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Serum Albumin Washing Specifically Enhances Arachidonate Incorporation into Synaptosomal Phosphatidylinositols
Author(s) -
Strosznajder Joanna,
Foudin Laurie,
Tang Wilson,
Sun Grace Y.
Publication year - 1983
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1983.tb12656.x
Subject(s) - synaptosome , bovine serum albumin , chemistry , biochemistry , arachidonic acid , phosphatidylinositol , albumin , phosphatidylcholine , polyunsaturated fatty acid , serum albumin , acyltransferase , acyltransferases , fatty acid , membrane , phospholipid , chromatography , enzyme , biosynthesis , kinase
Arachidonate incorporation into synaptosomal phospholipids was shown to be affected by factors including the procedure for preparation of the membrane fractions and preincubation of synaptosomes prior to assay of incorporation activity. Preincubation of synaptosomes gave rise to a decrease in incorporation of arachidonate into both phosphatidylcholine (PC) and phosphatidylinositol (PI). However, the inhibition toward incorporation into PIs, but not PCs, was fully reversed when the membranes were washed with bovine serum albumin. A twofold increase in arachidonate incorporation into PIs was also observed when freshly prepared synaptosomes were washed with serum albumin immediately before assay of incorporation activity. The inhibitory action is thought to be due to an increase in polyunsaturated fatty acids and/or their oxidation products which may then elicit a special effect on the acyltransferase responsible for transferring arachidonate into phosphatidylinositols. The differences in fatty acid uptake and response to serum albumin also suggest the presence of different acyltransferases for acyl transfer to PIs and PCs.