GPIHBP1 expression in gliomas promotes utilization of lipoprotein-derived nutrients
GPIHBP1, a GPI-anchored protein of capillary endothelial cells, binds lipoprotein lipase (LPL) within the subendothelial spaces and shuttles it to the capillary lumen. GPIHBP1-bound LPL is essential for the margination of triglyceride-rich lipoproteins (TRLs) along capillaries, allowing the lipolyti...
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2019-06-01
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| Series: | eLife |
| Subjects: | |
| Online Access: | https://elifesciences.org/articles/47178 |
| id |
doaj-c9e3de5bd1f74f16b0b5035d702b97d3 |
|---|---|
| record_format |
Article |
| collection |
DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| author |
Xuchen Hu Ken Matsumoto Rachel S Jung Thomas A Weston Patrick J Heizer Cuiwen He Norma P Sandoval Christopher M Allan Yiping Tu Harry V Vinters Linda M Liau Rochelle M Ellison Jazmin E Morales Lynn J Baufeld Nicholas A Bayley Liqun He Christer Betsholtz Anne P Beigneux David A Nathanson Holger Gerhardt Stephen G Young Loren G Fong Haibo Jiang |
| spellingShingle |
Xuchen Hu Ken Matsumoto Rachel S Jung Thomas A Weston Patrick J Heizer Cuiwen He Norma P Sandoval Christopher M Allan Yiping Tu Harry V Vinters Linda M Liau Rochelle M Ellison Jazmin E Morales Lynn J Baufeld Nicholas A Bayley Liqun He Christer Betsholtz Anne P Beigneux David A Nathanson Holger Gerhardt Stephen G Young Loren G Fong Haibo Jiang GPIHBP1 expression in gliomas promotes utilization of lipoprotein-derived nutrients eLife endothelial cells lipoprotein lipase cancer metabolism lipolysis triglycerides NanoSIMS |
| author_facet |
Xuchen Hu Ken Matsumoto Rachel S Jung Thomas A Weston Patrick J Heizer Cuiwen He Norma P Sandoval Christopher M Allan Yiping Tu Harry V Vinters Linda M Liau Rochelle M Ellison Jazmin E Morales Lynn J Baufeld Nicholas A Bayley Liqun He Christer Betsholtz Anne P Beigneux David A Nathanson Holger Gerhardt Stephen G Young Loren G Fong Haibo Jiang |
| author_sort |
Xuchen Hu |
| title |
GPIHBP1 expression in gliomas promotes utilization of lipoprotein-derived nutrients |
| title_short |
GPIHBP1 expression in gliomas promotes utilization of lipoprotein-derived nutrients |
| title_full |
GPIHBP1 expression in gliomas promotes utilization of lipoprotein-derived nutrients |
| title_fullStr |
GPIHBP1 expression in gliomas promotes utilization of lipoprotein-derived nutrients |
| title_full_unstemmed |
GPIHBP1 expression in gliomas promotes utilization of lipoprotein-derived nutrients |
| title_sort |
gpihbp1 expression in gliomas promotes utilization of lipoprotein-derived nutrients |
| publisher |
eLife Sciences Publications Ltd |
| series |
eLife |
| issn |
2050-084X |
| publishDate |
2019-06-01 |
| description |
GPIHBP1, a GPI-anchored protein of capillary endothelial cells, binds lipoprotein lipase (LPL) within the subendothelial spaces and shuttles it to the capillary lumen. GPIHBP1-bound LPL is essential for the margination of triglyceride-rich lipoproteins (TRLs) along capillaries, allowing the lipolytic processing of TRLs to proceed. In peripheral tissues, the intravascular processing of TRLs by the GPIHBP1–LPL complex is crucial for the generation of lipid nutrients for adjacent parenchymal cells. GPIHBP1 is absent from the capillaries of the brain, which uses glucose for fuel; however, GPIHBP1 is expressed in the capillaries of mouse and human gliomas. Importantly, the GPIHBP1 in glioma capillaries captures locally produced LPL. We use NanoSIMS imaging to show that TRLs marginate along glioma capillaries and that there is uptake of TRL-derived lipid nutrients by surrounding glioma cells. Thus, GPIHBP1 expression in gliomas facilitates TRL processing and provides a source of lipid nutrients for glioma cells. |
| topic |
endothelial cells lipoprotein lipase cancer metabolism lipolysis triglycerides NanoSIMS |
| url |
https://elifesciences.org/articles/47178 |
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doaj-c9e3de5bd1f74f16b0b5035d702b97d32021-05-05T17:39:40ZengeLife Sciences Publications LtdeLife2050-084X2019-06-01810.7554/eLife.47178GPIHBP1 expression in gliomas promotes utilization of lipoprotein-derived nutrientsXuchen Hu0https://orcid.org/0000-0002-0944-624XKen Matsumoto1Rachel S Jung2Thomas A Weston3Patrick J Heizer4Cuiwen He5Norma P Sandoval6Christopher M Allan7Yiping Tu8Harry V Vinters9Linda M Liau10Rochelle M Ellison11Jazmin E Morales12Lynn J Baufeld13Nicholas A Bayley14Liqun He15Christer Betsholtz16Anne P Beigneux17David A Nathanson18Holger Gerhardt19https://orcid.org/0000-0002-3030-0384Stephen G Young20https://orcid.org/0000-0001-7270-3176Loren G Fong21https://orcid.org/0000-0002-4465-5290Haibo Jiang22https://orcid.org/0000-0002-2384-4826Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United StatesVIB-KU Leuven Center for Cancer Biology (CCB), Leuven, BelgiumDepartment of Medicine, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United StatesDepartment of Medicine, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United StatesDepartment of Medicine, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United StatesDepartment of Medicine, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United StatesDepartment of Medicine, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United StatesDepartment of Medicine, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United StatesDepartment of Medicine, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United StatesDepartment of Pathology and Laboratory Medicine, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United StatesDepartment of Neurosurgery, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United States; Jonsson Comprehensive Cancer Center (JCCC), David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United StatesDepartment of Medicine, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United StatesDepartment of Medicine, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United StatesDepartment of Molecular and Medical Pharmacology, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United States; Ahmanson Translational Imaging Division, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United StatesDepartment of Molecular and Medical Pharmacology, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United States; Ahmanson Translational Imaging Division, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United StatesDepartment of Immunology, Genetics and Pathology, Rudbeck Laboratory, Uppsala University, Uppsala, SwedenDepartment of Immunology, Genetics and Pathology, Rudbeck Laboratory, Uppsala University, Uppsala, Sweden; Integrated Cardio Metabolic Centre (ICMC), Karolinska Institutet, Huddinge, SwedenDepartment of Medicine, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United StatesDepartment of Molecular and Medical Pharmacology, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United States; Ahmanson Translational Imaging Division, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United StatesVIB-KU Leuven Center for Cancer Biology (CCB), Leuven, Belgium; Max Delbrück Center for Molecular Medicine, Berlin, GermanyDepartment of Medicine, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United States; Department of Human Genetics, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United StatesDepartment of Medicine, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United StatesDepartment of Medicine, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United States; School of Molecular Sciences, University of Western Australia, Perth, AustraliaGPIHBP1, a GPI-anchored protein of capillary endothelial cells, binds lipoprotein lipase (LPL) within the subendothelial spaces and shuttles it to the capillary lumen. GPIHBP1-bound LPL is essential for the margination of triglyceride-rich lipoproteins (TRLs) along capillaries, allowing the lipolytic processing of TRLs to proceed. In peripheral tissues, the intravascular processing of TRLs by the GPIHBP1–LPL complex is crucial for the generation of lipid nutrients for adjacent parenchymal cells. GPIHBP1 is absent from the capillaries of the brain, which uses glucose for fuel; however, GPIHBP1 is expressed in the capillaries of mouse and human gliomas. Importantly, the GPIHBP1 in glioma capillaries captures locally produced LPL. We use NanoSIMS imaging to show that TRLs marginate along glioma capillaries and that there is uptake of TRL-derived lipid nutrients by surrounding glioma cells. Thus, GPIHBP1 expression in gliomas facilitates TRL processing and provides a source of lipid nutrients for glioma cells.https://elifesciences.org/articles/47178endothelial cellslipoprotein lipasecancer metabolismlipolysistriglyceridesNanoSIMS |