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Dihydro-leukotriene B4 (a 5,12-dihydroxy-eicosatrienoic acid) has been shown to be the primary metabolite of leukotriene B4 (LTB4) in a variety of cells other than human polymorphonuclear leukocytes (PMNLs). In this report we show that dihydro-LTB4 is significantly less active than LTB4 in different biological assay systems, i.e. leukocyte chemotaxis, chemokinesis, aggregation, adhesion to endothelium and superoxide anion production. This suggests that primary reduction constitutes a second so far unknown deactivation pathway for LTB4.
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