Electronic Resource
A Pressure-dependent Model for the Regulation of Lipoprotein Lipase by Apolipoprotein C-II
| العنوان: | A Pressure-dependent Model for the Regulation of Lipoprotein Lipase by Apolipoprotein C-II |
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| المؤلفون: | Meyers, Nathan L, Larsson, Mikael, Olivecrona, Gunilla, Small, Donald M |
| بيانات النشر: | Umeå universitet, Fysiologisk kemi Umeå universitet, Fysiologisk kemi Department of Medicine, UCLA, Los Angeles, California Bethesda 2015 |
| نوع الوثيقة: | Electronic Resource |
| مستخلص: | Apolipoprotein C-II (apoC-II) is the co-factor for lipoprotein lipase (LPL) at the surface of triacylglycerol-rich lipoproteins. LPL hydrolyzes triacylglycerol, which increases local surface pressure as surface area decreases and amphipathic products transiently accumulate at the lipoprotein surface. To understand how apoC-II adapts to these pressure changes, we characterized the behavior of apoC-II at multiple lipid/water interfaces. ApoC-II adsorption to a triacylglycerol/water interface resulted in large increases in surface pressure. ApoC-II was exchangeable at this interface and desorbed on interfacial compressions. These compressions increase surface pressure and mimic the action of LPL. Analysis of gradual compressions showed that apoC-II undergoes a two-step desorption, which indicates that lipid-bound apoC-II can exhibit at least two conformations. We characterized apoC-II at phospholipid/triacylglycerol/water interfaces, which more closely mimic lipoprotein surfaces. ApoC-II had a large exclusion pressure, similar to that of apoC-I and apoC-III. However, apoC-II desorbed at retention pressures higher than those seen with the other apoCs. This suggests that it is unlikely that apoC-I and apoC-III inhibit LPL via displacement of apoC-II from the lipoprotein surface. Upon rapid compressions and re-expansions, re-adsorption of apoC-II increased pressure by lower amounts than its initial adsorption. This indicates that apoC-II removed phospholipid from the interface upon desorption. These results suggest that apoC-II regulates the activity of LPL in a pressure-dependent manner. ApoC-II is provided as a component of triacylglycerol-rich lipoproteins and is the co-factor for LPL as pressure increases. Above its retention pressure, apoC-II desorbs and removes phospholipid. This triggers release of LPL from lipoproteins. |
| مصطلحات الفهرس: | Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy), Medicinsk bioteknologi (med inriktning mot cellbiologi (inklusive stamcellsbiologi), molekylärbiologi, mikrobiologi, biokemi eller biofarmaci), Article in journal, info:eu-repo/semantics/article, text |
| DOI: | 10.1074.jbc.M114.629865 |
| URL: | Journal of Biological Chemistry, 0021-9258, 2015, 290:29, s. 18029-18044 |
| الاتاحة: | Open access content. Open access content info:eu-repo/semantics/restrictedAccess |
| ملاحظة: | English |
| Other Numbers: | UPE oai:DiVA.org:umu-107297 doi:10.1074/jbc.M114.629865 PMID 26026161 ISI:000358511700035 1233611311 |
| المصدر المساهم: | UPPSALA UNIV LIBR From OAIster®, provided by the OCLC Cooperative. |
| رقم الانضمام: | edsoai.on1233611311 |
| قاعدة البيانات: | OAIster |
| DOI: | 10.1074.jbc.M114.629865 |
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