Premium
Modulation of phospholipase A 2 activity in human fibroblasts
Author(s) -
Solito Egle,
Parente Luca
Publication year - 1989
Publication title -
british journal of pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1111/j.1476-5381.1989.tb11865.x
Subject(s) - phospholipase a2 , arachidonic acid , medicine , prostaglandin e2 , endocrinology , bradykinin , phospholipase , stimulation , phospholipase a , chemistry , biology , biochemistry , enzyme , receptor
1 Human embryonic skin fibroblasts (HSF) incubated overnight with either human recombinant interleukin‐1α (rIL‐1α) or interleukin‐1β (rIL‐1β) released large amounts of prostaglandin E 2 (PGE 2 ). 2 rIL‐1β, bradykinin (Bk) and arachidonic acid (AA) significantly stimulated PGE 2 release from HSF incubated overnight in the presence of either interleukin. 3 Hydrocortisone inhibited the PGE 2 release induced by rIL‐1β and Bk, but not by AA. 4 The steroid inhibitory effect was reversed by actinomycin D as well as by an anti‐lipocortin monoclonal antibody. 5 The results suggest that in HSF, rIL‐1β is able to stimulate both cyclo‐oxygenase and phospholipase A 2 (PLA 2 ) activity. 6 The stimulation of PLA 2 activity by rIL‐1β is inhibited by hydrocortisone, probably via induction of lipocortin‐like proteins.