Pleiotropic effects of apolipoprotein C3 on HDL functionality and adipose tissue metabolic activity[S]
APOC3 is produced mainly by the liver and intestine and approximately half of plasma APOC3 associates with HDL. Though it was believed that APOC3 associates with HDL by simple binding to preexisting particles, recent data support that biogenesis of APOC3-containing HDL (APOC3-HDL) requires Abca1. Mo...
| Main Authors: | , , , , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2017-09-01
|
| Series: | Journal of Lipid Research |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S0022227520339572 |
| _version_ | 1818871381704572928 |
|---|---|
| author | Evangelia Zvintzou Marie Lhomme Stella Chasapi Serafoula Filou Vassilis Theodoropoulos Eva Xapapadaki Anatol Kontush George Spyroulias Constantinos C. Tellis Alexandros D. Tselepis Caterina Constantinou Kyriakos E. Kypreos |
| author_facet | Evangelia Zvintzou Marie Lhomme Stella Chasapi Serafoula Filou Vassilis Theodoropoulos Eva Xapapadaki Anatol Kontush George Spyroulias Constantinos C. Tellis Alexandros D. Tselepis Caterina Constantinou Kyriakos E. Kypreos |
| author_sort | Evangelia Zvintzou |
| collection | DOAJ |
| description | APOC3 is produced mainly by the liver and intestine and approximately half of plasma APOC3 associates with HDL. Though it was believed that APOC3 associates with HDL by simple binding to preexisting particles, recent data support that biogenesis of APOC3-containing HDL (APOC3-HDL) requires Abca1. Moreover, APOC3-HDL contributes to plasma triglyceride homeostasis by preventing APOC3 association with triglyceride-rich lipoproteins. Interestingly, APOC3-HDL also shows positive correlation with the morbidly obese phenotype. However, the roles of APOC3 in HDL functionality and adipose tissue metabolic activity remain unknown. Therefore, here we investigated the direct effects of APOC3 expression on HDL structure and function, as well as white adipose tissue (WAT) and brown adipose tissue (BAT) metabolic activity. C57BL/6 mice were infected with an adenovirus expressing human APOC3 or a recombinant attenuated control adenovirus expressing green fluorescent protein and blood and tissue samples were collected at 5 days postinfection. HDL was then analyzed for its apolipoprotein and lipid composition and particle functionality. Additionally, purified mitochondria from BAT and WAT were analyzed for uncoupling protein 1, cytochrome c (Cytc), and Cytc oxidase subunit 4 protein levels as an indirect measure of their metabolic activity. Serum metabolomic analysis was performed by NMR. Combined, our data show that APOC3 modulates HDL structure and function, while it selectively promotes BAT metabolic activation. |
| first_indexed | 2024-12-19T12:22:01Z |
| format | Article |
| id | doaj.art-e85b5c2769f44b8a9431e82c8ea5a7ce |
| institution | Directory Open Access Journal |
| issn | 0022-2275 |
| language | English |
| last_indexed | 2024-12-19T12:22:01Z |
| publishDate | 2017-09-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Lipid Research |
| spelling | doaj.art-e85b5c2769f44b8a9431e82c8ea5a7ce2022-12-21T20:21:45ZengElsevierJournal of Lipid Research0022-22752017-09-0158918691883Pleiotropic effects of apolipoprotein C3 on HDL functionality and adipose tissue metabolic activity[S]Evangelia Zvintzou0Marie Lhomme1Stella Chasapi2Serafoula Filou3Vassilis Theodoropoulos4Eva Xapapadaki5Anatol Kontush6George Spyroulias7Constantinos C. Tellis8Alexandros D. Tselepis9Caterina Constantinou10Kyriakos E. Kypreos11Pharmacology Department, University of Patras Medical School, Rio Achaias TK 26500, GreeceICANalytics and INSERM UMR_S 1166, ICAN, 75013 Paris, FranceDepartment of Pharmacy, University of Patras, 26504 Patras, GreecePharmacology Department, University of Patras Medical School, Rio Achaias TK 26500, GreecePharmacology Department, University of Patras Medical School, Rio Achaias TK 26500, GreecePharmacology Department, University of Patras Medical School, Rio Achaias TK 26500, GreeceFaculté de Médecine Pitié-Salpêtrière, ICAN, 75013 Paris, FranceDepartment of Pharmacy, University of Patras, 26504 Patras, GreeceLaboratory of Biochemistry, Department of Chemistry, University of Ioannina, 45110 Ioannina, GreeceLaboratory of Biochemistry, Department of Chemistry, University of Ioannina, 45110 Ioannina, GreecePharmacology Department, University of Patras Medical School, Rio Achaias TK 26500, GreeceTo whom correspondence should be addressed.; Pharmacology Department, University of Patras Medical School, Rio Achaias TK 26500, Greece; To whom correspondence should be addressed.APOC3 is produced mainly by the liver and intestine and approximately half of plasma APOC3 associates with HDL. Though it was believed that APOC3 associates with HDL by simple binding to preexisting particles, recent data support that biogenesis of APOC3-containing HDL (APOC3-HDL) requires Abca1. Moreover, APOC3-HDL contributes to plasma triglyceride homeostasis by preventing APOC3 association with triglyceride-rich lipoproteins. Interestingly, APOC3-HDL also shows positive correlation with the morbidly obese phenotype. However, the roles of APOC3 in HDL functionality and adipose tissue metabolic activity remain unknown. Therefore, here we investigated the direct effects of APOC3 expression on HDL structure and function, as well as white adipose tissue (WAT) and brown adipose tissue (BAT) metabolic activity. C57BL/6 mice were infected with an adenovirus expressing human APOC3 or a recombinant attenuated control adenovirus expressing green fluorescent protein and blood and tissue samples were collected at 5 days postinfection. HDL was then analyzed for its apolipoprotein and lipid composition and particle functionality. Additionally, purified mitochondria from BAT and WAT were analyzed for uncoupling protein 1, cytochrome c (Cytc), and Cytc oxidase subunit 4 protein levels as an indirect measure of their metabolic activity. Serum metabolomic analysis was performed by NMR. Combined, our data show that APOC3 modulates HDL structure and function, while it selectively promotes BAT metabolic activation.http://www.sciencedirect.com/science/article/pii/S0022227520339572cholesterol effluxhigh density lipoproteinlipidomicsmetabolomicsbrown adipose tissuewhite adipose tissue |
| spellingShingle | Evangelia Zvintzou Marie Lhomme Stella Chasapi Serafoula Filou Vassilis Theodoropoulos Eva Xapapadaki Anatol Kontush George Spyroulias Constantinos C. Tellis Alexandros D. Tselepis Caterina Constantinou Kyriakos E. Kypreos Pleiotropic effects of apolipoprotein C3 on HDL functionality and adipose tissue metabolic activity[S] Journal of Lipid Research cholesterol efflux high density lipoprotein lipidomics metabolomics brown adipose tissue white adipose tissue |
| title | Pleiotropic effects of apolipoprotein C3 on HDL functionality and adipose tissue metabolic activity[S] |
| title_full | Pleiotropic effects of apolipoprotein C3 on HDL functionality and adipose tissue metabolic activity[S] |
| title_fullStr | Pleiotropic effects of apolipoprotein C3 on HDL functionality and adipose tissue metabolic activity[S] |
| title_full_unstemmed | Pleiotropic effects of apolipoprotein C3 on HDL functionality and adipose tissue metabolic activity[S] |
| title_short | Pleiotropic effects of apolipoprotein C3 on HDL functionality and adipose tissue metabolic activity[S] |
| title_sort | pleiotropic effects of apolipoprotein c3 on hdl functionality and adipose tissue metabolic activity s |
| topic | cholesterol efflux high density lipoprotein lipidomics metabolomics brown adipose tissue white adipose tissue |
| url | http://www.sciencedirect.com/science/article/pii/S0022227520339572 |
| work_keys_str_mv | AT evangeliazvintzou pleiotropiceffectsofapolipoproteinc3onhdlfunctionalityandadiposetissuemetabolicactivitys AT marielhomme pleiotropiceffectsofapolipoproteinc3onhdlfunctionalityandadiposetissuemetabolicactivitys AT stellachasapi pleiotropiceffectsofapolipoproteinc3onhdlfunctionalityandadiposetissuemetabolicactivitys AT serafoulafilou pleiotropiceffectsofapolipoproteinc3onhdlfunctionalityandadiposetissuemetabolicactivitys AT vassilistheodoropoulos pleiotropiceffectsofapolipoproteinc3onhdlfunctionalityandadiposetissuemetabolicactivitys AT evaxapapadaki pleiotropiceffectsofapolipoproteinc3onhdlfunctionalityandadiposetissuemetabolicactivitys AT anatolkontush pleiotropiceffectsofapolipoproteinc3onhdlfunctionalityandadiposetissuemetabolicactivitys AT georgespyroulias pleiotropiceffectsofapolipoproteinc3onhdlfunctionalityandadiposetissuemetabolicactivitys AT constantinosctellis pleiotropiceffectsofapolipoproteinc3onhdlfunctionalityandadiposetissuemetabolicactivitys AT alexandrosdtselepis pleiotropiceffectsofapolipoproteinc3onhdlfunctionalityandadiposetissuemetabolicactivitys AT caterinaconstantinou pleiotropiceffectsofapolipoproteinc3onhdlfunctionalityandadiposetissuemetabolicactivitys AT kyriakosekypreos pleiotropiceffectsofapolipoproteinc3onhdlfunctionalityandadiposetissuemetabolicactivitys |