ArticleJournal of lipid research2021
rHDL modeling and the anchoring mechanism of LCAT activation.
Article in Journal of lipid research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- Decoding the crosstalk: interplay between macrophage programmed cell death networks and cholesterol efflux.Frontiers in cardiovascular medicine · 2026Review
- Dysfunction of the ABCA1 and ABCG1 Transporters and Their Impact on HDL Metabolism.Antioxidants (Basel, Switzerland) · 2025Review
- Comparison of cholesterol transport capacity of peptide- and polymer-based lipid Nanodiscs.Nanomedicine : nanotechnology, biology, and medicine · 2025Article
- Foam fractionation studies of recombinant human apolipoprotein A-I.Biochimica et biophysica acta. Biomembranes · 2024Article
- In Silico Description of the Direct Inhibition Mechanism of Endothelial Lipase by ANGPTL3.International journal of molecular sciences · 2024Article
- Metabolomics and Lipidomics Study Unveils the Impact of Tauroursodeoxycholic Acid on Hyperlipidemic Mice.Molecules (Basel, Switzerland) · 2023Article
- The roles of hepatokine and osteokine in liver-bone crosstalk: Advance in basic and clinical aspects.Frontiers in endocrinology · 2023Review
- Analysis of the orientation of cholesterol in high-density lipoprotein nanodiscs using solid-state NMR.Physical chemistry chemical physics : PCCP · 2022Article
- Influence of lecithin cholesterol acyltransferase alteration during different pathophysiologic conditions: A 45 years bibliometrics analysis.Frontiers in pharmacology · 2022Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lecithin:cholesterol-acyl transferase (LCAT) plays a major role in cholesterol metabolism as it is the only extracellular enzyme able to esterify cholesterol. LCAT activity is required for lipoprotein remodeling and, most specifically, for the growth and maturation of HDLs. In fact, genetic alterations affecting LCAT functionality may cause a severe reduction in plasma levels of HDL-cholesterol with important clinical consequences. Although several hypotheses were formulated, the exact molecular recognition mechanism between LCAT and HDLs is still unknown. We employed a combination of structural bioinformatics procedures to deepen the insights into the HDL-LCAT interplay that promotes LCAT activation and cholesterol esterification. We have generated a data-driven model of reconstituted HDL (rHDL) and studied the dynamics of an assembled rHDL::LCAT supramolecular complex, pinpointing the conformational changes originating from the interaction between LCAT and apolipoprotein A-I (apoA-I) that are necessary for LCAT activation. Specifically, we propose a mechanism in which the anchoring of LCAT lid to apoA-I helices allows the formation of a hydrophobic hood that expands the LCAT active site and shields it from the solvent, allowing the enzyme to process large hydrophobic substrates.
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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.