ArticleThe Biochemical journal2002
Ceramides increase the activity of the secretory phospholipase A2 and alter its fatty acid specificity.
Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 58 citations in OpenAlex.
- Short-term use of parenteral nutrition with a lipid emulsion containing a mixture of soybean oil, olive oil, medium-chain triglycerides, and fish oil: a randomized double-blind study in preterm infants.JPEN. Journal of parenteral and enteral nutrition · 2012Trial
- Fat of the Gut: Epithelial Phospholipids in Inflammatory Bowel Diseases.International journal of molecular sciences · 2021Review
- Developing preliminary blood metabolomics-based biomarkers of insufficient sleep in humans.Sleep · 2020Article
- Characterization of secretory sphingomyelinase activity, lipoprotein sphingolipid content and LDL aggregation in ldlr-/- mice fed on a high-fat diet.Bioscience reports · 2012Article
- Regulation of phosphatidic Acid metabolism by sphingolipids in the central nervous system.Journal of lipids · 2011Article
- Ceramide acyl chain length markedly influences miscibility with palmitoyl sphingomyelin in bilayer membranes.European biophysics journal : EBJ · 2010Article
- Alterations in the content and physiological role of sphingomyelin in plasma membranes of cells cultured in three-dimensional matrix.Molecular and cellular biochemistry · 2010Article
- The role of ceramide in major depressive disorder.European archives of psychiatry and clinical neuroscience · 2009Review
- Role of sphingomyelin and ceramide in the regulation of the activity and fatty acid specificity of group V secretory phospholipase A2.Archives of biochemistry and biophysics · 2007Article
- Regulation of the activity and fatty acid specificity of lecithin-cholesterol acyltransferase by sphingomyelin and its metabolites, ceramide and ceramide phosphate.Biochemistry · 2006Article
- Phospholipase A2 functions in Pseudomonas aeruginosa-induced apoptosis.Infection and immunity · 2006Article
- High activity of acid sphingomyelinase in major depression.Journal of neural transmission (Vienna, Austria : 1996) · 2005Article
- Modulation of the activity of secretory phospholipase A2 by antimicrobial peptides.Antimicrobial agents and chemotherapy · 2003Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Modulation of human recombinant secretory type II phospholipase A(2) activity by ceramide and cholesterol was investigated using model glycerophospholipid substrates composed of phosphatidylethanolamine and phosphatidylserine dispersed in aqueous medium. Enzyme activity was monitored by measurement of released fatty acids using capillary GC-MS. Fatty acids from the sn-2 position of the phospholipids were hydrolysed by the enzyme in proportion to the relative abundance of the phospholipid in the substrate. Addition of increasing amounts of ceramide to the substrate progressively enhanced phospholipase activity. The increased activity was accomplished largely by preferential hydrolysis of polyunsaturated fatty acids, particularly arachidonic acid, derived from phosphatidylethanolamine. The addition of sphingomyelin to the substrate glycerophospholipids inhibited phospholipase activity but its progressive substitution by ceramide, so as to mimic sphingomyelinase activity, counteracted the inhibition. The presence of cholesterol in dispersions of glycerophospholipid-substrate-containing ceramides suppressed activation of the enzyme resulting from the presence of ceramide. The molecular basis of enzyme modulation was investigated by analysis of the phase structure of the dispersed lipid substrate during temperature scans from 46 to 20 degrees C using small-angle synchrotron X-ray diffraction. These studies indicated that intermediate structures created after ceramide-dependent phase separation of hexagonal and lamellar phases represent the most susceptible form of the substrate for enzyme hydrolysis.
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