Abstract
Fatty acid composition of membrane phospholipids of cultured cardiomycotes can be modified by the type of polyunsaturated fatty acids (n−3 or n−6 PUFA) constituting the culture medium. In this study, we investigated the effect of fatty acid modification on the activities of the key enzymes involved in the deacylation-reacylation cycle of membrane phospholipids.
Results showed that cardiomyocytes grown in the presence of n−6 PUFA exhibited a higher specific alkaline phospholipase A (mainly A2) activity (+34%) and a moderately lower lysophospholipase activity(−17%) than when incubated with n−3 PUFA. AcylCoA:lysophosphatidylcholine acyltransferase, acid lysosomal phospholipase A1 and acylCoA synthetase activities were not significantly altered by changes in cellular PUFA composition. It was demonstrated that the differences between phospholipase A activities of the two types of cultured cells were linked neither to a differential leakage of enzyme nor to oxidative injury to the enzyme through blockage of essential sulfhydryl groups. One likely explanation is that the PUFA-induced changes in membrane composition alter membrane physical properties which, in turn, affect membrane-bound phospholipase A activity. Possible beneficial effects of the n−3 PUFA-induced changes on membrane stability are discussed.
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Abbreviations
- PUFA:
-
polyunsaturated fatty acids
- PC:
-
phosphatidylcholines
- PE:
-
phosphatidylethanolamines
- SM3:
-
n−3 PUFA-enriched synthetic media
- SM6:
-
n−6 PUFA-enriched synthetic media
- ACLAT:
-
acylCoA:lysophosphatidylcholine acyltransferase
- BME:
-
betamercaptoethanol
- PI:
-
phosphatidylinositol
- DPG:
-
diphosphatidylglycerol
- LPC:
-
lysophosphatidylcholine
- LPE:
-
lysophosphatidylethanolamine
- SPH:
-
sphingomyelin
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Nalbone, G., Grynberg, A., Chevalier, A. et al. Phospholipase a activity of cultured rat ventricular myocyte is affected by the nature of cellular polyunsaturated fatty acids. Lipids 25, 301–306 (1990). https://doi.org/10.1007/BF02544337
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DOI: https://doi.org/10.1007/BF02544337