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A Pressure-dependent Model for the Regulation of Lipoprotein Lipase by Apolipoprotein C-II
Umeå University, Faculty of Medicine, Department of Medical Biosciences, Physiological chemistry. Department of Medicine, UCLA, Los Angeles, California.
Umeå University, Faculty of Medicine, Department of Medical Biosciences, Physiological chemistry.
2015 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 290, no 29, 18029-18044 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
Bethesda: American Society for Biochemistry and Molecular Biology, 2015. Vol. 290, no 29, 18029-18044 p.
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Identifiers
URN: urn:nbn:se:umu:diva-107297DOI: 10.1074/jbc.M114.629865ISI: 000358511700035PubMedID: 26026161OAI: oai:DiVA.org:umu-107297DiVA: diva2:849134
Available from: 2015-08-27 Created: 2015-08-21 Last updated: 2017-12-04Bibliographically approved

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Larsson, MikaelOlivecrona, Gunilla
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