Protease-activated receptor signaling in platelets activates cytosolic phospholipase A2α differently for cyclooxygenase-1 and 12-lipoxygenase catalysis.
AUTHORS
Holinstat
M ,
Boutaud
O ,
Apopa
PL ,
Vesci
J ,
Bala
M ,
Oates
JA ,
Hamm
HE ,
. Arteriosclerosis, thrombosis, and vascular biology. 2011 2 ; 31(2). 435-42
- PMID: 21127289[PubMed].
ABSTRACT
The rate-limiting step in the biosynthesis of thromboxane A(2) (TxA(2)) and 12-hydroxyeicosatetraenoic acid (12-HETE) by platelets is activation of cytosolic phospholipase A(2α) (cPLA(2α)), which releases arachidonic acid, which is the substrate for cyclooxygenase-1 (COX-1) and 12-lipoxygenase. We evaluated signaling via the human platelet thrombin receptors, protease-activated receptor (PAR) 1 and PAR4, to the activation of cPLA(2α), which provides a substrate for the biosynthesis of TxA(2) and 12-HETE.