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A Lysophospholipase D Pathway in the Metabolism of Ether-linked Lipids in Brain Microsomes

From the ¹ From the Medical Division, Oak Ridge Associated Universities, Oak Ridge, Tennessee 37830

Microsomal preparations from rat brain in the presence of Mg²⁺ hydrolyzed the ethanolamine, choline, and phosphate moieties from 1-[1-¹⁴C]hexadecyl-sn-glycero-3-phosphorylethanolamine, 1-[1-¹⁴C]hexadec-1-enyl-sn-glycero-3-phosphorylethanolamine, and 1-[1-¹⁴C]hexadecyl-sn-glycero-3-phosphorylcholine. Studies of the hydrolysis of 1-[1-¹⁴C]-hexadecyl-sn-glycero-3-phosphorylethanolamine in this system indicated that the ethanolamine moiety was first removed by a phosphodiesterase to form 1-[1-¹⁴C]hexadecylglycero-3-phosphate which was then dephosphorylated to form 1-[1-¹⁴C]hexadecylglycerol. Only minimal hydrolysis occurred when the 2-positions of the substrates were acylated; otherwise the phosphodiesterase activity was similar to that of phospholipase D from plants. The occurrence of such a lysophospholipase D pathway has not been previously reported. When Ca²⁺ (5 mm) was added to the system instead of Mg²⁺ (5 mm), little, if any, stimulation occurred; higher concentrations of Ca²⁺ (25 mm) inhibited the reaction. Therefore, this reaction does not appear to be related to the Ca²⁺-stimulated base exchange reaction found in the brain by others.

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