Related Experiment Video
Updated: Oct 20, 2026

Separation of Rat Epidermis and Dermis with Thermolysin to Detect Site-Specific Inflammatory mRNA and Protein
Published on: September 29, 2021
Interleukin-1 stimulation of phospholipase activity in rat synovial fibroblasts. Possible regulation by
R W Godfrey1, W J Johnson, S T Hoffstein
1Department of Experimental Pathology, Smith Kline and French Laboratories, King of Prussia, PA 19406-0939.
Abstract:
Tritiated arachidonic acid (3H-AA)-labeled rat synovial fibroblasts stimulated with human recombinant interleukin-1 beta (rIL-1 beta) released incorporated radiolabel in a time-dependent and dose-dependent manner, with labeled prostaglandins representing 29% of the released radiolabel. Treatment of the cells with dibutyryl cAMP or prostaglandin E2 enhanced both spontaneous and rIL-1 beta-induced 3H-AA release; treatment with indomethacin or naproxen inhibited the response. The effects of these cyclooxygenase inhibitors on 3H-AA release were not reversed by the addition of prostaglandin E2. The activities of phospholipase A, phospholipase C, and diglyceride lipase were detected in the homogenates of rat synovial fibroblasts. Pretreatment of synovial cells with rIL-1 beta resulted in a threefold stimulation of phospholipase A activity and a slight increase in phospholipase C activity in cell homogenates. These data show that rIL-1 beta stimulates phospholipase activities in rat synovial fibroblasts and that at least one of these activities may be regulated by either prostaglandins or cAMP.
Related Concept Videos
The JAK-STAT Signaling Pathway
IP3/DAG Signaling Pathway
Acute Inflammation II: Cellular Phase

