Literature DB >> 3257870

Interleukin-1 activates phospholipase A2 in human synovial cells.

S C Gilman1, J Chang, P R Zeigler, J Uhl, E Mochan.   

Abstract

Interleukin-1 (IL-1) treatment of synovial cells from rheumatoid arthritis and osteoarthritis patients resulted in a dose-dependent secretion of phospholipase A2 (PLA2). IL-1 also stimulated prostaglandin E2 and plasminogen activator synthesis, in parallel with PLA2 activation; all 3 were detectable within 6 hours of IL-1 treatment and peaked by 24 hours. Synovial cell PLA2 required calcium (5 mM) and a neutral pH (7.5) for maximal activity and appears similar to the PLA2 in synovial fluid, which has been described previously. We conclude that PLA2 can be induced by IL-1, and its secretion may contribute significantly to the inflammatory actions of IL-1.

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Year:  1988        PMID: 3257870     DOI: 10.1002/art.1780310118

Source DB:  PubMed          Journal:  Arthritis Rheum        ISSN: 0004-3591


  16 in total

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8.  Increased expression of human type IIa secretory phospholipase A2 antigen in arthritic synovium.

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10.  Ganoderma lucidum polysaccharide peptide reduced the production of proinflammatory cytokines in activated rheumatoid synovial fibroblast.

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