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Biogenesis of chemotactic molecules by the arachidonate lipoxygenase system of platelets

Nature volume 257, pages 680–681 (1975)Cite this article

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.

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Authors and Affiliations

  1. Department of Biochemistry, Duke University Medical Center, Durham, North Carolina, 27710

    STEPHEN R. TURNER, JOHN A. TAINER & WILLIAM S. LYNN

Authors
  1. STEPHEN R. TURNER
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  2. JOHN A. TAINER
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  3. WILLIAM S. LYNN
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TURNER, S., TAINER, J. & LYNN, W. Biogenesis of chemotactic molecules by the arachidonate lipoxygenase system of platelets. Nature 257, 680–681 (1975). https://doi.org/10.1038/257680a0

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