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Phospholipase A 2 and Arachidonic Acid: a Common Link in the Generation of the Eosinophil Chemotactic Factor (ECF) from Human PMN by Various Stimuli
Author(s) -
TESCH H.,
KÖNIG W.
Publication year - 1980
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1980.tb00007.x
Subject(s) - phospholipase a2 , arachidonic acid , zymosan , biochemistry , phospholipase , chemotaxis , eosinophil , cytosol , chemistry , biology , granulocyte , phospholipase a , calcium , phospholipid , ionophore , enzyme , immunology , in vitro , receptor , organic chemistry , membrane , asthma
An eosinophil chemotactic factor (ECF) of low molecular weight can be generated and released from human polymorphonuclear neutrophils by the calcium ionophore, phagocytosis of zymosan particles, arachidonic acid, and phospholipase A 2 . Since the activation of cells by the ionophore and during the phagocytic event leads to phospholipid turnover, with the subsequent generation of arachidonic acid, it is reasonable that phospholipase A 2 represents the common link for ECF production. The kinetics of ECF release by phospholipase A 2 is similar to the pattern observed with the various stimuli. After a rapid rise in activity a decline occurred at later times of secretion, suggesting a mechanism of inactivation. During subcellular fractionation of cells an ECF‐generating component was enriched in the 200,000 g supernatant fraction, which represents the cytosol. Addition of arachidonic acid or phospholipase A 2 induced ECF generation. On gel filtration analysis the ECF‐generating component revealed a molecular weight of about 80,000 daltons. It is suggested that this component represents a lipoxygenase.