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Activity and subcellular distribution of phospholipase A1 from neuronal cell-enriched fractions of the rabbit cerebral cortex

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Abstract

Glycerophosphatides, specifically labeled either in the 1 or in the 2 position, were used to measure the activity of neuronal phospholipase A1 and to investigate the subcellular distribution of the enzyme. The microsomes were found to possess the highest phospholipase activity, with a threefold increase as compared to the cell homogenate. A considerable enzymatic activity could still be observed in the plasma membranes isolated from the neuronal-enriched cell fraction. Microsomal phospholipase possessed the highest activity with phosphatidylcholine, whereas phosphatidylserine was cleaved at a much lower rate. The rate of release of labeled fatty acids from the substrates by the microsomal phospholipase decreased with increasing degree of unsaturation of the fatty acids at the 1 position. The presence of plasmalogens and of alkylacyl analogues in the incubation mixture caused an appreciable inhibition of the hydrolysis of the diacyl glycerophosphatides.

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Woelk, H., Porcellati, G. & Gaiti, A. Activity and subcellular distribution of phospholipase A1 from neuronal cell-enriched fractions of the rabbit cerebral cortex. Neurochem Res 4, 535–543 (1979). https://doi.org/10.1007/BF00964647

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