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The molecular selectivity of phospholipase D in HL60 granulocytes
Author(s) -
Heung Yen Ming M.,
Postle Anthony D.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00399-t
Subject(s) - selectivity , phospholipase d , phosphatidylcholine , phospholipid , chemistry , biochemistry , phospholipase , butanol , enzyme , membrane , ethanol , catalysis
The molecular selectivity of PLD in PMA‐stimulated HL60 granulocytes was determined by HPLC analysis of [ 3 H]butanol incorporation into phosphatidyl[ 3 H]butanol (Ptd[ 3 H]But) molecular species. Comparison with phospholipid compositions confirmed that PLD acted primarily on phosphatidylcholine (PtdCho). Apparent enzyme selectivity was suggested by negligible formation of PB16:0/16:0 and preferential synthesis of Ptd[ 3 H]But species containing sn ‐1 18:0. Culture with exogenous 18:2n−6 or 20:4n−6 readily modified both PtdCho and Ptd[ 3 H]But compositions, and accentuated the apparent selectivity of stimulated PLD for sn ‐1 18:0 species of PtdCho. Such modifications to PLD‐based signalling mechanisms may contribute to the modulatory effects of altered dietary lipid intakes on cellular functions.