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May 30, 2015Journal of Biological ChemistryOpen Access

A Pressure-dependent Model for the Regulation of Lipoprotein Lipase by Apolipoprotein C-II

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Population

Lipid/water interfaces mimicking lipoprotein surfaces

Design

Preclinical

Authors

NMNathan L. MeyersGladstone InstitutesMLMikael LarssonCentre National de la Recherche ScientifiqueGOGunilla OlivecronaLipigon Pharmaceuticals (Sweden)

Discussion

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Implication

Elucidates apoC-II interfacial adaptation; leaves open physiological validation for LPL regulation.

Structured PICO

P
Population
Lipid/water interfaces (triacylglycerol/water and phospholipid/triacylglycerol/water) mimicking lipoprotein surfaces
I
Intervention
Interfacial compressions mimicking the action of lipoprotein lipase (LPL)
O
Outcome
ApoC-II adsorption, desorption, and surface pressure changessurrogate

ApoC-II regulates lipoprotein lipase activity through a pressure-dependent mechanism, where increased surface pressure leads to apoC-II desorption and subsequent LPL release.

Cite This Study

Meyers et al. (2015) studied this question.

synapsesocial.com/papers/6a70e368e71d69abee08ec12https://doi.org/10.1074/jbc.m114.629865
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Also Consider

Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Mechanisms of inhibition by apolipoprotein C of apolipoprotein E-dependent cellular metabolism of human triglyceride-rich lipoproteins through the low density lipoprotein receptor pathway.1991 · 285 citations
  2. 2Changes in helical content or net charge of apolipoprotein C-I alter its affinity for lipid/water interfaces2013 · 15 citations
  3. 3Functional Analyses of Human Apolipoprotein CII by Site-directed Mutagenesis2002 · 49 citations
  4. 4Surface behavior of apolipoprotein A-I and its deletion mutants at model lipoprotein interfaces2013 · 19 citations