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Regulation of the biosynthesis of platelet‐activating factor in alveolar macrophages
Author(s) -
Sugiura Takayuki,
OjimaUchiyama Ayako,
Masuzawa Yasuo,
Fujita Masamichi,
Nakagawa Yasuhito,
Waku Keizo
Publication year - 1991
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02536487
Subject(s) - acetyltransferase , platelet activating factor , intracellular , biosynthesis , biochemistry , enzyme , chemistry , lysis , clinical chemistry , alveolar macrophage , macrophage , microbiology and biotechnology , biology , in vitro , acetylation , endocrinology , gene
Activities of enzymes which metabolize lysoplatelet‐activating factor (lysoPAF) and platelet‐activating factor (PAF) were studied in rabbit alveolar macrophage lysates. Substantial acetyltransferase activity was noted in the presence of 100 μM acetyl‐coenzyme A (CoA), and this activity was increased in A23187‐stimulated cell lysate. On the other hand, in the absence of exogenous acetyl‐CoA, lysoPAF was mainly acylated through a transacylation pathway rather than by acetyltransferase in both control and A23187‐stimulated cell lysates. We confirmed that the intracellular concentration of acetyl‐CoA is relatively low. The observations suggest that the transacylation system may play an equally important role in the regulation of the availability of lysoPAF in intact cells. Intracellular lysoPAF was also maintained at relatively low levels. Interestingly, large amounts of PAF were produced even in unstimulated cells upon addition of an excess of exogenous lysoPAF, suggesting that generation of an adequate amount of lysoPAF within cells may be sufficient to trigger PAF synthesis in this type of cells.