Premium
Functional crosstalk between phospholipase D 2 and signaling phospholipase A 2 /cyclooxygenase‐2‐mediated prostaglandin biosynthetic pathways
Author(s) -
Ueno Noriko,
Murakami Makoto,
Kudo Ichiro
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01691-4
Subject(s) - phospholipase d , crosstalk , phospholipase , cyclooxygenase , lipid signaling , phospholipase a2 , enzyme , phospholipase a , cytosol , signal transduction , prostaglandin , chemistry , microbiology and biotechnology , prostaglandin e , enzyme activator , eicosanoid , biochemistry , arachidonic acid , biology , physics , optics
We performed reconstitution analyses of functional interaction between phospholipase A 2 (PLA 2 ) and phospholipase D (PLD) enzymes. Cotransfection of HEK293 cells with cytosolic (cPLA 2 ) or type IIA secretory (sPLA 2 ‐IIA) PLA 2 and PLD 2 , but not PLD 1 , led to marked augmentation of stimulus‐induced arachidonate release. Interleukin‐1‐stimulated arachidonate release was accompanied by prostaglandin E 2 production via cyclooxygenase‐2, the expression of which was augmented by PLD 2 . Conversely, activation of PLD 2 , not PLD 1 , was facilitated by cPLA 2 or sPLA 2 ‐IIA. Thus, our results revealed functional crosstalk between signaling PLA 2 s and PLD 2 in the regulation of various cellular responses in which these enzymes have been implicated.