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Regulation of the biosynthesis of acyl analogs of platelet‐activating factor by purinergic agonist in endothelial cells
Author(s) -
Balestrieri Maria Luisa,
Lee Ten-ching
Publication year - 2000
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/s0014-5793(00)01870-6
Subject(s) - platelet activating factor , chemistry , agonist , biochemistry , biosynthesis , purinergic receptor , microbiology and biotechnology , sphingosine , stereochemistry , biology , enzyme , receptor , endocrinology
We have previously shown that platelet‐activating factor (PAF)‐dependent transacetylase (TA) contains three catalytic activities, namely PAF: lysophospholipid TA (TA L ), PAF: sphingosine TA (TA S ) and PAF acetylhydrolase. It serves as a modifier of PAF actions by producing different lipid signal molecules. The TA L activity is involved in the biosynthesis of acyl analogs of PAF (acyl‐PAF, 1‐acyl‐2‐acetyl‐ sn ‐glycero‐3‐phosphocholine, acylacetyl‐GPC) in agonist‐stimulated endothelial cells. In the present investigation, we have studied the mechanism(s) by which the TA activity is regulated in ATP‐treated endothelial cells. We have demonstrated that ATP, and thiol‐modifying agents with ATP, specifically regulate only the TA L part of the TA activities.