ArticleThe Biochemical journal1998
Cholesterol relieves the inhibitory effect of sphingomyelin on type II secretory phospholipase A2.
Article in The Biochemical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
8 citing papers in PubMed, 40 citations in OpenAlex.
- Novel Lipids to Regulate Obesity and Brain Function: Comparing Available Evidence and Insights from QSAR In Silico Models.Foods (Basel, Switzerland) · 2023Review
- The Synergy of Membranotropic Effect of the Two PlaThe Journal of membrane biology · 2020Article
- Review
- Dietary sphingomyelin lowers hepatic lipid levels and inhibits intestinal cholesterol absorption in high-fat-fed mice.PloS one · 2013Article
- Guanidination of notexin alters its membrane-damaging activity in response to sphingomyelin and cholesterol.Journal of biosciences · 2010Article
- Ceramide acyl chain length markedly influences miscibility with palmitoyl sphingomyelin in bilayer membranes.European biophysics journal : EBJ · 2010Article
- Effects of cholesterol on physical properties of human erythrocyte membranes: impact on susceptibility to hydrolysis by secretory phospholipase A2.Biophysical journal · 2008Article
- Ceramides increase the activity of the secretory phospholipase A2 and alter its fatty acid specificity.The Biochemical journal · 2002Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Secretory type II phospholipase A2 (sPLA2) is inhibited by sphingomyelin (SPH); cholesterol either mixed with the model glycerophospholipid substrate or added to the assay medium as separated liposomes counteracts this inhibition efficiently. The inhibition of fatty acid release assayed by quantitative gas chromatography-MS is observed when SPH is added to erythrocyte membranes as the substrate instead of a readily hydrolysable phosphatidylethanolamine/phosphatidylserine model mixture. Hydrolysis of SPH by Staphylococcus aureus sphingomyelinase suppresses its inhibitory potency. The addition of cholesterol to SPH liposomes with a 1:1 stoichiometry relieves completely the inhibition of sPLA2 exerted by SPH. The mechanism of inhibition suggested by the binding assay is that sPLA2 binds with affinity to the SPH interface, after either phase segregation at the assay temperature or on the pure SPH liposomes added to the incubation medium. Cholesterol is shown to suppress the binding affinity of the enzyme for the SPH interface. A model for inhibition is suggested in which binding of the sphingosine moiety is competitive for sPLA2 (inhibition) or for cholesterol (release of the enzyme).
Indexed as
Identifiers
What OpenQuestion holds
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.