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Acylation of 1-palmitoyl-sn-glycerophosphocholine by chick brain microsomes is unaffected by fatty acid binding protein

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Abstract

Rates of incorporation of exogenously supplied fatty acids into 1-palmitoyl-sn-glycerophosphocholine were measured using the microsomal fraction from brains of 14–15 day old chick embryos. The substrate preferences for reacylation were: 18: 2(n − 6) = 20: 4(n − 6) ≥ 20: 5(n − 3) = 18: 3(n − 3) ≥ 18 : 1(n − 9) ≥ 22: 6(n − 3) ≥ 18: 0. The normalized rate with 18: 0 was significantly lower than all other rates except for 22: 6(n − 3), and the acylation rate with 22: 6(n − 3) was significantly lower than with 18: 2(n − 6) and 20: 5(n − 3). With the addition of fatty acid binding protein partially purified from brain cytosol, a decrease (not significant) in the rate of incorporation was observed; the substrate preference was unchanged. In the presence of FABP, normalized rates with 18: 2(n − 6) were significantly higher than with 18: 0, 18: 1(n − 9), or 22: 6(n − 3); rates with 20: 4(n - 6) were significantly higher than those with 22: 6(n − 3). Preliminary data on the acylation of 1-palmitoyl-sn-glycerophosphoethanolamine showed lower rates of incorporation than for the choline analogue and no clear substrate preference, but a similar lack of effect of fatty acid binding protein. These results do not support the proposed function of fatty acid binding protein in the establishment of a phospholipid composition rich in polyunsaturated fatty acids. The results are consistent, however, with the role of the reacylation reaction in the continual turnover of particular substrates [18: 2(n − 6) and 20: 4(n − 6)] used to generate second messengers.

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Abbreviations

GPC:

Glycerophosphocholine

GPE:

Glycerophosphoethanolamine

LPC:

1-palmitoyl-sn-glycerophosphocholine

LPE:

1-palmitoyl-sn-glycerophosphoethanolamine

PUFA:

Polyunsaturated Fatty Acids

FABP:

Fatty Acid Binding Protein

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Sellner, P.A., Phillips, A.R. Acylation of 1-palmitoyl-sn-glycerophosphocholine by chick brain microsomes is unaffected by fatty acid binding protein. Mol Cell Biochem 117, 119–125 (1992). https://doi.org/10.1007/BF00230750

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  • DOI: https://doi.org/10.1007/BF00230750

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