C. Dentan et al., PEFABLOC, 4-[2-AMINOETHYL]BENZENESULFONYL FLUORIDE, IS A NEW, POTENT NONTOXIC AND IRREVERSIBLE INHIBITOR OF PAF-DEGRADING ACETYLHYDROLASE, Biochimica et biophysica acta, L. Lipids and lipid metabolism, 1299(3), 1996, pp. 353-357
We report here that 4-[2-aminoethyl]benzenesulfonyl fluoride (Pefabloc
SC, Pefabloc), a new irreversible serine proteinase inhibitor, effici
ently inhibits both human and rat platelet activating factor (PAF)-deg
rading acetylhydrolase (acetylhydrolase). Indeed, low concentrations o
f Pefabloc (0.1 mM) rapidly and totally inactivate both human plasma-,
VLDL-, IDL-, LDL- and HDL-associated acetylhydrolase, and in addition
, acetylhydrolase synthesized and released by human adherent monocytes
in culture, as well as rat brain cytosolic acetylhydrolase. By contra
st, Pefabloc only minimally inhibited the phospholipase A(2) (PLA(2))
activity from Naja naja and from porcine pancreas. In addition, Pefabl
oc is relatively nontoxic, stable and convenient to use. Henceforth, P
efabloc may replace both DFP and PMSF and therefore constitutes a usef
ul and valuable tool in future studies of acetylhydrolase.