ArticleLipids2011
Kinetic analysis of lecithin:cholesterol acyltransferase activity toward discoidal HDL.
Article in Lipids, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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
3 citing papers in PubMed, 6 citations in OpenAlex.
- High-Density Lipoproteins as Homeostatic Nanoparticles of Blood Plasma.International journal of molecular sciences · 2020Review
- ApoA1 and ApoA1-specific self-antibodies in cardiovascular disease.Laboratory investigation; a journal of technical methods and pathology · 2016Review
- Sequence-specific apolipoprotein A-I effects on lecithin:cholesterol acyltransferase activity.Molecular and cellular biochemistry · 2013Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The kinetics of lecithin:cholesterol acyltransferase(LCAT, EC 2.3.1.43)-catalyzed generation of cholesteryl ester in discoidal high density lipoproteins (HDL) was analyzed in terms of initial binding of LCAT to the disc surface followed by a three-state reaction of the hydrolysis of phosphatidylcholine sn-2 ester bond and acyl-enzyme formation. Cholesterol was considered as alcoholic nucleophile that increases the solvolysis rate of acyl-LCAT. The raw kinetic data of Sparks et al. (J Biol Chem 270:5151-5157, 1995) for four preparations of reconstituted discoidal HDL with a constant level of apolipoprotein A-I and palmitoyloleoylphosphatidylcholine per disc but with cholesterol in a lipid phase continuously increasing from 2.1 to 12.5 mol%, were analyzed in terms of the kinetic equation and a complete set of rate constants was obtained. Data at high cholesterol content do not indicate a saturation phenomenon, thus giving no evidence for a binding of cholesterol to the enzyme. This analysis may be used in the study of LCAT activation by exchangeable apolipoproteins and contribution of the HDL structure.
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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.