Partial coverage of phospholipid model membranes with annexin V may completely inhibit their degradation by phospholipase A2
| Autor: | Chris P. M. Reutelingsperger, Wim Th. Hermens, Sylvia W.S. Jans, C. Erik Hack, Ger J. van der Vusse, Han Speijer |
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| Přispěvatelé: | VU University medical center, Faculteit der Geneeskunde |
| Rok vydání: | 1997 |
| Předmět: |
Surface Properties
Swine Lipid Bilayers Biophysics Phospholipid Phosphatidylserines Biochemistry Phospholipases A chemistry.chemical_compound Phospholipase A2 Structural Biology Annexin Phosphatidylcholine Genetics Animals Annexin A5 Molecular Biology Pancreas Phosphatidylethanolamine chemistry.chemical_classification biology Phosphatidylethanolamines Cell Biology Phosphatidylserine Kinetics Phospholipases A2 Membrane Enzyme chemistry biology.protein Phosphatidylcholines lipids (amino acids peptides and proteins) |
| Zdroj: | FEBS Letters, 402, 193-197. Wiley-Blackwell Speijer, H, Jans, S W S, Reutelingsperger, C P M, Hack, C E, van der Vusse, G J & Hermens, W T 1997, ' Partial converage of phospholipid model membranes with annexin V may competely inhibit their degradation by phospholipase A2 ', FEBS Letters, vol. 402, pp. 193-197 . https://doi.org/10.1016/S0014-5793(96)01527-X |
| ISSN: | 0014-5793 |
| Popis: | PhospholipaseA2 (PLA2)-mediated hydrolysis of membrane phospholipids was measured by ellipsometry, and the inhibition of this process by annexinV was studied. Planar membranes, consisting of phosphatidylcholine, phosphatidylethanolamine, and phosphatidylserine (PC/PE/PS; 54:33:13, on molar basis), were degraded by pancreatic PLA2, and the rate of hydrolysis was limited to about 0.7%/min. The influence of graded coverage of the membrane with annexinV was studied. The degree of PLA2 inhibition was nonlinearly related to the amount of membrane-bound annexinV, and binding of only 12% and 54% of full membrane coverage resulted in, respectively, 50% and 93% inhibition. These findings indicate that the inhibition of PLA2-mediated hydrolysis by annexinV cannot be simply explained by shielding of phospholipid substrates from the enzyme. Moreover, the present results leave room for a role of endogenous annexinV in regulating phospholipid turnover in the plasma membrane of parenchymal cells such as cardiomyocytes. |
| Databáze: | OpenAIRE |
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