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The mediating role of cPLA 2 in IL‐1 β and IL‐6 release in LPS‐induced HeLa cells
Author(s) -
Wang X. H.,
Yan G. T.,
Wang L. H.,
Hao X. H.,
Zhang K.,
Xue H.
Publication year - 2003
Publication title -
cell biochemistry and function
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.933
H-Index - 61
eISSN - 1099-0844
pISSN - 0263-6484
DOI - 10.1002/cbf.1052
Subject(s) - hela , transfection , lipopolysaccharide , phospholipase a2 , phospholipase a , microbiology and biotechnology , interleukin , cell , biology , chemistry , cell culture , immunology , biochemistry , cytokine , enzyme , genetics
Studies were conducted to characterize a HeLa cell model by which the roles of the 85‐kDa phospholipase A 2 (cPLA 2 ) in interleukin‐1 β (IL‐1 β) and interleukin‐6 (IL‐6) release could be evaluated. At first, untreated HeLa cells were compared with lipopolysaccharide (LPS)‐treated HeLa cells. The latter resulted in cPLA 2 overexpression and an increased trend of IL‐1 β and IL‐6 release. The indicated doses of 85‐kDa cPLA 2 antisense oligonucleotide directed against the initiation site were then used to block cPLA 2 in LPS‐induced HeLa cells. The process led to a dose‐dependent decrease in cPLA 2 protein with no noticeable change of cPLA 2 mRNA. Compared with that of LPS added only, a reduction of IL‐1 β and IL‐6 levels in the supernatants of transfected cells following the repression of cPLA 2 was observed. These results suggested that 85‐kDa cPLA 2 may mediate the signalling cascades by which IL‐1 β and IL‐6 were released in LPS‐induced HeLa cells. Copyright © 2003 John Wiley & Sons, Ltd.