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Transcellular metabolism of arachidonic acid: increased platelet
thromboxane generation in the presence of activated polymorphonuclear
leukocytes
N Maugeri, V Evangelista, P Piccardoni, G Dell'Elba, A Celardo, G de Gaetano and C Cerletti
Giulio Bizzozero Laboratory of Platelet and Leukocyte Pharmacology,
Istituto di Richerche Farmacologiche Mario Negri, Consorzio Mario Negri
Sud, Santa Maria Imbaro, Italy.
Human polymorphonuclear leukocytes (PMN) activated by n-formyl-
methionyl-leucyl-phenylalanine (fMLP), in the presence of cytochalasin B,
are able to induce activation of coincubated autologous platelets "via"
cathepsin G released from the azurophilic granules. However, thromboxane
(Tx) B2 production in this system cannot be completely explained by
cathepsin G-stimulated platelet arachidonate metabolism. Indeed, the amount
of TxB2 found in supernatants of platelet/PMN suspensions challenged with 1
mumol/L fMLP was twofold to fourfold higher than that measured when
platelets were stimulated by supernatants from fMLP-activated PMN. In the
present report, we analyzed the possibility that PMN-induced TxB2
production in this system is the result of transcellular metabolism of
arachidonic acid (AA) between fMLP-activated PMN and cathepsin G-stimulated
platelets. 3H-AA-labeled PMN were used to test if a transfer of AA or
metabolite(s) occur from PMN to platelets. Our results showed that: (1)
3H-TxB2 and 3H-12-HHT are synthesized when 3H-AA-labeled PMN are activated
mixed to unlabeled platelets; (2) total radioactivity released by
fMLP-stimulated PMN is increased in the presence of platelets, whereas the
membrane content of unesterified 3H-AA is reduced; (3) platelet
cyclooxygenase inhibition completely prevents 3H- TxB2 synthesis; and (4)
inhibition of cathepsin G-induced platelet activation with the antiprotease
eglin C blocks the formation of 3H- TxB2. These data show that in the
experimental system used, platelets use PMN-derived unmetabolized AA to
synthesize TxB2.
Volume 80,
Issue 2,
pp. 447-451,
07/15/1992
Copyright © 1992 by The American Society of Hematology
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