Interleukin-1 beta induces cytosolic PLA2 in parallel with prostaglandin E2 in rheumatoid synovial fibroblasts.
We investigated the temporal relationship between the increase in enzymatic activity and protein of a high molecular weight (100 kDa), cytosolic PLA2 (cPLA2) in interleukin-1 beta (IL-1 beta)-treated rheumatoid synovial fibroblasts (RSF). Both of these responses increased according to a similar time-course which correlates with PGE2 production by these cells. In contrast, 14 kDa, secreted PLA2 (sPLA2), which was also produced by RSF, was not affected by IL-1 beta treatment. These findings support that an augmentation of CPLA2 activity, caused by an induction of cPLA2 protein, rather than sPLA2, is temporally associated with increased PGE2 production in IL-1 beta-treated RSF.
Hulkower
K I
KI
Department of Bronchopulmonary Research, Hoffmann-La Roche Inc., Nutley, NJ 07110.
Coffey
J W
JW
Levin
W
W
Anderson
C M
CM
Chen
T
T
Hope
W C
WC
Bolin
D R
DR
Morgan
D W
DW
D001172:Arthritis, Rheumatoid / Q000378:metabolism*; D002478:Cells, Cultured; D003600:Cytosol / Q000201:enzymology / Q000378:metabolism; D015232:Dinoprostone / Q000096:biosynthesis*; D004790:Enzyme Induction; D005347:Fibroblasts / Q000187:drug effects / Q000378:metabolism; D006801:Humans; D007375:Interleukin-1 / Q000494:pharmacology*; D008970:Molecular Weight; D010741:Phospholipases A / Q000096:biosynthesis*; D054467:Phospholipases A2; D013583:Synovial Membrane / Q000187:drug effects / Q000378:metabolism* / Q000473:pathology
D007375:Interleukin-1; D010741:Phospholipases A; D054467:Phospholipases A2; D015232:Dinoprostone