Stimulation of fibroblast proliferation and prostaglandin production by purified recombinant murine interleukin 1.
Recombinant murine interleukin 1 (IL-1) obtained from a clone of Escherichia coli containing an IL-1 expression plasmid was purified to homogeneity using a sequential extraction procedure and gel filtration chromatography. The purified recombinant IL-1 exhibited a pI of approximately 5.2 and a sp act of 6 X 10(6) units/mg. These values are in agreement with those obtained with natural murine IL-1. The purified recombinant IL-1 enhanced the proliferation of human HEL and WI-38 fibroblasts in a serum-free medium. In addition, IL-1 stimulated fibroblast PGE2 5- to 30-fold over a 24-hr period. The effects of IL-1 on fibroblast activation were obtained with the same concentrations of IL-1 that are effective in the mouse thymocyte assay. These results unequivocally establish the ability of IL-1 to modulate fibroblast proliferation and function.
D000818:Animals; D002455:Cell Division / Q000187:drug effects; D015232:Dinoprostone; D004305:Dose-Response Relationship, Drug; D005347:Fibroblasts / Q000187:drug effects / Q000378:metabolism; D006801:Humans; D007375:Interleukin-1 / Q000302:isolation & purification / Q000502:physiology*; D051379:Mice; D008970:Molecular Weight; D011458:Prostaglandins E / Q000096:biosynthesis*; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000494:pharmacology*
D007375:Interleukin-1; D011458:Prostaglandins E; D011994:Recombinant Proteins; D015232:Dinoprostone