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Krug, H.F. ; Berndt, J.

Stimulation of arachidonic acid metabolism via phospholipase A2 by triethyl lead.

FEBS J. 162, 293-298 (1987)
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Human blood platelet aggregation and the formation of icosanoids were studied in response to triethyl lead chloride (Et3PbCl). Concentrations higher than 75 μM stimulate platelets to aggregate, whereas low concentrations (≦ 20 μM) caused platelet hypersensitivity to aggregating agents such as collagen or arachidonic acid. Incubation of suspensions of washed platelets with Et3PbCl resulted in a stimulated liberation and subsequent metabolism of arachidonic acid. This response was dependent on the concentration of Et3PbCl and the incubation time. Using low concentrations of Et3PbCl and up to 3 h of incubation, the lipoxygenase product 12-hydroxy-5,8,10,14-icosatetraenoic acid was the major metabolite. Under normal conditions, however, stimulation of platelets with collagen, thrombin, or arachidonic acid leads to higher amounts of the cyclooxygenase products 12-hydroxy-5,8,10-heptadecatrienoic acid and thromboxane B2.The aggregation of human platelets induced by Et3PbCl was inhibited by three different drugs: acetylsalicylic acid, forskolin and quinacrine; but only quinacrine could prevent the liberation of arachidonic acid and the appearance of its metabolites. These specific effects of the inhibitors on Et3PbCl-stimulated platelets as well as the differences in the pattern of arachidonic acid metabolites and phosphatidic acid suggest a direct stimulatory action of Et3PbCl on platelet phospholipase A2.  
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Sprache
Veröffentlichungsjahr 1987
HGF-Berichtsjahr 1987
ISSN (print) / ISBN 1742-464X
e-ISSN 1742-4658
Zeitschrift FEBS Journal, The
Quellenangaben Band: 162, Heft: 2, Seiten: 293-298 Artikelnummer: , Supplement: ,
Verlag Wiley
Begutachtungsstatus Peer reviewed
Institut(e) Institut für Toxikologie und Biochemie
DOI 10.1111/j.1432-1033.1987.tb10599.x
Scopus ID 0023144710
PubMed ID 3100296
Erfassungsdatum 1987-12-31
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