 - 1506 |
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| Main Authors | , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
01.08.2016
The American Society for Biochemistry and Molecular Biology Elsevier |
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| Online Access | Get full text |
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| Abstract | A reliable method for purifying envelope-stripped nuclei from immortalized murine embryonic fibroblasts (iMEFs) was established. Quantitative profiling of the glycerophospholipids (GPLs) in envelope-free iMEF nuclei yields several conclusions. First, we find the endonuclear glycerophospholipidome differs from that of bulk membranes, and phosphatidylcholine (PtdCho) and phosphatidylethanolamine species are the most abundant endonuclear GPLs by mass. By contrast, phosphatidylinositol (PtdIns) represents a minor species. We also find only a slight enrichment of saturated versus unsaturated GPL species in iMEF endonuclear fractions. Moreover, much lower values for GPL mass were measured in the iMEF nuclear matrix than those reported for envelope-stripped IMF-32 nuclei. The collective results indicate that the nuclear matrix in these cells is a GPL-poor environment where GPL occupies only approximately 0.1% of the total nuclear matrix volume. This value suggests GPL accommodation in this compartment can be satisfied by binding to resident proteins. Finally, we find no significant role for the PtdIns/PtdCho-transfer protein, PITPα, in shuttling PtdIns into the iMEF nuclear matrix. |
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| AbstractList | A reliable method for purifying envelope-stripped nuclei from immortalized murine embryonic fibroblasts (iMEFs) was established. Quantitative profiling of the glycerophospholipids (GPLs) in envelope-free iMEF nuclei yields several conclusions. First, we find the endonuclear glycerophospholipidome differs from that of bulk membranes, and phosphatidylcholine (PtdCho) and phosphatidylethanolamine species are the most abundant endonuclear GPLs by mass. By contrast, phosphatidylinositol (PtdIns) represents a minor species. We also find only a slight enrichment of saturated versus unsaturated GPL species in iMEF endonuclear fractions. Moreover, much lower values for GPL mass were measured in the iMEF nuclear matrix than those reported for envelope-stripped IMF-32 nuclei. The collective results indicate that the nuclear matrix in these cells is a GPL-poor environment where GPL occupies only approximately 0.1% of the total nuclear matrix volume. This value suggests GPL accommodation in this compartment can be satisfied by binding to resident proteins. Finally, we find no significant role for the PtdIns/PtdCho-transfer protein, PITPα, in shuttling PtdIns into the iMEF nuclear matrix. A reliable method for purifying envelope-stripped nuclei from immortalized murine embryonic fibroblasts (iMEFs) was established. Quantitative profiling of the glycerophospholipids (GPLs) in envelope-free iMEF nuclei yields several conclusions. First, we find the endonuclear glycerophospholipidome differs from that of bulk membranes, and phosphatidylcholine (PtdCho) and phosphatidylethanolamine species are the most abundant endonuclear GPLs by mass. By contrast, phosphatidylinositol (PtdIns) represents a minor species. We also find only a slight enrichment of saturated versus unsaturated GPL species in iMEF endonuclear fractions. Moreover, much lower values for GPL mass were measured in the iMEF nuclear matrix than those reported for envelope-stripped IMF-32 nuclei. The collective results indicate that the nuclear matrix in these cells is a GPL-poor environment where GPL occupies only approximately 0.1% of the total nuclear matrix volume. This value suggests GPL accommodation in this compartment can be satisfied by binding to resident proteins. Finally, we find no significant role for the PtdIns/PtdCho-transfer protein, PITPα, in shuttling PtdIns into the iMEF nuclear matrix.A reliable method for purifying envelope-stripped nuclei from immortalized murine embryonic fibroblasts (iMEFs) was established. Quantitative profiling of the glycerophospholipids (GPLs) in envelope-free iMEF nuclei yields several conclusions. First, we find the endonuclear glycerophospholipidome differs from that of bulk membranes, and phosphatidylcholine (PtdCho) and phosphatidylethanolamine species are the most abundant endonuclear GPLs by mass. By contrast, phosphatidylinositol (PtdIns) represents a minor species. We also find only a slight enrichment of saturated versus unsaturated GPL species in iMEF endonuclear fractions. Moreover, much lower values for GPL mass were measured in the iMEF nuclear matrix than those reported for envelope-stripped IMF-32 nuclei. The collective results indicate that the nuclear matrix in these cells is a GPL-poor environment where GPL occupies only approximately 0.1% of the total nuclear matrix volume. This value suggests GPL accommodation in this compartment can be satisfied by binding to resident proteins. Finally, we find no significant role for the PtdIns/PtdCho-transfer protein, PITPα, in shuttling PtdIns into the iMEF nuclear matrix. A reliable method for purifying envelope-stripped nuclei from immortalized murine embryonic fibroblasts (iMEFs) was established. Quantitative profiling of the glycerophospholipids (GPLs) in envelope-free iMEF nuclei yields several conclusions. First, we find the endonuclear glycerophospholipidome differs from that of bulk membranes, and phosphatidylcholine (PtdCho) and phosphatidylethanolamine species are the most abundant endonuclear GPLs by mass. By contrast, phosphatidylinositol (PtdIns) represents a minor species. We also find only a slight enrichment of saturated versus unsaturated GPL species in iMEF endonuclear fractions. Moreover, much lower values for GPL mass were measured in the iMEF nuclear matrix than those reported for envelope-stripped IMF-32 nuclei. The collective results indicate that the nuclear matrix in these cells is a GPL-poor environment where GPL occupies only approximately 0.1% of the total nuclear matrix volume. This value suggests GPL accommodation in this compartment can be satisfied by binding to resident proteins. Finally, we find no significant role for the PtdIns/PtdCho-transfer protein, PITP alpha , in shuttling PtdIns into the iMEF nuclear matrix. |
| Author | Cocco, Lucio Tribble, Emily K. Faenza, Irene Bankaitis, Vytas A. Alb, James G. Brown, H. Alex Ivanova, Pavlina T. Grabon, Aby |
| Author_xml | – sequence: 1 givenname: Emily K. surname: Tribble fullname: Tribble, Emily K. email: Emily.k.tribble@gmail.com organization: Lineberger Comprehensive Cancer Center,University of North Carolina School of Medicine, Chapel Hill, NC – sequence: 2 givenname: Pavlina T. surname: Ivanova fullname: Ivanova, Pavlina T. organization: Departments of Pharmacology and Biochemistry,Vanderbilt University School of Medicine, Vanderbilt Institute of Chemical Biology, Nashville, TN – sequence: 3 givenname: Aby surname: Grabon fullname: Grabon, Aby organization: Lineberger Comprehensive Cancer Center,University of North Carolina School of Medicine, Chapel Hill, NC – sequence: 4 givenname: James G. surname: Alb fullname: Alb, James G. organization: Lineberger Comprehensive Cancer Center,University of North Carolina School of Medicine, Chapel Hill, NC – sequence: 5 givenname: Irene surname: Faenza fullname: Faenza, Irene organization: Cellular Signaling Laboratory, Department of Biomedical Sciences, University of Bologna, Bologna, Italy – sequence: 6 givenname: Lucio surname: Cocco fullname: Cocco, Lucio organization: Cellular Signaling Laboratory, Department of Biomedical Sciences, University of Bologna, Bologna, Italy – sequence: 7 givenname: H. Alex surname: Brown fullname: Brown, H. Alex organization: Departments of Pharmacology and Biochemistry,Vanderbilt University School of Medicine, Vanderbilt Institute of Chemical Biology, Nashville, TN – sequence: 8 givenname: Vytas A. surname: Bankaitis fullname: Bankaitis, Vytas A. email: vytas@tamhsc.edu organization: Lineberger Comprehensive Cancer Center,University of North Carolina School of Medicine, Chapel Hill, NC |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/27256690$$D View this record in MEDLINE/PubMed |
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| Keywords | lipids phospholipids/phosphatidylinositol nuclear receptors/lipid ligands phospholipids/metabolism cell signaling |
| Language | English |
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| SubjectTerms | Animals Cell Nucleus - metabolism Cell Nucleus - ultrastructure cell signaling Cells, Cultured Embryo, Mammalian - chemistry Fibroblasts - metabolism Fibroblasts - ultrastructure lipids Mice Nuclear Envelope - metabolism nuclear receptors/lipid ligands Phospholipid Transfer Proteins - metabolism Phospholipids - metabolism phospholipids/phosphatidylinositol |
| Title | Quantitative profiling of the endonuclear glycerophospholipidome of murine embryonic fibroblasts[S] |
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