ArticleThe Journal of biological chemistry2015
A Pressure-dependent Model for the Regulation of Lipoprotein Lipase by Apolipoprotein C-II.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
19 citing papers in PubMed, 32 citations in OpenAlex.
- Lipoprotein lipase requires a flexible lid and stable C-terminal, both maintained by ApoC-II peptide binding.bioRxiv : the preprint server for biology · 2025Article
- Changes in apolipoproteins following ingestion of a beverage deliveringFrontiers in nutrition · 2025Article
- Macromolecular Interactions of Lipoprotein Lipase (LPL).Sub-cellular biochemistry · 2024Review
- Use of Apolipoprotein B in the Era of Precision Medicine: Time for a Paradigm Change?Journal of clinical medicine · 2023Review
- Quartet of APOCs and the Different Roles They Play in Diabetes.Arteriosclerosis, thrombosis, and vascular biology · 2023Review
- Integrated Quantitative Targeted Lipidomics and Proteomics Reveal Unique Fingerprints of Multiple Metabolic Conditions.Biomolecules · 2022Article
- Apolipoproteins in vascular biology and atherosclerotic disease.Nature reviews. Cardiology · 2022Review
- Lipoprotein size is a main determinant for the rate of hydrolysis by exogenous LPL in human plasma.Journal of lipid research · 2022Article
- Apolipoprotein E content of VLDL limits LPL-mediated triglyceride hydrolysis.Journal of lipid research · 2022Article
- The Importance of Lipoprotein Lipase Regulation in Atherosclerosis.Biomedicines · 2021Review
- Review
- A dual apolipoprotein C-II mimetic-apolipoprotein C-III antagonist peptide lowers plasma triglycerides.Science translational medicine · 2020Article
- Development and application of a high throughput one-pot extraction protocol for quantitative LC-MS/MS analysis of phospholipids in serum and lipoprotein fractions in normolipidemic and dyslipidemic subjects.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2019Article
- Dual binding motifs underpin the hierarchical association of perilipins1-3 with lipid droplets.Molecular biology of the cell · 2019Article
- Apolipoprotein C-II Mimetic Peptide Promotes the Plasma Clearance of Triglyceride-Rich Lipid Emulsion and the Incorporation of Fatty Acids into Peripheral Tissues of Mice.Journal of nutrition and metabolism · 2019Article
- Apolipoprotein C-II: New findings related to genetics, biochemistry, and role in triglyceride metabolism.Atherosclerosis · 2017Review
- Aromatic residues in the C terminus of apolipoprotein C-III mediate lipid binding and LPL inhibition.Journal of lipid research · 2017Article
- Triglyceride-Rich Lipoproteins and Remnants: Targets for Therapy?Current cardiology reports · 2016Review
- Association of the lipoprotein lipase and Apolipoprotein C-II gene polymorphisms with risk of dyslipidemia in smokers and non-smokers male.Indian heart journalArticle
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.