The molecular selectivity of PLD in PMA-stimulated HL60 granulocytes w
as determined by HPLC analysis of [H-3]butanol incorporation into phos
phatidyl[3H]butanol (Ptd[H-3]But) molecular species. Comparison with p
hospholipid compositions confirmed that PLD acted primarily on phospha
tidylcholine (PtdCho). Apparent enzyme selectivity was suggested by ne
gligible formation of PB16:0/16:0 and preferential synthesis of Ptd[H-
3]But species containing sn-1 18:0, Culture with exogenous 18:2n-6 or
20:4n-6 readily modified both PtdCho and Ptd[H-3]But compositions, and
accentuated the apparent selectivity of stimulated PLD for sn-1 18:0
species of PtdCho. Such modifications to PLD-based signalling mechanis
ms may contribute to the modulatory effects of altered dietary lipid i
ntakes on cellular functions.