Abstract
Stimulation of prostaglandin synthesis in transformed mouse fibroblasts by serum, thrombin, and bradykinin was blocked by actinomycin D and cycloheximide. These RNA and protein synthesis inhibitors did not affect prostaglandin synthetase in vitro or in vivo; nor did they affect the acylation of arachidonic acid into phospholipids. Serum-stimulated release of arachidonic acid and prostaglandins from [3H]arachidonic acid-labeled cells also was inhibited by actinomycin D and cycloheximide. RNA and protein synthesis appear to be required for expression of phospholipase activity; a prerequisite for prostaglandin synthesis by these cells.
Highlights
Stimulation of prostaglandin synthesis in transformed mouse fibroblasts by serum, thrombin, and bradykinin was blocked by actinomycin D and cycloheximide
MC5-5 cells, an established cell line of methylcholanthrenetransformed mouse fibroblasts, synthesize prostaglandins that are secreted into the culture medium [3]
The present studies show that stimulations of prostaglandin production by serum, bradykinin, and thrombin are blocked by actinomycin
Summary
Stimulation of prostaglandin synthesis in transformed mouse fibroblasts by serum, thrombin, and bradykinin was blocked by actinomycin D and cycloheximide These RNA and protein synthesis inhibitors did not affect prostaglandin synthetase in vitro or in duo; nor did they affect the acylation of arachidonic acid into phospholipids. When incubated in the presence of serum, bradykinin, or thrombin, or when mechanically manipulated or killed by an excess of hydroquinone, ultraviolet radiation, or antibody and complement, the cells are stimulated to produce increased levels of prostaglandins [3,4,5] These stimulations of prostaglandin biosynthesis result from increased deacylation of phospholipids [6]. The present studies show that stimulations of prostaglandin production by serum, bradykinin, and thrombin are blocked by actinomycin
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have