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Acylation of Rat Brain Myelin Proteolipid Protein with Different Fatty Acids
Author(s) -
Bizzozero Oscar A.,
McGarry James F.,
Lees Marjorie B.
Publication year - 1986
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.1471-4159.1986.tb00678.x
Subject(s) - myristic acid , palmitic acid , acylation , oleic acid , chemistry , biochemistry , fatty acid , phospholipid , organic chemistry , chromatography , membrane , catalysis
The acylation of rat brain proteolipid protein (PLP) with tritiated palmitic, oleic, and myristic acids was studied in vivo and in vitro and compared with the acylation of lipids. Twenty‐four hours after intracranial injection of [ 3 H]myristic acid, only 16% of the PLP‐bound label appeared as myristic acid, with 66% as palmitic, 9% as stearic, and 6% as oleic acid, whereas >63% of the label in total or myelin phospholipid was in the form of myristic acid. In contrast, after labelling with [ 3 H]palmitic or oleic acids, 75% and 86%, respectively, of the radioactivity in PLP remained in the original form. When brain tissue slices were incubated for short periods of time, the incorporation of palmitic and oleic acids into PLP exceeded that of myristic acid by a factor of 8. In both systems and with all precursors studied, the label associated with PLP was shown to be in ester linkage. The results suggest a preferential acylation of PLP with palmitic and oleic acids as compared with myristic acid. This is consistent with the fatty acid composition of the isolated PLP.