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  • Title: Biosynthesis of paf-acether. XIV. Paf-acether output in murine peritoneal macrophages is regulated by the level of acetylhydrolase.
    Author: Palmantier R, Dulioust A, Maiza H, Benveniste J, Ninio E.
    Journal: Biochem Biophys Res Commun; 1989 Jul 14; 162(1):475-82. PubMed ID: 2751666.
    Abstract:
    Paf-acether (paf) synthesis was previously shown to be impaired in 24 hr-adherent and Bacillus Calmette-Guérin-activated murine peritoneal macrophages as compared to resident macrophages. We report here that the induction of acetylhydrolase was responsible for the decreased paf output in 24 hr-adherent macrophages. The kinetic analysis of the enzymes derived from 2 hr-, 24 hr- and BCG-activated adherent macrophages and from plasma revealed that the Km for paf was similar whatever the source of the acetylhydrolase whereas the Vmax was five-fold increased in 24 hr-cultured macrophages. The acetylhydrolase activity was Ca2+-independent and was not inhibited by addition of alkyl-acyl (long chain)-glycero-phosphocholine suggesting that the enzyme was not a phospholipase A2.
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