We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Biogenesis of chemotactic molecules by the arachidonate lipoxygenase system of platelets.
- Authors
TURNER, STEPHEN R.; TAINER, JOHN A.; LYNN, WILLIAM S.
- Abstract
BLOOD platelets contain two aggregation-activated enzyme systems that oxygenate arachidonic acid. One system is a cyclo-oxygenase that converts arachidonic acid into the biologically active endoperoxide prostaglandin G2 (PGG2), a precursor of classical prostaglandins E2 (PGE2 and Fa2α (PGF2α), as well as several non-prostanoate hydroxy fatty acids1. The second aggregation-activated platelet enzyme is a lipoxygenase that transforms arachidonic acid into 12-L-hydroxy-5,8,10,14-eicosatetraenoic acid (HETE)2. Although HETE is produced in significant quantities by aggregated platelets, no biological function for this compound has been reported. We now have evidence that HETE is a potent mediator of neutrophil chemotaxis.
- Publication
Nature, 1975, Vol 257, Issue 5528, p680
- ISSN
0028-0836
- Publication type
Article
- DOI
10.1038/257680a0